SCN5A
entrez
6331
canonical
uniprot
Q14524
canonical
ensembl
ENSG00000183873
resolver
ensp
ENSP00000328968
resolver
ensp
ENSP00000398266
resolver
ensp
ENSP00000398962
resolver
ensp
ENSP00000399524
resolver
ensp
ENSP00000403355
resolver
ensp
ENSP00000410257
resolver
ensp
ENSP00000767026
resolver
enst
ENST00000413689
resolver
enst
ENST00000414099
resolver
enst
ENST00000450102
resolver
enst
ENST00000455624
resolver
genesymbol
SCN5A
resolver
hgnc
HGNC:10593
resolver
uniprot
A5H1P8
resolver
uniprot
A6N922
resolver
uniprot
A6N923
resolver
uniprot
B2RTU0
resolver
uniprot
E7ET19
resolver
uniprot
E9PEF3
resolver
uniprot
E9PEK2
resolver
uniprot
E9PFW7
resolver
uniprot
E9PG18
resolver
uniprot
E9PHB6
resolver
uniprot
H9KVD2
resolver
uniprot
K4DIA1
resolver
uniprot
Q59H93
resolver
uniprot
Q75RX9
resolver
uniprot
Q75RY0
resolver
uniprot
Q86UR3
resolver
uniprot
Q86V90
resolver
uniprot
Q8IZC9
resolver
uniprot
Q96J69
resolver
uniprot_entry
E9PG18_HUMAN
resolver
uniprot_entry
E9PHB6_HUMAN
resolver
uniprot_entry
H9KVD2_HUMAN
resolver
uniprot_entry
K4DIA1_HUMAN
resolver
uniprot_entry
Q86V90_HUMAN
resolver
uniprot_entry
SCN5A_HUMAN
resolver
uniprot_sec
A5H1P8
resolver
uniprot_sec
A6N922
resolver
uniprot_sec
A6N923
resolver
uniprot_sec
B2RTU0
resolver
uniprot_sec
E7ET19
resolver
uniprot_sec
E9PEF3
resolver
uniprot_sec
E9PEK2
resolver
uniprot_sec
E9PFW7
resolver
uniprot_sec
Q59H93
resolver
uniprot_sec
Q75RX9
resolver
uniprot_sec
Q75RY0
resolver
uniprot_sec
Q86UR3
resolver
uniprot_sec
Q8IZC9
resolver
uniprot_sec
Q96J69
resolver
activity_regulation
ACTIVITY REGULATION: Channel inactivation is regulated by intracellular calcium levels (PubMed:19074138). It is a tetrodotoxin-resistant voltage-gated Na(+) channel (Nav) (PubMed:1309946, PubMed:40768348). {ECO:0000269|PubMed:1309946, ECO:0000269|PubMed:19074138, ECO:0000269|PubMed:40768348}.
uniprot
proteins
amino_acid_sequence
MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSTTLQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPQELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPIRRAAVKILVHSLFNMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIIMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTALNGTNGSVEADGLVWESLDLYLSDPENYLLKNGTSDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVNSHERRSKRRKRMSSGTEECGEDRLPKSDSEDGPRAMNHLSLTRGLSRTSMKPRSSRGSIFTFRRRDLGSEADFADDENSTAGESESHHTSLLVPWPLRRTSAQGQPSPGTSAPGHALHGKKNSTVDCNGVVSLLGAGDPEATSPGSHLLRPVMLEHPPDTTTPSEEPGGPQMLTSQAPCVDGFEEPGARQRALSAVSVLTSALEELEESRHKCPPCWNRLAQRYLIWECCPLWMSIKQGVKLVVMDPFTDLTITMCIVLNTLFMALEHYNMTSEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSRMSNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRDSDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDREMNNLQLALARIQRGLRFVKRTTWDFCCGLLRQRPQKPAALAAQGQLPSCIATPYSPPPPETEKVPPTRKETRFEEGEQPGQGTPGDPEPVCVPIAVAESDTDDQEEDEENSLGTEEESSKQQESQPVSGGPEAPPDSRTWSQVSATASSEAEASASQADWRQQWKAEPQAPGCGETPEDSCSEGSTADMTNTAELLEQIPDLGQDVKDPEDCFTEGCVRRCPCCAVDTTQAPGKVWWRLRKTCYHIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSQCESLNLTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEYNLYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKINILAKINLLFVAIFTGECIVKLAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPTLPNSNGSRGDCGSPAVGILFFTTYIIISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYSVLSDFADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSAMVIQRAFRRHLLQRSLKHASFLFRQQAGSGLSEEDAPEREGLIAYVMSENFSRPLGPPSSSSISSTSFPPSYDSVTRATSDNLQVRGSDYSHSEDLADFPPSPDRDRESIV
uniprot
proteins
disease_involvement
DISEASE: Progressive familial heart block 1A (PFHB1A) [MIM:113900]: A cardiac bundle branch disorder characterized by progressive alteration of cardiac conduction through the His-Purkinje system, with a pattern of a right bundle-branch block and/or left anterior hemiblock occurring individually or together. It leads to complete atrio-ventricular block causing syncope and sudden death. {ECO:0000269|PubMed:11234013, ECO:0000269|PubMed:11804990, ECO:0000269|PubMed:12569159, ECO:0000269|PubMed:12574143, ECO:0000269|PubMed:19251209, ECO:0000269|PubMed:23420830}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Long QT syndrome 3 (LQT3) [MIM:603830]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:10377081, ECO:0000269|PubMed:10508990, ECO:0000269|PubMed:10590249, ECO:0000269|PubMed:10627139, ECO:0000269|PubMed:10911008, ECO:0000269|PubMed:10973849, ECO:0000269|PubMed:11304498, ECO:0000269|PubMed:11410597, ECO:0000269|PubMed:11535573, ECO:0000269|PubMed:11710892, ECO:0000269|PubMed:11889015, ECO:0000269|PubMed:11997281, ECO:0000269|PubMed:12209021, ECO:0000269|PubMed:12454206, ECO:0000269|PubMed:12673799, ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:16414944, ECO:0000269|PubMed:16922724, ECO:0000269|PubMed:18060054, ECO:0000269|PubMed:18378609, ECO:0000269|PubMed:18451998, ECO:0000269|PubMed:18708744, ECO:0000269|PubMed:18848812, ECO:0000269|PubMed:18929331, ECO:0000269|PubMed:19027780, ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:26392562, ECO:0000269|PubMed:7651517, ECO:0000269|PubMed:7889574, ECO:0000269|PubMed:8541846, ECO:0000269|PubMed:9506831, ECO:0000269|PubMed:9686753, ECO:0000269|Ref.39}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Brugada syndrome 1 (BRGDA1) [MIM:601144]: A tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs, the individual will faint and may die in a few minutes if the heart is not reset. {ECO:0000269|PubMed:10532948, ECO:0000269|PubMed:10618304, ECO:0000269|PubMed:10690282, ECO:0000269|PubMed:11410597, ECO:0000269|PubMed:11748104, ECO:0000269|PubMed:11823453, ECO:0000269|PubMed:11901046, ECO:0000269|PubMed:12051963, ECO:0000269|PubMed:12106943, ECO:0000269|PubMed:15023552, ECO:0000269|PubMed:15338453, ECO:0000269|PubMed:15579534, ECO:0000269|PubMed:15851320, ECO:0000269|PubMed:16266370, ECO:0000269|PubMed:16325048, ECO:0000269|PubMed:16616735, ECO:0000269|PubMed:17075016, ECO:0000269|PubMed:17081365, ECO:0000269|PubMed:17198989, ECO:0000269|PubMed:18252757, ECO:0000269|PubMed:18341814, ECO:0000269|PubMed:18451998, ECO:0000269|PubMed:18456723, ECO:0000269|PubMed:18616619, ECO:0000269|PubMed:19027780, ECO:0000269|PubMed:19251209, ECO:0000269|PubMed:19272188, ECO:0000269|PubMed:20129283, ECO:0000269|PubMed:23085483, ECO:0000269|PubMed:23420830, ECO:0000269|PubMed:24167619, ECO:0000269|PubMed:26279430, ECO:0000269|PubMed:26776555, ECO:0000269|PubMed:32850980, ECO:0000269|PubMed:9521325}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Sick sinus syndrome 1 (SSS1) [MIM:608567]: The term 'sick sinus syndrome' encompasses a variety of conditions caused by sinus node dysfunction. The most common clinical manifestations are syncope, presyncope, dizziness, and fatigue. Electrocardiogram typically shows sinus bradycardia, sinus arrest, and/or sinoatrial block. Episodes of atrial tachycardias coexisting with sinus bradycardia ('tachycardia-bradycardia syndrome') are also common in this disorder. SSS occurs most often in the elderly associated with underlying heart disease or previous cardiac surgery, but can also occur in the fetus, infant, or child without heart disease or other contributing factors. SSS1 onset is in utero, infancy, or early childhood. {ECO:0000269|PubMed:11748104, ECO:0000269|PubMed:14523039, ECO:0000269|PubMed:22795782}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Familial paroxysmal ventricular fibrillation 1 (VF1) [MIM:603829]: A cardiac arrhythmia marked by fibrillary contractions of the ventricular muscle due to rapid repetitive excitation of myocardial fibers without coordinated contraction of the ventricle and by absence of atrial activity. {ECO:0000269|PubMed:10940383}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Sudden infant death syndrome (SIDS) [MIM:272120]: SIDS is the sudden death of an infant younger than 1 year that remains unexplained after a thorough case investigation, including performance of a complete autopsy, examination of the death scene, and review of clinical history. Pathophysiologic mechanisms for SIDS may include respiratory dysfunction, cardiac dysrhythmias, cardiorespiratory instability, and inborn errors of metabolism, but definitive pathogenic mechanisms precipitating an infant sudden death remain elusive. {ECO:0000269|PubMed:18596570, ECO:0000269|PubMed:19302788}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Atrial standstill 1 (ATRST1) [MIM:108770]: A rare arrhythmia characterized by the absence of electrical and mechanical activity in the atria. Electrocardiographically, it is characterized by bradycardia, the absence of P waves, and a junctional narrow complex escape rhythm. {ECO:0000269|PubMed:12522116, ECO:0000269|PubMed:23420830}. Note=The disease may be caused by variants affecting distinct genetic loci, including the gene represented in this entry. A mutation in SCN5A has been detected in combination with a rare GJA5 genotype in a large family with atrial standstill.; DISEASE: Cardiomyopathy, dilated, 1E (CMD1E) [MIM:601154]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:15466643, ECO:0000269|PubMed:23420830}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Atrial fibrillation, familial, 10 (ATFB10) [MIM:614022]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:18088563, ECO:0000269|PubMed:18378609}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Pore-forming subunit of Nav1.5, a voltage-gated sodium (Nav) channel that directly mediates the depolarizing phase of action potentials in excitable membranes (PubMed:33712541, PubMed:40768348). Navs, also called VGSCs (voltage-gated sodium channels) or VDSCs (voltage-dependent sodium channels), operate by switching between closed and open conformations depending on the voltage difference across the membrane. In the open conformation they allow Na(+) ions to selectively pass through the pore, along their electrochemical gradient (PubMed:33712541, PubMed:40768348). The influx of Na(+) ions provokes membrane depolarization, initiating the propagation of electrical signals throughout cells and tissues (PubMed:1309946, PubMed:21447824, PubMed:23085483, PubMed:23420830, PubMed:25370050, PubMed:26279430, PubMed:26392562, PubMed:26776555). Nav1.5 is the predominant sodium channel expressed in myocardial cells and it is responsible for the initial upstroke of the action potential in cardiac myocytes, thereby initiating the heartbeat (PubMed:11234013, PubMed:11804990, PubMed:12569159, PubMed:1309946). Required for normal electrical conduction including formation of the infranodal ventricular conduction system and normal action potential configuration, as a result of its interaction with XIRP2 (By similarity). {ECO:0000250|UniProtKB:Q9JJV9, ECO:0000269|PubMed:11234013, ECO:0000269|PubMed:11804990, ECO:0000269|PubMed:12569159, ECO:0000269|PubMed:1309946, ECO:0000269|PubMed:19074138, ECO:0000269|PubMed:21447824, ECO:0000269|PubMed:23085483, ECO:0000269|PubMed:23420830, ECO:0000269|PubMed:24167619, ECO:0000269|PubMed:25370050, ECO:0000269|PubMed:26279430, ECO:0000269|PubMed:26392562, ECO:0000269|PubMed:26776555, ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348}.
uniprot
proteins
mass_dalton
226940
uniprot
proteins
mutagenesis
MUTAGEN 1476; /note="Q->K: Induces accelerated recovery from channel fast inactivation."; /evidence="ECO:0000269|PubMed:16054936"; MUTAGEN 1610; /note="D->A: Complete loss of channel inhibition by the spider Jingzhaotoxin-I."; /evidence="ECO:0000269|PubMed:26721415"; MUTAGEN 1610; /note="D->R: High decrease in affinity to the sea anemone toxin anthopleurin-B."; /evidence="ECO:0000269|PubMed:24898004"; MUTAGEN 1614; /note="K->A: 4.2-fold decrease of channel inhibition potency by the spider Jingzhaotoxin-I."; /evidence="ECO:0000269|PubMed:26721415"; MUTAGEN 1802..1804; /note="DPE->APA: Abolishes calcium response on channel inactivation."; /evidence="ECO:0000269|PubMed:19074138"; MUTAGEN 1974; /note="P->A: Strongly reduces interaction with NEDD4, NEDD4L or WWP2."; /evidence="ECO:0000269|PubMed:15548568"; MUTAGEN 1975; /note="P->A: Strongly reduces interaction with NEDD4, NEDD4L or WWP2."; /evidence="ECO:0000269|PubMed:15548568"; MUTAGEN 1976; /note="S->A: Strongly reduces interaction with NEDD4, NEDD4L or WWP2."; /evidence="ECO:0000269|PubMed:15548568"; MUTAGEN 1977; /note="Y->A: Strongly reduces interaction with NEDD4, NEDD4L or WWP2."; /evidence="ECO:0000269|PubMed:15217910, ECO:0000269|PubMed:15548568"; MUTAGEN 1978; /note="D->A: No effect on interaction with NEDD4, NEDD4L or WWP2."; /evidence="ECO:0000269|PubMed:15548568"; MUTAGEN 1979; /note="S->A: No effect on interaction with NEDD4, NEDD4L or WWP2."; /evidence="ECO:0000269|PubMed:15548568"; MUTAGEN 1980; /note="V->A: No effect on interaction with NEDD4, NEDD4L or WWP2."; /evidence="ECO:0000269|PubMed:15217910, ECO:0000269|PubMed:15548568"; MUTAGEN 1980; /note="V->D,R: Strongly reduces interaction with NEDD4L."; /evidence="ECO:0000269|PubMed:15217910, ECO:0000269|PubMed:15548568
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by NEDD4L; which promotes its endocytosis. Does not seem to be ubiquitinated by NEDD4 or WWP2. {ECO:0000269|PubMed:15217910, ECO:0000269|PubMed:15548568}.; PTM: Phosphorylation at Ser-1503 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents (Probable). Regulated through phosphorylation by CaMK2D (By similarity). {ECO:0000250|UniProtKB:Q9JJV9, ECO:0000305|PubMed:19666841}.; PTM: Lacks the cysteine which covalently binds the conotoxin GVIIJ. This cysteine (position 868) is speculated in other sodium channel subunits alpha to be implied in covalent binding with the sodium channel subunit beta-2 or beta-4. {ECO:0000250|UniProtKB:P15389}.; PTM: N-glycosylated at Asn-318, probably hinders potential interaction with regulatory subunits. {ECO:0000250|UniProtKB:P15389}.
uniprot
proteins
protein_family
Nav1.5/SCN5A subfamily
uniprot
proteins
protein_family
Sodium channel (TC 1.A.1.10) family
uniprot
proteins
pubmed
10377081
uniprot
proteins
pubmed
10471492
uniprot
proteins
pubmed
10508990
uniprot
proteins
pubmed
10532948
uniprot
proteins
pubmed
10590249
uniprot
proteins
pubmed
10618304
uniprot
proteins
pubmed
10627139
uniprot
proteins
pubmed
10690282
uniprot
proteins
pubmed
10911008
uniprot
proteins
pubmed
10940383
uniprot
proteins
pubmed
10973849
uniprot
proteins
pubmed
11234013
uniprot
proteins
pubmed
11304498
uniprot
proteins
pubmed
11410597
uniprot
proteins
pubmed
11535573
uniprot
proteins
pubmed
11710892
uniprot
proteins
pubmed
11748104
uniprot
proteins
pubmed
11804990
uniprot
proteins
pubmed
11823453
uniprot
proteins
pubmed
11889015
uniprot
proteins
pubmed
11901046
uniprot
proteins
pubmed
11997281
uniprot
proteins
pubmed
12051963
uniprot
proteins
pubmed
12106943
uniprot
proteins
pubmed
12193783
uniprot
proteins
pubmed
12209021
uniprot
proteins
pubmed
12358675
uniprot
proteins
pubmed
12454206
uniprot
proteins
pubmed
12471205
uniprot
proteins
pubmed
12522116
uniprot
proteins
pubmed
12569159
uniprot
proteins
pubmed
12574143
uniprot
proteins
pubmed
12673799
uniprot
proteins
pubmed
1309946
uniprot
proteins
pubmed
14500339
uniprot
proteins
pubmed
14523039
uniprot
proteins
pubmed
15023552
uniprot
proteins
pubmed
15217910
uniprot
proteins
pubmed
15338453
uniprot
proteins
pubmed
15466643
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15548568
uniprot
proteins
pubmed
15579534
uniprot
proteins
pubmed
15840476
uniprot
proteins
pubmed
15851320
uniprot
proteins
pubmed
16054936
uniprot
proteins
pubmed
16115203
uniprot
proteins
pubmed
16266370
uniprot
proteins
pubmed
16325048
uniprot
proteins
pubmed
16414944
uniprot
proteins
pubmed
16616735
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16922724
uniprot
proteins
pubmed
17075016
uniprot
proteins
pubmed
17081365
uniprot
proteins
pubmed
17198989
uniprot
proteins
pubmed
18060054
uniprot
proteins
pubmed
18088563
uniprot
proteins
pubmed
18252757
uniprot
proteins
pubmed
18341814
uniprot
proteins
pubmed
18368697
uniprot
proteins
pubmed
18378609
uniprot
proteins
pubmed
18451998
uniprot
proteins
pubmed
18456723
uniprot
proteins
pubmed
18596570
uniprot
proteins
pubmed
18599870
uniprot
proteins
pubmed
18616619
uniprot
proteins
pubmed
18708744
uniprot
proteins
pubmed
18848812
uniprot
proteins
pubmed
18929244
uniprot
proteins
pubmed
18929331
uniprot
proteins
pubmed
19027780
uniprot
proteins
pubmed
19056759
uniprot
proteins
pubmed
19074138
uniprot
proteins
pubmed
19251209
uniprot
proteins
pubmed
19272188
uniprot
proteins
pubmed
19302788
uniprot
proteins
pubmed
19376164
uniprot
proteins
pubmed
19666841
uniprot
proteins
pubmed
19716085
uniprot
proteins
pubmed
20129283
uniprot
proteins
pubmed
20398673
uniprot
proteins
pubmed
21109022
uniprot
proteins
pubmed
21167176
uniprot
proteins
pubmed
21447824
uniprot
proteins
pubmed
21726068
uniprot
proteins
pubmed
21817159
uniprot
proteins
pubmed
21994374
uniprot
proteins
pubmed
22705208
uniprot
proteins
pubmed
22795782
uniprot
proteins
pubmed
23085483
uniprot
proteins
pubmed
23092124
uniprot
proteins
pubmed
23420830
uniprot
proteins
pubmed
24167619
uniprot
proteins
pubmed
24898004
uniprot
proteins
pubmed
25370050
uniprot
proteins
pubmed
26279430
uniprot
proteins
pubmed
26392562
uniprot
proteins
pubmed
26721415
uniprot
proteins
pubmed
26776555
uniprot
proteins
pubmed
32850980
uniprot
proteins
pubmed
33712541
uniprot
proteins
pubmed
35348702
uniprot
proteins
pubmed
37117223
uniprot
proteins
pubmed
40768348
uniprot
proteins
pubmed
7651517
uniprot
proteins
pubmed
7889574
uniprot
proteins
pubmed
8541846
uniprot
proteins
pubmed
9506831
uniprot
proteins
pubmed
9521325
uniprot
proteins
pubmed
9686753
uniprot
proteins
sequence_length
2016
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1309946, ECO:0000269|PubMed:19074138, ECO:0000269|PubMed:21447824, ECO:0000269|PubMed:23085483, ECO:0000269|PubMed:23420830, ECO:0000269|PubMed:25370050, ECO:0000269|PubMed:26279430}; Multi-pass membrane protein {ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21447824}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:P15389}. Cell junction {ECO:0000250|UniProtKB:P15389}. Note=RANGRF promotes trafficking to the cell membrane. Colocalizes with PKP2 at intercalated disks in the heart (By similarity). {ECO:0000250|UniProtKB:P15389, ECO:0000269|PubMed:21447824, ECO:0000269|PubMed:23420830}.
uniprot
proteins
transmembrane_region
TRANSMEM 130..149; /note="Helical; Name=S1 of repeat I"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 158..179; /note="Helical; Name=S2 of repeat I"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 189..209; /note="Helical; Name=S3 of repeat I"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 217..236; /note="Helical; Name=S4 of repeat I"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 250..272; /note="Helical; Name=S5 of repeat I"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 387..413; /note="Helical; Name=S6 of repeat I"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 720..737; /note="Helical; Name=S1 of repeat II"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 747..769; /note="Helical; Name=S2 of repeat II"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 776..796; /note="Helical; Name=S3 of repeat II"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 807..821; /note="Helical; Name=S4 of repeat II"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 839..860; /note="Helical; Name=S5 of repeat II"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 913..941; /note="Helical; Name=S6 of repeat II"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 1204..1225; /note="Helical; Name=S1 of repeat III"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 1237..1259; /note="Helical; Name=S2 of repeat III"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 1269..1291; /note="Helical; Name=S3 of repeat III"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 1298..1317; /note="Helical; Name=S4 of repeat III"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 1331..1355; /note="Helical; Name=S5 of repeat III"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 1446..1470; /note="Helical; Name=S6 of repeat III"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 1529..1547; /note="Helical; Name=S1 of repeat IV"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 1559..1580; /note="Helical; Name=S2 of repeat IV"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 1590..1612; /note="Helical; Name=S3 of repeat IV"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 1620..1640; /note="Helical; Name=S4 of repeat IV"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 1651..1679; /note="Helical; Name=S5 of repeat IV"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH"; TRANSMEM 1746..1771; /note="Helical; Name=S6 of repeat IV"; /evidence="ECO:0000269|PubMed:33712541, ECO:0000269|PubMed:40768348, ECO:0007744|PDB:7DTC, ECO:0007744|PDB:9ITH
uniprot
proteins