SCN9A
entrez
6335
canonical
uniprot
Q15858
canonical
ensembl
ENSG00000169432
resolver
ensp
ENSP00000386306
resolver
ensp
ENSP00000495601
resolver
ensp
ENSP00000495983
resolver
genesymbol
SCN9A
resolver
genesymbol_syn
NENA
resolver
hgnc
HGNC:10597
resolver
uniprot
A1BUH5
resolver
uniprot
Q6B4R9
resolver
uniprot
Q6B4S0
resolver
uniprot
Q6B4S1
resolver
uniprot
Q70HX1
resolver
uniprot
Q70HX2
resolver
uniprot
Q8WTU1
resolver
uniprot
Q8WWN4
resolver
uniprot_entry
SCN9A_HUMAN
resolver
uniprot_sec
A1BUH5
resolver
uniprot_sec
Q6B4R9
resolver
uniprot_sec
Q6B4S0
resolver
uniprot_sec
Q6B4S1
resolver
uniprot_sec
Q70HX1
resolver
uniprot_sec
Q70HX2
resolver
uniprot_sec
Q8WTU1
resolver
uniprot_sec
Q8WWN4
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by tetrodotoxin (PubMed:23077250, PubMed:7720699). Weakly inhibited by saxitoxin (PubMed:23077250). Inhibited by the spider huwentoxin-IV that binds the extracellular loop S3-S4 of repeat II (PubMed:20855463, PubMed:21659528, PubMed:30765606). Inhibited by the spider protoxin-II that binds the extracellular loop S3-S4 of repeats II and IV (PubMed:20855463, PubMed:30661758, PubMed:30765606). Inhibited by the scorpion alpha-toxins CvIV4 and AaH2 (PubMed:21887265, PubMed:30733386). Inhibited by the conotoxin GVIIJ (PubMed:24497506). Inhibited by the spider beta/delta-theraphotoxin-Pre1a (PubMed:28428547). {ECO:0000269|PubMed:20855463, ECO:0000269|PubMed:21659528, ECO:0000269|PubMed:21887265, ECO:0000269|PubMed:23077250, ECO:0000269|PubMed:24497506, ECO:0000269|PubMed:28428547, ECO:0000269|PubMed:30661758, ECO:0000269|PubMed:30733386, ECO:0000269|PubMed:30765606, ECO:0000269|PubMed:7720699}.
uniprot
proteins
amino_acid_sequence
MAMLPPPGPQSFVHFTKQSLALIEQRIAERKSKEPKEEKKDDDEEAPKPSSDLEAGKQLPFIYGDIPPGMVSEPLEDLDPYYADKKTFIVLNKGKTIFRFNATPALYMLSPFSPLRRISIKILVHSLFSMLIMCTILTNCIFMTMNNPPDWTKNVEYTFTGIYTFESLVKILARGFCVGEFTFLRDPWNWLDFVVIVFAYLTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLKHKCFRNSLENNETLESIMNTLESEEDFRKYFYYLEGSKDALLCGFSTDSGQCPEGYTCVKIGRNPDYGYTSFDTFSWAFLALFRLMTQDYWENLYQQTLRAAGKTYMIFFVVVIFLGSFYLINLILAVVAMAYEEQNQANIEEAKQKELEFQQMLDRLKKEQEEAEAIAAAAAEYTSIRRSRIMGLSESSSETSKLSSKSAKERRNRRKKKNQKKLSSGEEKGDAEKLSKSESEDSIRRKSFHLGVEGHRRAHEKRLSTPNQSPLSIRGSLFSARRSSRTSLFSFKGRGRDIGSETEFADDEHSIFGDNESRRGSLFVPHRPQERRSSNISQASRSPPMLPVNGKMHSAVDCNGVVSLVDGRSALMLPNGQLLPEVIIDKATSDDSGTTNQIHKKRRCSSYLLSEDMLNDPNLRQRAMSRASILTNTVEELEESRQKCPPWWYRFAHKFLIWNCSPYWIKFKKCIYFIVMDPFVDLAITICIVLNTLFMAMEHHPMTEEFKNVLAIGNLVFTGIFAAEMVLKLIAMDPYEYFQVGWNIFDSLIVTLSLVELFLADVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINDDCTLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVYMMVMVIGNLVVLNLFLALLLSSFSSDNLTAIEEDPDANNLQIAVTRIKKGINYVKQTLREFILKAFSKKPKISREIRQAEDLNTKKENYISNHTLAEMSKGHNFLKEKDKISGFGSSVDKHLMEDSDGQSFIHNPSLTVTVPIAPGESDLENMNAEELSSDSDSEYSKVRLNRSSSSECSTVDNPLPGEGEEAEAEPMNSDEPEACFTDGCVWRFSCCQVNIESGKGKIWWNIRKTCYKIVEHSWFESFIVLMILLSSGALAFEDIYIERKKTIKIILEYADKIFTYIFILEMLLKWIAYGYKTYFTNAWCWLDFLIVDVSLVTLVANTLGYSDLGPIKSLRTLRALRPLRALSRFEGMRVVVNALIGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYECINTTDGSRFPASQVPNRSECFALMNVSQNVRWKNLKVNFDNVGLGYLSLLQVATFKGWTIIMYAAVDSVNVDKQPKYEYSLYMYIYFVVFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPGNKIQGCIFDLVTNQAFDISIMVLICLNMVTMMVEKEGQSQHMTEVLYWINVVFIILFTGECVLKLISLRHYYFTVGWNIFDFVVVIISIVGMFLADLIETYFVSPTLFRVIRLARIGRILRLVKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEDGINDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSKPPDCDPKKVHPGSSVEGDCGNPSVGIFYFVSYIIISFLVVVNMYIAVILENFSVATEESTEPLSEDDFEMFYEVWEKFDPDATQFIEFSKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDSLRSQMEERFMSANPSKVSYEPITTTLKRKQEDVSATVIQRAYRRYRLRQNVKNISSIYIKDGDRDDDLLNKKDMAFDNVNENSSPEKTDATSSTTSPPSYDSVTKPDKEKYEQDRTEKEDKGKDSKESKK
uniprot
proteins
disease_involvement
DISEASE: Primary erythermalgia (PERYTHM) [MIM:133020]: Autosomal dominant disease characterized by recurrent episodes of severe pain associated with redness and warmth in the feet or hands. {ECO:0000269|PubMed:14985375, ECO:0000269|PubMed:15385606, ECO:0000269|PubMed:15955112, ECO:0000269|PubMed:15958509, ECO:0000269|PubMed:16216943, ECO:0000269|PubMed:16392115, ECO:0000269|PubMed:16702558, ECO:0000269|PubMed:16988069, ECO:0000269|PubMed:18945915, ECO:0000269|PubMed:19369487, ECO:0000269|PubMed:24311784}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Indifference to pain, congenital, autosomal recessive (CIP) [MIM:243000]: A disorder characterized by congenital inability to perceive any form of pain, in any part of the body. All other sensory modalities are preserved and the peripheral and central nervous systems are apparently intact. Patients perceive the sensations of touch, warm and cold temperature, proprioception, tickle and pressure, but not painful stimuli. There is no evidence of a motor or sensory neuropathy, either axonal or demyelinating. {ECO:0000269|PubMed:20635406}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Paroxysmal extreme pain disorder (PEXPD) [MIM:167400]: An autosomal dominant paroxysmal disorder of pain and autonomic dysfunction. The distinctive features are paroxysmal episodes of burning pain in the rectal, ocular, and mandibular areas accompanied by autonomic manifestations such as skin flushing. {ECO:0000269|PubMed:17145499, ECO:0000269|PubMed:18945915, ECO:0000269|PubMed:25285947}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Pore-forming subunit of Nav1.7, a voltage-gated sodium (Nav) channel that directly mediates the depolarizing phase of action potentials in excitable membranes (PubMed:38381792, 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:38381792, PubMed:40768348). The influx of Na(+) ions provokes membrane depolarization, initiating the propagation of electrical signals throughout cells and tissues (PubMed:15385606, PubMed:16988069, PubMed:17145499, PubMed:17167479, PubMed:19369487, PubMed:24311784, PubMed:25240195, PubMed:26680203, PubMed:7720699). Nav1.7 plays a crucial role in controlling the excitability and action potential propagation from nociceptor neurons, thereby contributing to the sensory perception of pain (PubMed:17145499, PubMed:17167479, PubMed:19369487, PubMed:24311784). {ECO:0000269|PubMed:15178348, ECO:0000269|PubMed:15385606, ECO:0000269|PubMed:16988069, ECO:0000269|PubMed:17145499, ECO:0000269|PubMed:17167479, ECO:0000269|PubMed:19369487, ECO:0000269|PubMed:24311784, ECO:0000269|PubMed:25240195, ECO:0000269|PubMed:26680203, ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000269|PubMed:7720699}.
uniprot
proteins
mass_dalton
226372
uniprot
proteins
mutagenesis
MUTAGEN 304; /note="Y->L: Impairs interaction with SCN1B and ion conductance."; /evidence="ECO:0000269|PubMed:40768348"; MUTAGEN 365; /note="N->R: Impairs interaction with SCN1B and ion conductance."; /evidence="ECO:0000269|PubMed:40768348"; MUTAGEN 406; /note="E->K: Hyperpolarizes the voltage dependence of activation by 10.6 mV and prolonges fast-inactivation duration when coexpressed with SCN1B and SCN2B."; /evidence="ECO:0000269|PubMed:30765606"; MUTAGEN 764; /note="E->Q: 5-fold less blocked by the spider huwentoxin-IV."; /evidence="ECO:0000269|PubMed:21659528"; MUTAGEN 778; /note="I->A: 5-fold less inhibited by the spider protoxin-II."; /evidence="ECO:0000269|PubMed:30661758"; MUTAGEN 822; /note="E->A: No change in inhibition (IC(50)) by the spider protoxin-II, but has a significant impact on channel activation by shifiting the V(50) towart 0 mV when targeted by protoxin-II."; /evidence="ECO:0000269|PubMed:30661758"; MUTAGEN 822; /note="E->Q: 18-fold less blocked by the spider huwentoxin-IV."; /evidence="ECO:0000269|PubMed:21659528"; MUTAGEN 823; /note="L->A: 9-fold less inhibited by the spider protoxin-II."; /evidence="ECO:0000269|PubMed:30661758"; MUTAGEN 824; /note="F->A: 4-fold less inhibited by the spider protoxin-II."; /evidence="ECO:0000269|PubMed:30661758"; MUTAGEN 824; /note="F->C: Less inhibited by the spider protoxin-II."; /evidence="ECO:0000269|PubMed:30661758"; MUTAGEN 825; /note="L->A: No change in inhibition by the spider protoxin-II."; /evidence="ECO:0000269|PubMed:30661758"; MUTAGEN 825; /note="L->C: 19-fold less blocked by the spider huwentoxin-IV."; /evidence="ECO:0000269|PubMed:21659528"; MUTAGEN 826; /note="A->L: 8-fold less inhibited by the spider protoxin-II."; /evidence="ECO:0000269|PubMed:30661758"; MUTAGEN 827; /note="D->A: 13-fold less blocked by the spider huwentoxin-IV, 3-fold less inhibited by the spider protoxin-II, and has a significant impact on channel activation by shifiting the V(50) towart 0 mV when targeted by protoxin-II."; /evidence="ECO:0000269|PubMed:21659528, ECO:0000269|PubMed:30661758"; MUTAGEN 829; /note="E->C: 400-fold less blocked by the spider huwentoxin-IV."; /evidence="ECO:0000269|PubMed:20855463"; MUTAGEN 1409..1410; /note="TI->MD: Important increase in inhibition by saxitoxin and little increase in inhibition by tetrodotoxin."; /evidence="ECO:0000269|PubMed:23077250"; MUTAGEN 1490; /note="S->A: Abolishes stimulation by agents that stimulate PKC activity."; /evidence="ECO:0000269|PubMed:25240195"; MUTAGEN 1490; /note="S->D,E: Increases current amplitude."; /evidence="ECO:0000269|PubMed:25240195"; MUTAGEN 1597; /note="D->A: Decrease of the inhibition of fast inactivation produced by scorpion alpha-toxins CvIV4 and AaH2 on this channel."; /evidence="ECO:0000269|PubMed:21887265, ECO:0000269|PubMed:30733386"; MUTAGEN 1600; /note="E->Q: Decrease of the inhibition of fast inactivation produced by the scorpion alpha-toxin CvIV4 on this channel."; /evidence="ECO:0000269|PubMed:21887265"; MUTAGEN 1643; /note="A->D: Depolarizes the voltage-dependence of steady-state fast inactivation; enhances persistent current."; /evidence="ECO:0000269|PubMed:24311784"; MUTAGEN 1643; /note="A->K: No effect on voltage-dependence of steady-state fast inactivation."; /evidence="ECO:0000269|PubMed:24311784"; MUTAGEN 1643; /note="A->V: No effect on voltage-dependence of steady-state fast inactivation."; /evidence="ECO:0000269|PubMed:24311784"; MUTAGEN 1671; /note="K->W: Impairs interaction with SCN1B and ion conductance."; /evidence="ECO:0000269|PubMed:40768348
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-1490 by PKC in a highly conserved cytoplasmic loop increases peak sodium currents. {ECO:0000269|PubMed:25240195}.; PTM: Ubiquitinated by NEDD4L; which may promote its endocytosis. {ECO:0000250|UniProtKB:Q62205}.
uniprot
proteins
protein_family
Nav1.7/SCN9A subfamily
uniprot
proteins
protein_family
Sodium channel (TC 1.A.1.10) family
uniprot
proteins
pubmed
14985375
uniprot
proteins
pubmed
15178348
uniprot
proteins
pubmed
15302875
uniprot
proteins
pubmed
15385606
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
15955112
uniprot
proteins
pubmed
15958509
uniprot
proteins
pubmed
16216943
uniprot
proteins
pubmed
16392115
uniprot
proteins
pubmed
16702558
uniprot
proteins
pubmed
16988069
uniprot
proteins
pubmed
17145499
uniprot
proteins
pubmed
17167479
uniprot
proteins
pubmed
18945915
uniprot
proteins
pubmed
19369487
uniprot
proteins
pubmed
19763161
uniprot
proteins
pubmed
20635406
uniprot
proteins
pubmed
20855463
uniprot
proteins
pubmed
21659528
uniprot
proteins
pubmed
21887265
uniprot
proteins
pubmed
23077250
uniprot
proteins
pubmed
24311784
uniprot
proteins
pubmed
24497506
uniprot
proteins
pubmed
25240195
uniprot
proteins
pubmed
25285947
uniprot
proteins
pubmed
26680203
uniprot
proteins
pubmed
28428547
uniprot
proteins
pubmed
30661758
uniprot
proteins
pubmed
30733386
uniprot
proteins
pubmed
30765606
uniprot
proteins
pubmed
30795902
uniprot
proteins
pubmed
31647222
uniprot
proteins
pubmed
33216760
uniprot
proteins
pubmed
37117223
uniprot
proteins
pubmed
38381792
uniprot
proteins
pubmed
40768348
uniprot
proteins
pubmed
7720699
uniprot
proteins
pubmed
9169448
uniprot
proteins
sequence_length
1988
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15385606, ECO:0000269|PubMed:17167479, ECO:0000269|PubMed:19369487, ECO:0000269|PubMed:24311784, ECO:0000269|PubMed:25240195, ECO:0000269|PubMed:26680203, ECO:0000269|PubMed:7720699}; Multi-pass membrane protein {ECO:0000269|PubMed:30765606, ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348}. Cell projection, neuron projection {ECO:0000269|PubMed:30795902}. Cell projection, axon {ECO:0000269|PubMed:30795902}. Note=Localizes to neuron terminals (PubMed:30765606, PubMed:30795902). Also detected at Nodes of Ranvier (PubMed:30795902). {ECO:0000269|PubMed:30765606, ECO:0000269|PubMed:30795902}.
uniprot
proteins
transmembrane_region
TRANSMEM 126..145; /note="Helical; Name=S1 of repeat I"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 151..172; /note="Helical; Name=S2 of repeat I"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 186..204; /note="Helical; Name=S3 of repeat I"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 211..227; /note="Helical; Name=S4 of repeat I"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 242..267; /note="Helical; Name=S5 of repeat I"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 377..402; /note="Helical; Name=S6 of repeat I"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 746..762; /note="Helical; Name=S1 of repeat II"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 772..796; /note="Helical; Name=S2 of repeat II"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 806..822; /note="Helical; Name=S3 of repeat II"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 832..848; /note="Helical; Name=S4 of repeat II"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 866..888; /note="Helical; Name=S5 of repeat II"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 941..967; /note="Helical; Name=S6 of repeat II"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 1188..1212; /note="Helical; Name=S1 of repeat III"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 1225..1250; /note="Helical; Name=S2 of repeat III"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 1253..1278; /note="Helical; Name=S3 of repeat III"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 1288..1304; /note="Helical; Name=S4 of repeat III"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 1318..1342; /note="Helical; Name=S5 of repeat III"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 1432..1457; /note="Helical; Name=S6 of repeat III"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 1515..1534; /note="Helical; Name=S1 of repeat IV"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 1546..1567; /note="Helical; Name=S2 of repeat IV"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 1577..1598; /note="Helical; Name=S3 of repeat IV"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 1608..1627; /note="Helical; Name=S4 of repeat IV"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 1641..1663; /note="Helical; Name=S5 of repeat IV"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI"; TRANSMEM 1734..1759; /note="Helical; Name=S6 of repeat IV"; /evidence="ECO:0000269|PubMed:38381792, ECO:0000269|PubMed:40768348, ECO:0000305|PubMed:30765606, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:8XMM, ECO:0007744|PDB:8XMN, ECO:0007744|PDB:8XMO, ECO:0007744|PDB:9ITI
uniprot
proteins