ACE
entrez
1636
canonical
uniprot
P12821
canonical
ensembl
ENSG00000159640
resolver
ensp
ENSP00000290863
resolver
ensp
ENSP00000290866
resolver
ensp
ENSP00000392247
resolver
genesymbol
ACE
resolver
genesymbol_syn
DCP
resolver
genesymbol_syn
DCP1
resolver
hgnc
HGNC:2707
resolver
uniprot
B0LPF0
resolver
uniprot
B4DKH4
resolver
uniprot
B4DXI3
resolver
uniprot
E7EU16
resolver
uniprot
P22966
resolver
uniprot
Q53YX9
resolver
uniprot
Q59GY8
resolver
uniprot
Q7M4L4
resolver
uniprot_entry
ACE_HUMAN
resolver
uniprot_entry
B4DKH4_HUMAN
resolver
uniprot_sec
B0LPF0
resolver
uniprot_sec
B4DXI3
resolver
uniprot_sec
E7EU16
resolver
uniprot_sec
P22966
resolver
uniprot_sec
Q53YX9
resolver
uniprot_sec
Q59GY8
resolver
uniprot_sec
Q7M4L4
resolver
activity_regulation
ACTIVITY REGULATION: The dipeptidyl carboxypeptidase activity is strongly activated by chloride (PubMed:11432860, PubMed:12540854, PubMed:15615692, PubMed:16476442, PubMed:7683654). The dipeptidyl carboxypeptidase activity is specifically inhibited by lisinopril, captopril and enalaprilat (PubMed:12540854, PubMed:1320019, PubMed:16476442, PubMed:6208535, PubMed:6270633, PubMed:7876104, PubMed:8609242). {ECO:0000269|PubMed:11432860, ECO:0000269|PubMed:12540854, ECO:0000269|PubMed:1320019, ECO:0000269|PubMed:15615692, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:6208535, ECO:0000269|PubMed:6270633, ECO:0000269|PubMed:7683654, ECO:0000269|PubMed:7876104, ECO:0000269|PubMed:8609242}.; ACTIVITY REGULATION: [Isoform Testis-specific]: Strongly inhibited by lisinopril and captopril. {ECO:0000269|PubMed:1668266, ECO:0000269|PubMed:21810173}.
uniprot
proteins
amino_acid_sequence
MGAASGRRGPGLLLPLPLLLLLPPQPALALDPGLQPGNFSADEAGAQLFAQSYNSSAEQVLFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIWQNFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWNATHMFRVAEEFFTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLQAGSSRPWQEVLKDMVGLDALDAQPLLKYFQPVTQWLQEQNQQNGEVLGWPEYQWHPPLPDNYPEGIDLVTDEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYGTQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAMLSYFKPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLPDSGRVSFLGLDLDAQQARVGQWLLLFLGIALLVATLGLSQRLFSIRHRSLHRHSHGPQFGSEVELRHS
uniprot
proteins
disease_involvement
DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. {ECO:0000269|PubMed:15534175}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Renal tubular dysgenesis (RTD) [MIM:267430]: Autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype). {ECO:0000269|PubMed:16116425}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Microvascular complications of diabetes 3 (MVCD3) [MIM:612624]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. {ECO:0000269|PubMed:10099885}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Intracerebral hemorrhage (ICH) [MIM:614519]: A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke. {ECO:0000269|PubMed:15277638}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.15.1
uniprot
proteins
function
FUNCTION: Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity (PubMed:15615692, PubMed:20826823, PubMed:2558109, PubMed:4322742, PubMed:7523412, PubMed:7683654). Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates (PubMed:10913258, PubMed:1320019, PubMed:1851160, PubMed:19773553, PubMed:7683654, PubMed:7876104). Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin (PubMed:11432860, PubMed:1851160, PubMed:19773553, PubMed:23056909, PubMed:4322742). Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response (PubMed:15615692, PubMed:2558109, PubMed:4322742, PubMed:6055465, PubMed:6270633, PubMed:7683654). Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins (PubMed:15615692, PubMed:6208535, PubMed:6270633, PubMed:656131). Catalyzes degradation of different enkephalin neuropeptides (Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met-enkephalin-Arg-Gly-Leu) (PubMed:2982830, PubMed:6270633, PubMed:656131). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin (By similarity). Met-enkephalin-Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long-term synaptic potentiation of glutamate release (By similarity). Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) (PubMed:26403559, PubMed:7876104, PubMed:8257427, PubMed:8609242). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (PubMed:18077343). Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation (PubMed:11604391, PubMed:16154999, PubMed:19773553). Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones (PubMed:10336644, PubMed:2983326, PubMed:7683654, PubMed:9371719). Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region (PubMed:10336644, PubMed:19773553, PubMed:7876104). {ECO:0000250|UniProtKB:P09470, ECO:0000269|PubMed:10336644, ECO:0000269|PubMed:10913258, ECO:0000269|PubMed:11432860, ECO:0000269|PubMed:11604391, ECO:0000269|PubMed:1320019, ECO:0000269|PubMed:15615692, ECO:0000269|PubMed:16154999, ECO:0000269|PubMed:18077343, ECO:0000269|PubMed:1851160, ECO:0000269|PubMed:19773553, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:23056909, ECO:0000269|PubMed:2558109, ECO:0000269|PubMed:26403559, ECO:0000269|PubMed:2982830, ECO:0000269|PubMed:2983326, ECO:0000269|PubMed:4322742, ECO:0000269|PubMed:6055465, ECO:0000269|PubMed:6208535, ECO:0000269|PubMed:6270633, ECO:0000269|PubMed:656131, ECO:0000269|PubMed:7523412, ECO:0000269|PubMed:7683654, ECO:0000269|PubMed:7876104, ECO:0000269|PubMed:8257427, ECO:0000269|PubMed:8609242, ECO:0000269|PubMed:9371719}.; FUNCTION: [Angiotensin-converting enzyme, soluble form]: Soluble form that is released in blood plasma and other body fluids following proteolytic cleavage in the juxtamembrane stalk region. {ECO:0000269|PubMed:10769174, ECO:0000269|PubMed:11274151, ECO:0000269|PubMed:7499427, ECO:0000269|PubMed:8253769}.; FUNCTION: [Isoform Testis-specific]: Isoform produced by alternative promoter usage that is specifically expressed in spermatocytes and adult testis, and which is required for male fertility (PubMed:1651327, PubMed:1668266). In contrast to somatic isoforms, only contains one catalytic domain (PubMed:1651327, PubMed:1668266). Acts as a dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of substrates (PubMed:1668266, PubMed:24297181). The identity of substrates that are needed for male fertility is unknown (By similarity). May also have a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. The GPIase activity was reported to be essential for the egg-binding ability of the sperm (By similarity). This activity is however unclear and has been challenged by other groups, suggesting that it may be indirect (By similarity). {ECO:0000250|UniProtKB:P09470, ECO:0000269|PubMed:1651327, ECO:0000269|PubMed:1668266, ECO:0000269|PubMed:24297181}.
uniprot
proteins
mass_dalton
149715
uniprot
proteins
mutagenesis
MUTAGEN 318; /note="N->D: In Ndom123456 mutant; abolished dipeptidyl carboxypeptidase activity; when associated with D-445 and D-509. In Ndom1234569 mutant; does not affect dipeptidyl carboxypeptidase activity; when associated with D-445."; /evidence="ECO:0000269|PubMed:20826823"; MUTAGEN 390..394; /note="HEMGH->KEMGK: Abolished dipeptidyl carboxypeptidase activity; when associated with 988-K--K-992. Abolished N-terminal active sites, leading to impaired ability to degrade the hemoregulatory peptide N-acetyl-SDKP (AcSDKP). In contrast, does not affect cleavage of other substrates, such as Cholecystokinin-5."; /evidence="ECO:0000269|PubMed:10336644, ECO:0000269|PubMed:1320019, ECO:0000269|PubMed:1851160, ECO:0000269|PubMed:7683654, ECO:0000269|PubMed:7876104, ECO:0000269|PubMed:7961923"; MUTAGEN 391; /note="E->D: Abolished peptidase activity, leading to increased levels of amyloid-beta; when associated with D-989."; /evidence="ECO:0000269|PubMed:16154999, ECO:0000269|PubMed:19773553"; MUTAGEN 445; /note="N->D: In Ndom123456 mutant; abolished dipeptidyl carboxypeptidase activity; when associated with D-318 and D-445. In Ndom1234569 mutant; does not affect dipeptidyl carboxypeptidase activity; when associated with D-318."; /evidence="ECO:0000269|PubMed:20826823"; MUTAGEN 509; /note="N->D: In Ndom123456 mutant; abolished dipeptidyl carboxypeptidase activity; when associated with D-318 and D-445."; /evidence="ECO:0000269|PubMed:20826823"; MUTAGEN 529; /note="R->Q: Abolished dependence to chloride, leading to reduced peptidyl dipeptidase activity."; /evidence="ECO:0000269|PubMed:11432860"; MUTAGEN 988..992; /note="HEMGH->KEMGK: Abolished dipeptidyl carboxypeptidase activity; when associated with 390-K--K-394. Abolishes the second active site, preventing maturation of Cholecystokinin-5."; /evidence="ECO:0000269|PubMed:10336644, ECO:0000269|PubMed:1320019, ECO:0000269|PubMed:1851160, ECO:0000269|PubMed:7683654"; MUTAGEN 989; /note="E->D: Abolished peptidase activity, leading to increased levels of amyloid-beta; when associated with D-391."; /evidence="ECO:0000269|PubMed:16154999, ECO:0000269|PubMed:19773553"; MUTAGEN 1016; /note="E->D: Strongly decreased dipeptidyl carboxypeptidase activity; when associated with 390-K--K-394."; /evidence="ECO:0000269|PubMed:7961923"; MUTAGEN 1016; /note="E->V: Abolished dipeptidyl carboxypeptidase activity; when associated with 390-K--K-394."; /evidence="ECO:0000269|PubMed:7961923"; MUTAGEN 1020; /note="D->E,A: Decreased dipeptidyl carboxypeptidase activity; when associated with 390-K--K-394."; /evidence="ECO:0000269|PubMed:7961923"; MUTAGEN 1116; /note="K->A: Decreased ability to cleave substance P and bradykinin. Reduced binding to captopril inhibitor."; /evidence="ECO:0000269|PubMed:15615692"; MUTAGEN 1125; /note="Y->F: Decreased ability to cleave substance P and captopril inhibitor."; /evidence="ECO:0000269|PubMed:15615692"; MUTAGEN 1127; /note="R->Q: Abolished dependence to chloride, leading to reduced peptidyl dipeptidase activity."; /evidence="ECO:0000269|PubMed:11432860"; MUTAGEN 1166; /note="R->Q: Does not prevent cleavage and secretion of the soluble form, suggesting that processing can take place at different sites."; /evidence="ECO:0000269|PubMed:8253769"; MUTAGEN 1229; /note="N->Q: Increased cleavage and secretion of the soluble form by generating a new cleavage site."; /evidence="ECO:0000269|PubMed:11274151"; MUTAGEN 1299; /note="S->A: Abolishes phosphorylation and decreases membrane retention."; /evidence="ECO:0000269|PubMed:12386153, ECO:0000269|PubMed:21901117"; MUTAGEN P12821-3:103; /note="N->D: In ACE(t)g0 mutant; abolished N-glycosylation leading to impaired stability and degradation; when associated with D-121, D-140, D-368 and D-617. In ACE(t)g2 mutant; decreased N-glycosylation without affecting stability; when associated with D-140, D-368 and D-617. In ACE(t)g3 mutant; decreased N-glycosylation leading to impaired stability and degradation; when associated with D-121, D-368 and D-617."; /evidence="ECO:0000269|PubMed:8626443"; MUTAGEN P12821-3:121; /note="N->D: In ACE(t)g0 mutant; abolished N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-140, D-368 and D-617. In ACE(t)g1 mutant; decreased N-glycosylation without affecting stability; when associated with D-140, D-368 and D-617. In ACE(t)g3 mutant; decreased N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-368 and D-617."; /evidence="ECO:0000269|PubMed:8626443"; MUTAGEN P12821-3:140; /note="N->D: In ACE(t)g0 mutant; abolished N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-121, D-368 and D-617. In ACE(t)g1 mutant; decreased N-glycosylation without affecting stability; when associated with D-121, D-368 and D-617. In ACE(t)g2 mutant; decreased N-glycosylation without affecting stability; when associated with D-103, D-368 and D-617."; /evidence="ECO:0000269|PubMed:8626443"; MUTAGEN P12821-3:368; /note="N->D: In ACE(t)g0 mutant; abolished N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-121, D-140 and D-617. In ACE(t)g1 mutant; decreased N-glycosylation without affecting stability; when associated with D-121, D-140 and D-617. In ACE(t)g2 mutant; decreased N-glycosylation without affecting stability; when associated with D-103, D-140 and D-617. In ACE(t)g3 mutant; decreased N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-121 and D-617."; /evidence="ECO:0000269|PubMed:8626443"; MUTAGEN P12821-3:553; /note="R->K,Q: Abolished binding to chloride ion."; /evidence="ECO:0000269|PubMed:24297181"; MUTAGEN P12821-3:617; /note="N->D: In ACE(t)g0 mutant; abolished N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-121, D-140 and D-368. In ACE(t)g1 mutant; decreased N-glycosylation without affecting stability; when associated with D-121, D-140 and D-368. In ACE(t)g2 mutant; decreased N-glycosylation without affecting stability; when associated with D-103, D-140 and D-368. In ACE(t)g3 mutant; decreased N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-121 and D-368."; /evidence="ECO:0000269|PubMed:8626443
uniprot
proteins
post_translational_modification
PTM: [Angiotensin-converting enzyme, soluble form]: Produced following proteolytic cleavage by secretase enzymes that cleave the transmembrane form in the juxtamembrane stalk region upstream of the transmembrane region (PubMed:10769174, PubMed:11274151, PubMed:7499427, PubMed:8253769). Cleavage can take place at different sites of the juxtamembrane stalk region (PubMed:10769174, PubMed:11274151, PubMed:7499427, PubMed:8253769). {ECO:0000269|PubMed:10769174, ECO:0000269|PubMed:11274151, ECO:0000269|PubMed:7499427, ECO:0000269|PubMed:8253769}.; PTM: Phosphorylated by CK2 on Ser-1299; which allows membrane retention (PubMed:12386153). Phosphorylated on tyrosine residues on its extracellular part, promoting cleavage by secretase enzymes and formation of the soluble form (Angiotensin-converting enzyme, soluble form) (By similarity). {ECO:0000250|UniProtKB:P12822, ECO:0000269|PubMed:12386153}.
uniprot
proteins
protein_family
Peptidase M2 family
uniprot
proteins
pubmed
10099885
uniprot
proteins
pubmed
10319862
uniprot
proteins
pubmed
10336644
uniprot
proteins
pubmed
10391210
uniprot
proteins
pubmed
10769174
uniprot
proteins
pubmed
10913258
uniprot
proteins
pubmed
10924499
uniprot
proteins
pubmed
10969042
uniprot
proteins
pubmed
11076943
uniprot
proteins
pubmed
11274151
uniprot
proteins
pubmed
11432860
uniprot
proteins
pubmed
11551873
uniprot
proteins
pubmed
11604391
uniprot
proteins
pubmed
12386153
uniprot
proteins
pubmed
12459472
uniprot
proteins
pubmed
12540854
uniprot
proteins
pubmed
12542396
uniprot
proteins
pubmed
1320019
uniprot
proteins
pubmed
14694062
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15151696
uniprot
proteins
pubmed
15236580
uniprot
proteins
pubmed
15277638
uniprot
proteins
pubmed
15534175
uniprot
proteins
pubmed
15615692
uniprot
proteins
pubmed
15671045
uniprot
proteins
pubmed
16116425
uniprot
proteins
pubmed
16154999
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16476442
uniprot
proteins
pubmed
16476786
uniprot
proteins
pubmed
1649623
uniprot
proteins
pubmed
1651327
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
1668266
uniprot
proteins
pubmed
18077343
uniprot
proteins
pubmed
1851160
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19773553
uniprot
proteins
pubmed
20826823
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21810173
uniprot
proteins
pubmed
21901117
uniprot
proteins
pubmed
23056909
uniprot
proteins
pubmed
24297181
uniprot
proteins
pubmed
2547653
uniprot
proteins
pubmed
2554286
uniprot
proteins
pubmed
2558109
uniprot
proteins
pubmed
25787250
uniprot
proteins
pubmed
26403559
uniprot
proteins
pubmed
2849100
uniprot
proteins
pubmed
2982830
uniprot
proteins
pubmed
2983326
uniprot
proteins
pubmed
4322742
uniprot
proteins
pubmed
6055465
uniprot
proteins
pubmed
6208535
uniprot
proteins
pubmed
6270633
uniprot
proteins
pubmed
656131
uniprot
proteins
pubmed
7499427
uniprot
proteins
pubmed
7523412
uniprot
proteins
pubmed
7683654
uniprot
proteins
pubmed
7876104
uniprot
proteins
pubmed
7961923
uniprot
proteins
pubmed
8253769
uniprot
proteins
pubmed
8257427
uniprot
proteins
pubmed
8609242
uniprot
proteins
pubmed
8626443
uniprot
proteins
pubmed
8755737
uniprot
proteins
pubmed
9013598
uniprot
proteins
pubmed
9371719
uniprot
proteins
pubmed
9642152
uniprot
proteins
sequence_length
1306
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12386153}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P09470}. Note=Detected in both cell membrane and cytoplasm in neurons. {ECO:0000250|UniProtKB:P09470}.; SUBCELLULAR LOCATION: [Angiotensin-converting enzyme, soluble form]: Secreted {ECO:0000269|PubMed:10769174, ECO:0000269|PubMed:11274151, ECO:0000269|PubMed:7499427, ECO:0000269|PubMed:8253769}.; SUBCELLULAR LOCATION: [Isoform Testis-specific]: Cell membrane {ECO:0000269|PubMed:1668266, ECO:0000269|PubMed:8626443}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:1668266}. Note=The testis-specific isoform can be cleaved before the transmembrane region, releasing a soluble form. {ECO:0000269|PubMed:1668266}.
uniprot
proteins
transmembrane_region
TRANSMEM 1257..1277; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins