ACE_PANTR
ID ACE_PANTR Reviewed; 1304 AA.
AC Q9GLN7; Q9GLN6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000303|PubMed:11013071};
DE Short=ACE {ECO:0000303|PubMed:11013071};
DE EC=3.4.15.1 {ECO:0000250|UniProtKB:P12821};
DE AltName: Full=Dipeptidyl carboxypeptidase I;
DE AltName: Full=Kininase II {ECO:0000250|UniProtKB:P12821};
DE AltName: CD_antigen=CD143;
DE Contains:
DE RecName: Full=Angiotensin-converting enzyme, soluble form {ECO:0000250|UniProtKB:P12821};
DE Flags: Precursor;
GN Name=ACE {ECO:0000303|PubMed:11013071}; Synonyms=DCP1;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11013071; DOI=10.1006/geno.2000.6313;
RA Dufour C., Casane D., Denton D., Wickings J., Corvol P., Jeunemaitre X.;
RT "Human-chimpanzee DNA sequence variation in the four major genes of the
RT renin angiotensin system.";
RL Genomics 69:14-26(2000).
CC -!- FUNCTION: Dipeptidyl carboxypeptidase that removes dipeptides from the
CC C-terminus of a variety of circulating hormones, such as angiotensin I,
CC bradykinin or enkephalins, thereby playing a key role in the regulation
CC of blood pressure, electrolyte homeostasis or synaptic plasticity.
CC Composed of two similar catalytic domains, each possessing a functional
CC active site, with different selectivity for substrates. Plays a major
CC role in the angiotensin-renin system that regulates blood pressure and
CC sodium retention by the kidney by converting angiotensin I to
CC angiotensin II, resulting in an increase of the vasoconstrictor
CC activity of angiotensin. Also able to inactivate bradykinin, a potent
CC vasodilator, and therefore enhance the blood pressure response. Acts as
CC a regulator of synaptic transmission by mediating cleavage of
CC neuropeptide hormones, such as substance P, neurotensin or enkephalins.
CC Catalyzes degradation of different enkephalin neuropeptides (Met-
CC enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met-
CC enkephalin-Arg-Gly-Leu) (By similarity). Acts as a regulator of
CC synaptic plasticity in the nucleus accumbens of the brain by mediating
CC cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid
CC receptor OPRM1, into Met-enkephalin. Met-enkephalin-Arg-Phe cleavage by
CC ACE decreases activation of OPRM1, leading to long-term synaptic
CC potentiation of glutamate release (By similarity). Also acts as a
CC regulator of hematopoietic stem cell differentiation by mediating
CC degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP). Acts as a
CC regulator of cannabinoid signaling pathway by mediating degradation of
CC hemopressin, an antagonist peptide of the cannabinoid receptor CNR1.
CC Involved in amyloid-beta metabolism by catalyzing degradation of
CC Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby
CC preventing plaque formation. Catalyzes cleavage of cholecystokinin
CC (maturation of Cholecystokinin-8 and Cholecystokinin-5) and
CC Gonadoliberin-1 (both maturation and degradation) hormones. Degradation
CC of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta
CC proteins is mediated by the N-terminal catalytic domain, while
CC angiotensin I and cholecystokinin cleavage is mediated by the C-
CC terminal catalytic region (By similarity).
CC {ECO:0000250|UniProtKB:P09470, ECO:0000250|UniProtKB:P12821}.
CC -!- FUNCTION: [Angiotensin-converting enzyme, soluble form]: Soluble form
CC that is released in blood plasma and other body fluids following
CC proteolytic cleavage in the juxtamembrane stalk region.
CC {ECO:0000250|UniProtKB:P12821}.
CC -!- FUNCTION: [Isoform Testis-specific]: Isoform produced by alternative
CC promoter usage that is specifically expressed in spermatocytes and
CC adult testis, and which is required for male fertility. In contrast to
CC somatic isoforms, only contains one catalytic domain. Acts as a
CC dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus
CC of substrates (By similarity). The identity of substrates that are
CC needed for male fertility is unknown. May also have a glycosidase
CC activity which releases GPI-anchored proteins from the membrane by
CC cleaving the mannose linkage in the GPI moiety. The GPIase activity was
CC reported to be essential for the egg-binding ability of the sperm. This
CC activity is however unclear and has been challenged by other groups,
CC suggesting that it may be indirect (By similarity).
CC {ECO:0000250|UniProtKB:P09470, ECO:0000250|UniProtKB:P12821}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa,
CC when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion
CC of angiotensin I to angiotensin II, with increase in vasoconstrictor
CC activity, but no action on angiotensin II.; EC=3.4.15.1;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=angiotensin I + H2O = angiotensin II + L-histidyl-L-leucine;
CC Xref=Rhea:RHEA:63560, ChEBI:CHEBI:15377, ChEBI:CHEBI:58506,
CC ChEBI:CHEBI:147350, ChEBI:CHEBI:147392; EC=3.4.15.1;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63561;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bradykinin + H2O = bradykinin(1-7) + L-Phe-L-Arg;
CC Xref=Rhea:RHEA:71451, ChEBI:CHEBI:15377, ChEBI:CHEBI:132988,
CC ChEBI:CHEBI:133147, ChEBI:CHEBI:147352;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71452;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + substance P = L-Leu-L-Met-NH2 + substance P(1-9);
CC Xref=Rhea:RHEA:71459, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692,
CC ChEBI:CHEBI:190693, ChEBI:CHEBI:190700;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71460;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + substance P = Gly-L-Leu-L-Met-NH2 + substance P(1-8);
CC Xref=Rhea:RHEA:71463, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692,
CC ChEBI:CHEBI:190694, ChEBI:CHEBI:190699;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71464;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + substance P = L-Phe-L-Phe-Gly-L-Leu-L-Met-NH2 +
CC substance P(1-6); Xref=Rhea:RHEA:71471, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:190692, ChEBI:CHEBI:190696, ChEBI:CHEBI:190697;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71472;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + neurotensin = L-isoleucyl-L-leucine + neurotensin(1-11);
CC Xref=Rhea:RHEA:71475, ChEBI:CHEBI:15377, ChEBI:CHEBI:147362,
CC ChEBI:CHEBI:190704, ChEBI:CHEBI:190706;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71476;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=goralatide + H2O = L-lysyl-L-proline + N-acetyl-L-seryl-L-
CC aspartate; Xref=Rhea:RHEA:71455, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:190701, ChEBI:CHEBI:190702, ChEBI:CHEBI:190703;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71456;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + Met-enkephalin = L-phenylalanyl-L-methionine + L-
CC tyrosylglycylglycine; Xref=Rhea:RHEA:71483, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:189868, ChEBI:CHEBI:190708, ChEBI:CHEBI:190709;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71484;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + Leu-enkephalin = L-phenylalanyl-L-leucine + L-
CC tyrosylglycylglycine; Xref=Rhea:RHEA:71487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:190689, ChEBI:CHEBI:190708, ChEBI:CHEBI:190710;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71488;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + Met-enkephalin-Arg-Phe = L-arginyl-L-phenylalanine +
CC Met-enkephalin; Xref=Rhea:RHEA:70675, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:189868, ChEBI:CHEBI:189869, ChEBI:CHEBI:189870;
CC Evidence={ECO:0000250|UniProtKB:P09470};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70676;
CC Evidence={ECO:0000250|UniProtKB:P09470};
CC -!- CATALYTIC ACTIVITY: [Isoform Testis-specific]:
CC Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa,
CC when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion
CC of angiotensin I to angiotensin II, with increase in vasoconstrictor
CC activity, but no action on angiotensin II.; EC=3.4.15.1;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P12821};
CC -!- COFACTOR: [Isoform Testis-specific]:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC Note=Isoform Testis-specific only binds 1 Zn(2+) ion per subunit.
CC {ECO:0000250|UniProtKB:P12821};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC Note=Binds 3 chloride ions per subunit. {ECO:0000250|UniProtKB:P12821};
CC -!- COFACTOR: [Isoform Testis-specific]:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:P12821};
CC -!- ACTIVITY REGULATION: The dipeptidyl carboxypeptidase activity is
CC strongly activated by chloride. The dipeptidyl carboxypeptidase
CC activity is specifically inhibited by lisinopril, captopril and
CC enalaprilat. {ECO:0000250|UniProtKB:P12821}.
CC -!- ACTIVITY REGULATION: [Isoform Testis-specific]: Strongly inhibited by
CC lisinopril and captopril. {ECO:0000250|UniProtKB:P12821}.
CC -!- SUBUNIT: Monomer and homodimer; homodimerizes following binding to an
CC inhibitor (By similarity). Interacts with calmodulin (CALM1, CALM2 or
CC CALM3); interaction takes place in the cytoplasmic region and regulates
CC phosphorylation and proteolytic cleavage (By similarity).
CC {ECO:0000250|UniProtKB:P12821, ECO:0000250|UniProtKB:P12822}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P12821};
CC Single-pass type I membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000250|UniProtKB:P09470}. Note=Detected in both cell membrane and
CC cytoplasm in neurons. {ECO:0000250|UniProtKB:P09470}.
CC -!- SUBCELLULAR LOCATION: [Angiotensin-converting enzyme, soluble form]:
CC Secreted {ECO:0000250|UniProtKB:P12821}.
CC -!- SUBCELLULAR LOCATION: [Isoform Testis-specific]: Cell membrane
CC {ECO:0000250|UniProtKB:P12821}; Single-pass type I membrane protein
CC {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:P12821}. Note=The
CC testis-specific isoform can be cleaved before the transmembrane region,
CC releasing a soluble form. {ECO:0000250|UniProtKB:P12821}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=Somatic;
CC IsoId=Q9GLN7-1; Sequence=Displayed;
CC Name=Testis-specific; Synonyms=ACE-T;
CC IsoId=Q9GLN7-2, Q9GLN6-1;
CC Sequence=VSP_037640, VSP_037641;
CC -!- PTM: [Angiotensin-converting enzyme, soluble form]: Produced following
CC proteolytic cleavage by secretase enzymes that cleave the transmembrane
CC form in the juxtamembrane stalk region upstream of the transmembrane
CC region. Cleavage can take place at different sites of the juxtamembrane
CC stalk region. {ECO:0000250|UniProtKB:P12821}.
CC -!- PTM: Phosphorylated by CK2 on Ser-1297; which allows membrane retention
CC (By similarity). Phosphorylated on tyrosine residues on its
CC extracellular part, promoting cleavage by secretase enzymes and
CC formation of the soluble form (Angiotensin-converting enzyme, soluble
CC form) (By similarity). {ECO:0000250|UniProtKB:P12821,
CC ECO:0000250|UniProtKB:P12822}.
CC -!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
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DR EMBL; AF193486; AAG31358.1; -; Genomic_DNA.
DR EMBL; AF193462; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193464; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193463; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193465; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193467; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193469; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193471; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193473; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193482; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193481; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193480; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193479; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193478; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193477; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193476; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193475; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193474; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193485; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193484; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193483; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193472; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193470; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193468; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193466; AAG31358.1; JOINED; Genomic_DNA.
DR EMBL; AF193486; AAG31359.1; -; Genomic_DNA.
DR EMBL; AF193473; AAG31359.1; JOINED; Genomic_DNA.
DR EMBL; AF193474; AAG31359.1; JOINED; Genomic_DNA.
DR EMBL; AF193475; AAG31359.1; JOINED; Genomic_DNA.
DR EMBL; AF193476; AAG31359.1; JOINED; Genomic_DNA.
DR EMBL; AF193477; AAG31359.1; JOINED; Genomic_DNA.
DR EMBL; AF193478; AAG31359.1; JOINED; Genomic_DNA.
DR EMBL; AF193479; AAG31359.1; JOINED; Genomic_DNA.
DR EMBL; AF193480; AAG31359.1; JOINED; Genomic_DNA.
DR EMBL; AF193481; AAG31359.1; JOINED; Genomic_DNA.
DR EMBL; AF193482; AAG31359.1; JOINED; Genomic_DNA.
DR EMBL; AF193483; AAG31359.1; JOINED; Genomic_DNA.
DR EMBL; AF193484; AAG31359.1; JOINED; Genomic_DNA.
DR EMBL; AF193485; AAG31359.1; JOINED; Genomic_DNA.
DR RefSeq; XP_016785980.1; XM_016930491.1. [Q9GLN7-2]
DR AlphaFoldDB; Q9GLN7; -.
DR SMR; Q9GLN7; -.
DR STRING; 9598.ENSPTRP00000038991; -.
DR MEROPS; M02.001; -.
DR PRIDE; Q9GLN7; -.
DR Ensembl; ENSPTRT00000102035; ENSPTRP00000073589; ENSPTRG00000009513. [Q9GLN7-2]
DR GeneID; 449567; -.
DR CTD; 1636; -.
DR eggNOG; KOG3690; Eukaryota.
DR GeneTree; ENSGT00940000162051; -.
DR InParanoid; Q9GLN7; -.
DR OMA; WPEYNDS; -.
DR Proteomes; UP000002277; Chromosome 17.
DR Bgee; ENSPTRG00000009513; Expressed in testis and 18 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; ISS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0008241; F:peptidyl-dipeptidase activity; ISS:UniProtKB.
DR GO; GO:0002003; P:angiotensin maturation; ISS:UniProtKB.
DR GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
DR GO; GO:0042447; P:hormone catabolic process; ISS:UniProtKB.
DR GO; GO:0042445; P:hormone metabolic process; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IBA:GO_Central.
DR GO; GO:0010814; P:substance P catabolic process; ISS:UniProtKB.
DR CDD; cd06461; M2_ACE; 2.
DR InterPro; IPR001548; Peptidase_M2.
DR PANTHER; PTHR10514; PTHR10514; 2.
DR Pfam; PF01401; Peptidase_M2; 2.
DR PRINTS; PR00791; PEPDIPTASEA.
DR PROSITE; PS00142; ZINC_PROTEASE; 2.
PE 3: Inferred from homology;
KW Alternative promoter usage; Calmodulin-binding; Carboxypeptidase;
KW Cell membrane; Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase;
KW Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix; Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT CHAIN 28..1304
FT /note="Angiotensin-converting enzyme"
FT /id="PRO_0000028545"
FT CHAIN 28..1230
FT /note="Angiotensin-converting enzyme, soluble form"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT /id="PRO_0000028546"
FT TOPO_DOM 28..1257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1258..1274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1275..1304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 28..628
FT /note="Peptidase M2 1"
FT REGION 629..1230
FT /note="Peptidase M2 2"
FT REGION 1213..1254
FT /note="Juxtamembrane stalk"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT ACT_SITE 389
FT /note="Proton acceptor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 518
FT /note="Proton donor 1"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT ACT_SITE 987
FT /note="Proton acceptor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 1116
FT /note="Proton donor 2"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 229
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 527
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 789
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 827
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 986
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 990
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 1014
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 1088
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 1092
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 1125
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT MOD_RES 1297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 155..163
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT DISULFID 755..761
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT DISULFID 955..973
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT DISULFID 1141..1153
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT VAR_SEQ 1..572
FT /note="Missing (in isoform Testis-specific)"
FT /evidence="ECO:0000305"
FT /id="VSP_037640"
FT VAR_SEQ 573..639
FT /note="AGSSRPWQEVLKDMVGLDALDAQPLLKYFQPVTQWLQEQNQQNGEVLGWPEY
FT QWHPPLPDNYPEGID -> MGQGWATAGLPSLLFLLLCYGHPLLVPSQEAPRQVTVTHG
FT TSSQATTSGQTTTHQATAHQTSAQSPN (in isoform Testis-specific)"
FT /evidence="ECO:0000305"
FT /id="VSP_037641"
SQ SEQUENCE 1304 AA; 149370 MW; DCF728D0BA0F1314 CRC64;
MGAASGRRGP GLLLPLLLLL PPQPALALDP GLQPGNFSAD EAGAQLFAQS YNSSAEQVLF
QSVAASWAHD TNITAENARR QEEAALLSQE FAEAWGQKAK ELYEPVWQNF TDPQLRRIIG
AVRTLGSANL PLAKRQQYNA LLSNMSRIYS TAKVCLPNKT ATCWSLDPDL TNILASSRSY
AMLLFAWEGW HNAAGIPLKP LYEDFTALSN EAYKQDGFTD TGAYWRSWYN SPTFEDDLEH
LYQQLEPLYL NLHAFVRRAL HRRYGDRYIN LRGPIPAHLL GDMWAQSWEN IYDMVVPFPD
KPNLDVTSTM LQQGWNATHM FRVAEEFFTS LELSPMPPEF WEGSMLEKPA DGREVVCHAS
AWDFYNRKDF RIKQCTRVTM DQLSTVHHEM GHIQYYLQYK DLPVSLRGGA NPGFHEAIGD
VLALSVSTPA HLHKIGLLDN VTNDTESDIN YLLKMALEKI AFLPFGYLVD QWRWGVFSGR
TPNSRYNFDW WYLRTKYQGI CPPVTRNETH FDAGAKFHVP NVTPYIRYFV SFVLQFQFHE
ALCKEAGYEG PLHQCDIYQS TKAGAKLRKV LQAGSSRPWQ EVLKDMVGLD ALDAQPLLKY
FQPVTQWLQE QNQQNGEVLG WPEYQWHPPL PDNYPEGIDL VTDEAEASKF VEEYDRTSQV
VWNEYAEANW NYNTNITTET SKILLQKNMQ IANHTLKYGT QARRFDVNQL QNTTIKRIIK
KVQDLERAAL PAQELEEYNK ILLDMETTYS VATVCHTNGS CLQLEPDLTN VMATSRKYED
LLWAWEGWRD KAGRAILQFY PKYVELINQA ARLNGYVDAG DSWRSMYETP SLEQDLERLF
QELQPLYLNL HAYVRRALHR HYGAQHINLE GPIPAHLLGN MWAQTWSNIY DLVVPFPSAP
SMDTTEAMLK QGWTPRRMFK EADDFFTSLG LLPVPPEFWN KSMLEKPTDG REVVCHASAW
DFYNGKDFRI KQCTTVNLED LVVAHHEMGH IQYFMQYKDL PVALREGANP GFHEAIGDVL
ALSVSTPKHL HSLNLLSSEG GSDEHDINFL MKMALDKIAF IPFSYLVDQW RWRVFDGSIT
KENYNQEWWS LRLKYQGLCP PVPRTQGDFD PGAKFHIPSS VPYIRYFVSF IIQFQFHEAL
CQAAGHTGPL HKCDIYQSKE AGQRLATAMK LGFSRPWPEA MQLITGQPNM SASAMLSYFK
PLLDWLRTEN ELHGEKLGWP QYNWTPNSAR SEGPLPDSGR VSFLGLDLDA QQARVGQWLL
LFLGIALLVA TLGLSQRLFS IRHRSLHRHS HGPQFDSEVE LRHS
