ID   ACE_BOVIN               Reviewed;        1306 AA.
AC   P12820; F1MQJ0; Q0GA41;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 3.
DT   04-NOV-2026, entry version 135.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000303|PubMed:3028395};
DE            Short=ACE {ECO:0000303|PubMed:3028395};
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:3028395}; Synonyms=DCP1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
RA   Mungunsukh O., Day R.M.;
RT   "Analysis of the angiotensin converting enzyme promoter from Bos taurus.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 29-50.
RC   TISSUE=Lung;
RX   PubMed=3028395; DOI=10.1016/s0006-291x(86)80138-3;
RA   St Clair D.K., Presper K.A., Smith P.L., Stump D.C., Heath E.C.;
RT   "Bovine angiotensin-converting enzyme: amino-terminal sequence analysis and
RT   preliminary characterization of a hybridization-selected primary
RT   translation product.";
RL   Biochem. Biophys. Res. Commun. 141:968-972(1986).
RN   [4]
RP   PROTEIN SEQUENCE OF 29-50.
RX   PubMed=2835538; DOI=10.1038/ki.1988.48;
RA   Bernstein K.E., Martin B.M., Striker L., Striker G.;
RT   "Partial protein sequence of mouse and bovine kidney angiotensin converting
RT   enzyme.";
RL   Kidney Int. 33:652-655(1988).
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   -!- 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 = L-histidyl-L-leucine + angiotensin II;
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 = L-Phe-L-Arg + bradykinin(1-7);
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=substance P + H2O = substance P(1-9) + L-Leu-L-Met-NH2;
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=substance P + H2O = substance P(1-8) + Gly-L-Leu-L-Met-NH2;
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=substance P + H2O = 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=neurotensin + H2O = neurotensin(1-11) + L-isoleucyl-L-leucine;
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 = N-acetyl-L-seryl-L-aspartate + L-lysyl-L-
CC         proline; Xref=Rhea:RHEA:71455, ChEBI:CHEBI:15377, ChEBI:CHEBI:190701,
CC         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=Met-enkephalin + H2O = 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=Leu-enkephalin + H2O = L-tyrosylglycylglycine + L-
CC         phenylalanyl-L-leucine; 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=Met-enkephalin-Arg-Phe + H2O = 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   -!- 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:
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   -!- 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   -!- 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   -!- 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-1299; 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; DQ885942; ABI35897.2; -; Genomic_DNA.
DR   PIR; A26376; A26376.
DR   RefSeq; NP_001193597.1; NM_001206668.1.
DR   AlphaFoldDB; P12820; -.
DR   SMR; P12820; -.
DR   FunCoup; P12820; 4.
DR   IntAct; P12820; 1.
DR   STRING; 9913.ENSBTAP00000053314; -.
DR   MEROPS; M02.001; -.
DR   GlyCosmos; P12820; 16 sites, No reported glycans.
DR   GlyGen; P12820; 16 sites.
DR   PaxDb; 9913-ENSBTAP00000053314; -.
DR   Ensembl; ENSBTAT00000150312.1; ENSBTAP00000106585.1; ENSBTAG00000024950.8.
DR   Ensembl; ENSBTAT00085023370; ENSBTAP00085003360; ENSBTAG00085028575.
DR   GeneID; 509484; -.
DR   KEGG; bta:509484; -.
DR   CTD; 1636; -.
DR   VEuPathDB; HostDB:ENSBTAG00000024950; -.
DR   VGNC; VGNC:107264; ACE.
DR   eggNOG; KOG3690; Eukaryota.
DR   GeneTree; ENSGT00940000162051; -.
DR   InParanoid; P12820; -.
DR   OMA; AADYMMN; -.
DR   OrthoDB; 10029630at2759; -.
DR   BRENDA; 3.4.15.1; 908.
DR   Reactome; R-BTA-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000024950; Expressed in spermatid and 101 other cell types or tissues.
DR   ExpressionAtlas; P12820; baseline.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0031711; F:bradykinin receptor binding; IEA:Ensembl.
DR   GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB.
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:0051019; F:mitogen-activated protein kinase binding; IEA:Ensembl.
DR   GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IEA:Ensembl.
DR   GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; ISS:UniProtKB.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0050435; P:amyloid-beta metabolic process; IEA:Ensembl.
DR   GO; GO:0002003; P:angiotensin maturation; ISS:UniProtKB.
DR   GO; GO:0038166; P:angiotensin-activated signaling pathway; IEA:Ensembl.
DR   GO; GO:0050482; P:arachidonate secretion; IEA:Ensembl.
DR   GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
DR   GO; GO:0071838; P:cell proliferation in bone marrow; IEA:Ensembl.
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:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:1903597; P:negative regulation of gap junction assembly; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IBA:GO_Central.
DR   GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0060177; P:regulation of angiotensin metabolic process; IEA:Ensembl.
DR   GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR   GO; GO:1902033; P:regulation of hematopoietic stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR   GO; GO:0010814; P:substance P catabolic process; ISS:UniProtKB.
DR   CDD; cd06461; M2_ACE; 2.
DR   FunFam; 1.10.1370.30:FF:000004; Angiotensin-converting enzyme; 2.
DR   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF25; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01401; Peptidase_M2; 2.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
DR   PROSITE; PS52011; PEPTIDASE_M2; 2.
DR   PROSITE; PS00142; ZINC_PROTEASE; 2.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Carboxypeptidase; Cell membrane; Cytoplasm;
KW   Direct protein sequencing; 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..28
FT                   /evidence="ECO:0000269|PubMed:2835538,
FT                   ECO:0000269|PubMed:3028395"
FT   CHAIN           29..1306
FT                   /note="Angiotensin-converting enzyme"
FT                   /id="PRO_0000078151"
FT   CHAIN           29..1232
FT                   /note="Angiotensin-converting enzyme, soluble form"
FT                   /evidence="ECO:0000250|UniProtKB:P12821"
FT                   /id="PRO_0000455834"
FT   TOPO_DOM        29..1256
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1257..1277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1278..1306
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          40..624
FT                   /note="Peptidase M2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DOMAIN          643..1222
FT                   /note="Peptidase M2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   REGION          1215..1256
FT                   /note="Juxtamembrane stalk"
FT                   /evidence="ECO:0000250|UniProtKB:P12821"
FT   ACT_SITE        391
FT                   /note="Proton acceptor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   ACT_SITE        520
FT                   /note="Proton donor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   ACT_SITE        989
FT                   /note="Proton acceptor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   ACT_SITE        1118
FT                   /note="Proton donor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         231
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         390
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         394
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         418
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         529
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         791
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         829
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         988
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         992
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         1016
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         1090
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         1094
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         1127
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   SITE            1232..1233
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:P12821"
FT   MOD_RES         1299
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12821"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        509
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        523
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        673
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        695
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        714
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        760
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        942
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        157..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DISULFID        359..377
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DISULFID        545..557
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DISULFID        757..763
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DISULFID        957..975
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DISULFID        1143..1155
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
SQ   SEQUENCE   1306 AA;  150097 MW;  6F780FF27D21CE51 CRC64;
     MGAASGRRSP PLLLPLLLLL LPPPPVILEL DPALQPGNFP ADEAGAQIFA ASFNSSAEQV
     LFQSTAASWA HDTNITEENA RLQEEAALLS QEFSEAWGQK AKDLFDPVWQ NFTDPTLLRI
     IGAVRTLGPA NLDLEKRQKY NSLLSNMSRI YSTAKVCFPN KTAPCWSLDP ELTNILASSR
     SYTLLLYAWE GWHNAAGIPL KPLYQDFTAL SNEAYKQDGF SDTGAYWRSW YDSPTFTEDL
     ERLYQQLEPL YLNLHAYVRR ALHRRYGDRY INLRGPIPAH LLGNMWAQSW ENIYDTVVPF
     PDKPNLDVTD VMVQKGWNAT HMFRVAEEFF TSLGLLPMPP EFWAESMLEK PSDGREVVCH
     ASAWDFYNRK DFRIKQCTRV TMDQLSTVHH EMGHVQYYLQ YKGQHVSLRR GANPGFHEAI
     GDVLALSVST PAHLHKIGLL DQVTNDTESD INYLLKMALE KIAFLPFGYL VDQWRWGVFS
     GRTPPSRYNY DWWYLRTKYQ GICPPVVRNE THFDAGAKFH VPNVTPYIRY FVSFVLQFQF
     HEALCKEAGH QGPLHQCDIY QSTQAGAKLR ALLQAGSSRP WQEVLKDMVG SDNLDARPLL
     SYFQPVTQWL EEQNQQNGEV LGWPEYQWRP PMPDNYPEGI DLVSDEDEAR KFVEEYDRRS
     QVVWNEYAEA NWNYSTDIST DNSKLLMEKN LQMANHTVKY GTWARKFDVT NFQNATMKRM
     IKKIQDLERA ALPTKELEEY NQILLDMETV YSVASVCHEN GTCLRLEPDL TNLMATSRNY
     QDLAWAWKSW RDKVGRSILP YFPKYVELTN KAARLNGYQD GGDSWRSMYE MPFLEEELEQ
     LFQELQPLYL NLHAYVRRAL HRHYGPDVIN LEGPIPAHLL GNMWAQSWSN IYDLVAPFPS
     APKMDATEAM IKQGWTPLRM FKEADNFFTS LGLLPMPPEF WNKSMLEKPT DGREVVCHAS
     AWDFFNGKDF RIKQCTSVNM EDLVVAHHEM GHIQYFMQYK DLPVTFREGA NPGFHEAIGD
     VLALSVSTPT HLHKINLLSS GDGGYEEDIN FLMKMALEKI AFIPFSFLVD QWRWRVFDGS
     VTRENYNQEW WSLRLKYQGV CPPLARSQDD FDPGAKFHIP ASVPYVRYFV SFVIQFQFHQ
     ALCQAAGHQG PLHKCDIYQS KEAGKLLADA MKLGFSQPWP EAMRLITGQS NMSAAAMMTY
     FKPLLDWLVT ENGRHGEKLG WPQYNWTPNS ARLEGPFVGS GRVNFLGLNL EEQQARVGQW
     VLLFLGVALL VATLGLTQRL FSIRHHSLRR PHRGPQFGSE VELRHS
//