ID   ACE_MESAU               Reviewed;        1314 AA.
AC   Q50JE5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000303|PubMed:17343204};
DE            Short=ACE {ECO:0000303|PubMed:17343204};
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:17343204}; Synonyms=Dcp1;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=17343204; DOI=10.1080/10425170600724816;
RA   Uchide T., Fujimori Y., Fukushima U., Uechi M., Sasaki T., Temma K.;
RT   "cDNA cloning of hamster angiotensin-converting enzyme and mRNA
RT   expression.";
RL   DNA Seq. 17:319-325(2006).
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=Q50JE5-1; Sequence=Displayed;
CC       Name=Testis-specific; Synonyms=ACE-T;
CC         IsoId=Q50JE5-2; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Widely expressed with dominant expression in lung
CC       and kidney. {ECO:0000269|PubMed:17343204}.
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-1307; 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; AB212958; BAD98304.1; -; mRNA.
DR   RefSeq; NP_001268510.1; NM_001281581.1. [Q50JE5-1]
DR   AlphaFoldDB; Q50JE5; -.
DR   SMR; Q50JE5; -.
DR   STRING; 10036.ENSMAUP00000016025; -.
DR   MEROPS; M02.001; -.
DR   MEROPS; M02.004; -.
DR   GlyCosmos; Q50JE5; 13 sites, No reported glycans.
DR   GeneID; 101824864; -.
DR   KEGG; maua:101824864; -.
DR   eggNOG; KOG3690; Eukaryota.
DR   OrthoDB; 2898149at2759; -.
DR   BRENDA; 3.4.15.1; 3239.
DR   Proteomes; UP000189706; Unplaced.
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:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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: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:0008217; P:regulation of blood pressure; ISS:UniProtKB.
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   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF27; 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   2: Evidence at transcript level;
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..35
FT                   /evidence="ECO:0000250|UniProtKB:P12821"
FT   CHAIN           36..1314
FT                   /note="Angiotensin-converting enzyme"
FT                   /id="PRO_0000028536"
FT   CHAIN           36..1238
FT                   /note="Angiotensin-converting enzyme, soluble form"
FT                   /evidence="ECO:0000250|UniProtKB:P12821"
FT                   /id="PRO_0000028537"
FT   TOPO_DOM        36..1265
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1266..1282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1283..1314
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          46..630
FT                   /note="Peptidase M2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DOMAIN          649..1228
FT                   /note="Peptidase M2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   REGION          1221..1262
FT                   /note="Juxtamembrane stalk"
FT                   /evidence="ECO:0000250|UniProtKB:P12821"
FT   REGION          1293..1314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        397
FT                   /note="Proton acceptor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   ACT_SITE        526
FT                   /note="Proton donor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   ACT_SITE        995
FT                   /note="Proton acceptor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   ACT_SITE        1124
FT                   /note="Proton donor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         237
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         396
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         400
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         424
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         535
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         797
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         835
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         994
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         998
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         1022
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         1096
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         1100
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   BINDING         1133
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   MOD_RES         1307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12821"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        515
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        683
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        701
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        720
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        766
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        948
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        163..171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DISULFID        365..383
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DISULFID        551..563
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DISULFID        763..769
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DISULFID        963..981
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
FT   DISULFID        1149..1161
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01355"
SQ   SEQUENCE   1314 AA;  151595 MW;  74E29238E87F157E CRC64;
     MGAASGQRGQ GPPSPLLLLW LSLLLLLLPP SPAPALDPGL QPGNFSADEI GAHLFAESYN
     SSAEQVIFQS TVASWAYDTN MTEENARLQE EAELIWQEFA EVWGKKAKEL FDAIRQNFTD
     SKLRRVIETI RTLGPANLPL ARRQQYNSLQ NNMNRIYSTS KVCLPNKTAT CWSLEPELTN
     ILASSRSYAK LLFAWESWHD VVGIPLKPLY QDFTALSNEA YKQDGFSDTG AYWRSAYDSP
     SFEETLEHLY HQLEPLYLNL HAYVRRALHR RYGDKYINLR GPIPAHLLGD MWAQSWDNIY
     DMVVPFPNKP NLDVTNTMVQ KGWNVTHMFR VAEEFFTSMG LSPMPPEFWA ESMLEKPTDG
     REVVCHASAW DFFNRKDFRI KQCTRITMEQ LSTVHHEMGH VQYYLQYKDL TVPLRRGANP
     GFHEAIGDVL ALSVSTPAHL HKIGLLDRVA NDLESDINYL LKMALEKIAF LPFGYLVDQW
     RWGVFSGHTP PSRYNFDWWY FRTKYQGICP PVVRNETHFD AGAKFHIPSG TPYIRYFVSF
     ILQFQFHQAL CKEAGHQGPL HQCDIYQSTQ AGAKLQRVLQ AGYSRPWQEV LKEMVGSDTL
     DAQALLEYFQ PVIRWLQEQN QRNGEVLGWP EYQWRPPLPD NYPEGIDLVT DETEAERFVE
     EYDRTARVLW NEYAEANWQY NTNITLEASK ILLQKNKKVA NHTLKYGTLA KKFDVSNFQN
     YTIKRIIKKV QNMDRAVLPP KELEEYNQIL MDMETTYSIA NVCYLNGTCL HLEPDLTNVM
     ATSRKYEELL WVWKSWRDKV GRAILPLFPK YVELSNKIAH LNGYADGGDS WRSSYESKSL
     EQDLEQLYQE LQPLYLNLHA YVRRSLHRHY GSQHINLDGP IPAHLLGNMW AQTWSNIYDL
     VAPFPSAPNL DATEAMIKQG WTPRRIFKEA DDFFTSLGLL PVSEEFWNKS MLEKPGDGRE
     VVCHASAWDF YNGKDFRIKQ CTSVNMEDLV IAHHEMGHIQ YFMQYKDLPV TFREGANPGF
     HEAIGDVLAL SVSTPKHLHS LNLLSSEGGG YEHDINFLMK MALDKIAFIP FSYLIDQWRW
     RVFDGSITKE NYNQEWWSLR LKYQGLCPPV PRSQDDFDPG SKFHVPANVP YIRYFVSFII
     QFQFHEALCR AAGHTGPLHK CDIYQSKEAG KLLADTMKMG YSKPWPEAMK LITGQPNMSA
     SAMMNYFKPL TEWLVTENRR HGETLGWPEY NWTPNTARSE GPFPESGRVN FLGMYLEPQQ
     ARVGQWVLLF LGVSLLVATL GLTHRLFSIR QHGHSLHRPH RGPQFGSEVE LRHS
//