ACE_PIG
ID ACE_PIG Reviewed; 1309 AA.
AC F1RRW5;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 3.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000305};
DE Short=ACE {ECO:0000250|UniProtKB:P12821};
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 Contains:
DE RecName: Full=Angiotensin-converting enzyme, soluble form {ECO:0000250|UniProtKB:P12821};
DE Flags: Precursor;
GN Name=ACE {ECO:0000250|UniProtKB:P12821};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc;
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=4962200; DOI=10.1016/0024-3205(67)90090-2;
RA Erdos E.G., Yang H.Y.;
RT "An enzyme in microsomal fraction of kidney that inactivates bradykinin.";
RL Life Sci. 6:569-574(1967).
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 (By
CC similarity). Composed of two similar catalytic domains, each possessing
CC a functional active site, with different selectivity for substrates (By
CC similarity). Plays a major role in the angiotensin-renin system that
CC regulates blood pressure and sodium retention by the kidney by
CC converting angiotensin I to angiotensin II, resulting in an increase of
CC the vasoconstrictor activity of angiotensin (By similarity). Also able
CC to inactivate bradykinin, a potent vasodilator, and therefore enhance
CC the blood pressure response (PubMed:4962200). Acts as a regulator of
CC synaptic transmission by mediating cleavage of neuropeptide hormones,
CC such as substance P, neurotensin or enkephalins (By similarity).
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 (By similarity). Met-enkephalin-
CC Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long-
CC term synaptic potentiation of glutamate release (By similarity). Also
CC acts as a regulator of hematopoietic stem cell differentiation by
CC mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP)
CC (By similarity). Acts as a regulator of cannabinoid signaling pathway
CC by mediating degradation of hemopressin, an antagonist peptide of the
CC cannabinoid receptor CNR1 (By similarity). Involved in amyloid-beta
CC metabolism by catalyzing degradation of Amyloid-beta protein 40 and
CC Amyloid-beta protein 42 peptides, thereby preventing plaque formation
CC (By similarity). Catalyzes cleavage of cholecystokinin (maturation of
CC Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both
CC maturation and degradation) hormones (By similarity). Degradation of
CC hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins
CC is mediated by the N-terminal catalytic domain, while angiotensin I and
CC cholecystokinin cleavage is mediated by the C-terminal catalytic region
CC (By similarity). {ECO:0000250|UniProtKB:P09470,
CC ECO:0000250|UniProtKB:P12821, ECO:0000269|PubMed:4962200}.
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 = 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:0000305|PubMed:4962200};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71452;
CC Evidence={ECO:0000305|PubMed:4962200};
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 -!- 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-1302; 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; AEMK02000080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; F1RRW5; -.
DR STRING; 9823.ENSSSCP00000030627; -.
DR BindingDB; F1RRW5; -.
DR ChEMBL; CHEMBL4523113; -.
DR PeptideAtlas; F1RRW5; -.
DR PRIDE; F1RRW5; -.
DR Ensembl; ENSSSCT00000018828.4; ENSSSCP00000018326.3; ENSSSCG00000017296.5.
DR eggNOG; KOG3690; Eukaryota.
DR GeneTree; ENSGT00940000162051; -.
DR HOGENOM; CLU_006219_0_0_1; -.
DR Reactome; R-SSC-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Proteomes; UP000008227; Chromosome 12.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000017296; Expressed in testis and 43 other tissues.
DR ExpressionAtlas; F1RRW5; baseline and differential.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031711; F:bradykinin receptor binding; IEA:Ensembl.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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; IDA: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:0050482; P:arachidonic acid secretion; IEA:Ensembl.
DR GO; GO:0010815; P:bradykinin catabolic process; IDA:UniProtKB.
DR GO; GO:0071838; P:cell proliferation in bone marrow; IEA:Ensembl.
DR GO; GO:0060047; P:heart contraction; 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:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR GO; GO:0002446; P:neutrophil mediated immunity; IEA:Ensembl.
DR GO; GO:2000170; P:positive regulation of peptidyl-cysteine S-nitrosylation; IEA:Ensembl.
DR GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; 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:1902033; P:regulation of hematopoietic stem cell proliferation; IEA:Ensembl.
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:0007283; P:spermatogenesis; IEA:Ensembl.
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 1: Evidence at protein level;
KW Calmodulin-binding; Carboxypeptidase; Cell membrane; Cytoplasm;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Phosphoprotein; Protease; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1309
FT /note="Angiotensin-converting enzyme"
FT /id="PRO_5013039630"
FT CHAIN 34..1235
FT /note="Angiotensin-converting enzyme, soluble form"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT /id="PRO_0000455961"
FT TOPO_DOM 34..1259
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1260..1280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1281..1309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 34..633
FT /note="Peptidase M2 1"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT REGION 634..1235
FT /note="Peptidase M2 2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT REGION 1218..1259
FT /note="Juxtamembrane stalk"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT ACT_SITE 395
FT /note="Proton acceptor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 523
FT /note="Proton donor 1"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT ACT_SITE 992
FT /note="Proton acceptor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 1121
FT /note="Proton donor 2"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 235
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 394
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 398
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 422
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 532
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 794
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 832
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 991
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 995
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 1019
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 1093
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 1097
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 1130
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT SITE 1236..1237
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..169
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT DISULFID 760..766
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT DISULFID 960..978
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT DISULFID 1146..1158
FT /evidence="ECO:0000250|UniProtKB:P12821"
SQ SEQUENCE 1309 AA; 150312 MW; 051472DD687F702A CRC64;
MGAASGCRWP WPPLLPLLLM LLLPPPPLPV ALALDSALQP GNFTADEAGA EDFAQSFNSS
SEQVLFQSTA ASWAHDTNIT EENARRQEEA ALISQEFSEV WGQKAKALYD PIWQNFTSRT
LRRIIGVVRT LGSANLSPAK RQQYNSLLSN MTRIYSTAKV CFPNKTATCW SLDPELTNIL
ATSRSYTLLL YAWEGWHNAA GIPLKPLYQD FTALSNEAYK QDGFSDTGAY WRSLYDSPTF
TEDLERLYHQ LEPLYLNLHA YVRRALHRQY GDRFINLRGP IPAHLLGNMW AQSWNNIYDM
VVPFPGKPSL DVTSAMVQKG WNVTHMFRVA EEFFTSLGLL PMPPEFWAES MLEKPSDGRE
VVCHASAWDF YNRKDFRIKQ CTQVTMDQLS TVHHEMGHVQ YYLQYKDQHV SLRRGANPGF
HEAIGDVLAL SVSTPAHLHK IGLLDHVTSD WESDINYLLK MALEKIAFLP FGYLVDQWRW
GVFSGRTPPL YNYDWWYLRT KYQGVCPPVV RNETHFDAGA KYHVPNVTPY IRYFVSFILQ
FQFHQALCKE AGHQGPLHQC DIYQSTRAGA KLRAVLQAGS SRPWQEVLKD MVGSGALDAQ
PLLDYFQPVT QWLEEQNQRS GDILGWPEYQ WRPPMPDNYP EGIDLVSDEA EASKFVEEYD
RRSQVVLNEY AEANWDYNTN ITAEGSKRVL EKSTQMANHT VKYGIWARKF DVANIQNFTL
KRMIKKIQDL ERAALPFKEL EEYNQILLDM ETAYSVASVC HANSTCLQLE PDLTNLMATS
RSYEELLWAW KGWRDKVGRA ILPYFPKYVE LTNKAARLNG YEDGGDAWRA AYEMPFLEQE
LEQLFQELQP LYLNLHAYVR RALHHHYGPE HINLEGPIPA HLLGNMWAQT WSNIYDLVVP
FPSASKMDAS EAMINQGWTP QRMFKEADNF FTSLGLLPVP PEFWNKSMLE KPTDGREVVC
HASAWDFFNG KDFRIKQCTT VNMEDLVVAH HEMGHIQYFM QYKDLPVTFR EGANPGFHEA
IGDVLALSVS TPKHLRSINL LKSEDDGYEE DINFLMKMAL DKVAFVPFSY LVDQWRWRVF
DRSITKENYN QEWWSLRLKY QGLCPPVARS QGDFDPGAKF HIPSSVPYIR YFVSFIIQFQ
FHEALCQAAG HKGPLHKCDI YQSKEAGRRL ADAMKLGLSK PWPEAMQLIT GQPNVSASAM
MTYFKPLLDW LVTENGRHGE KLGWPQYNWT PNSARLEGSF AGTGRVNFLG LNLEEQQARV
GQWVLLFLGV TLLVATMGLT QRLFSIRHQI LRRTHRGPQF GSEVELRHS
