ACE_BOVIN
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 03-AUG-2022, entry version 116.
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 = 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 -!- 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 AlphaFoldDB; P12820; -.
DR SMR; P12820; -.
DR IntAct; P12820; 1.
DR MINT; P12820; -.
DR STRING; 9913.ENSBTAP00000047966; -.
DR MEROPS; M02.001; -.
DR PaxDb; P12820; -.
DR Ensembl; ENSBTAT00000061106.3; ENSBTAP00000053314.3; ENSBTAG00000024950.6.
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 OrthoDB; 422699at2759; -.
DR BRENDA; 3.4.15.1; 908.
DR Proteomes; UP000009136; Chromosome 19.
DR Proteomes; UP000009136; Unplaced.
DR Bgee; ENSBTAG00000024950; Expressed in spermatid and 101 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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: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; 1.
DR Pfam; PF01401; Peptidase_M2; 1.
DR PRINTS; PR00791; PEPDIPTASEA.
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 REGION 30..630
FT /note="Peptidase M2 1"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT REGION 631..1232
FT /note="Peptidase M2 2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
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:0000250|UniProtKB:P12821"
FT ACT_SITE 520
FT /note="Proton donor 1"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT ACT_SITE 989
FT /note="Proton acceptor 2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT ACT_SITE 1118
FT /note="Proton donor 2"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 231
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 390
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 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 418
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 529
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 791
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 829
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 988
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 992
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 1016
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 1090
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 1094
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 1127
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P12821"
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:0000250|UniProtKB:P12821"
FT DISULFID 757..763
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT DISULFID 957..975
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT DISULFID 1143..1155
FT /evidence="ECO:0000250|UniProtKB:P12821"
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
