ACE_MESAU
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 03-AUG-2022, entry version 78.
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.XP_005070087.1; -.
DR MEROPS; M02.001; -.
DR MEROPS; M02.004; -.
DR GeneID; 101824864; -.
DR eggNOG; KOG3690; Eukaryota.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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 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 REGION 36..636
FT /note="Peptidase M2 1"
FT REGION 637..1238
FT /note="Peptidase M2 2"
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:PRU10095"
FT ACT_SITE 526
FT /note="Proton donor 1"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT ACT_SITE 995
FT /note="Proton acceptor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 1124
FT /note="Proton donor 2"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 237
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 396
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 400
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 424
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 535
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 797
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 835
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 994
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 998
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 1022
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 1096
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 1100
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 1133
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P12821"
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:0000250|UniProtKB:P12821"
FT DISULFID 763..769
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT DISULFID 963..981
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT DISULFID 1149..1161
FT /evidence="ECO:0000250|UniProtKB:P12821"
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
