ACE_CHICK
ID ACE_CHICK Reviewed; 1281 AA.
AC Q10751; F1NYM0; J7GZN9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000303|PubMed:7811282};
DE Short=ACE {ECO:0000303|PubMed:7811282};
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 Flags: Precursor;
GN Name=ACE {ECO:0000303|PubMed:7811282}; Synonyms=DCP1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=7811282; DOI=10.1006/bbrc.1994.2894;
RA Esther C.R., Thomas K.E., Bernstein K.E.;
RT "Chicken lacks the testis specific isozyme of angiotensin converting enzyme
RT found in mammals.";
RL Biochem. Biophys. Res. Commun. 205:1916-1921(1994).
RN [2] {ECO:0000312|EMBL:AFP83450.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Peng J., Zhang H.;
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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 (By similarity). 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). Also acts as a regulator of
CC hematopoietic stem cell differentiation by mediating degradation of
CC hemoregulatory peptide N-acetyl-SDKP (AcSDKP) (By similarity).
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 -!- 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 -!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
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DR EMBL; L40175; AAA75554.1; -; mRNA.
DR EMBL; JX218994; AFP83450.1; -; mRNA.
DR EMBL; AADN05000732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JC2489; JC2489.
DR AlphaFoldDB; Q10751; -.
DR SMR; Q10751; -.
DR STRING; 9031.ENSGALP00000039731; -.
DR MEROPS; M02.001; -.
DR MEROPS; M02.004; -.
DR PaxDb; Q10751; -.
DR Ensembl; ENSGALT00000040528; ENSGALP00000039731; ENSGALG00000000498.
DR GeneID; 419953; -.
DR KEGG; gga:419953; -.
DR CTD; 1636; -.
DR VEuPathDB; HostDB:geneid_419953; -.
DR eggNOG; KOG3690; Eukaryota.
DR GeneTree; ENSGT00940000163600; -.
DR HOGENOM; CLU_006219_0_0_1; -.
DR InParanoid; Q10751; -.
DR OMA; PKHLHTI; -.
DR OrthoDB; 422699at2759; -.
DR PhylomeDB; Q10751; -.
DR TreeFam; TF312861; -.
DR Proteomes; UP000000539; Chromosome 27.
DR Bgee; ENSGALG00000000498; Expressed in lung and 7 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IDA:AgBase.
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:0008241; F:peptidyl-dipeptidase activity; IDA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISA:AgBase.
DR GO; GO:0002003; P:angiotensin maturation; ISS:UniProtKB.
DR GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:AgBase.
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:0060319; P:primitive erythrocyte differentiation; IMP:AgBase.
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; 2.
DR Pfam; PF01401; Peptidase_M2; 2.
DR PRINTS; PR00791; PEPDIPTASEA.
DR PROSITE; PS00142; ZINC_PROTEASE; 2.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Cell membrane; Cytoplasm; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Phosphoprotein;
KW Protease; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1281
FT /note="Angiotensin-converting enzyme"
FT /id="PRO_0000078152"
FT TOPO_DOM 18..1241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1242..1262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1263..1281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 18..616
FT /note="Peptidase M2 1"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT REGION 617..1218
FT /note="Peptidase M2 2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT REGION 1201..1240
FT /note="Juxtamembrane stalk"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT ACT_SITE 377
FT /note="Proton acceptor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 506
FT /note="Proton donor 1"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT ACT_SITE 975
FT /note="Proton acceptor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 1104
FT /note="Proton donor 2"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 217
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 376
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 380
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 404
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 515
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 777
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 815
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 974
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 978
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 1002
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 1076
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 1080
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT BINDING 1113
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT SITE 1152..1153
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT SITE 1218..1219
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 145..151
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT DISULFID 743..749
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT DISULFID 943..961
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT DISULFID 1129..1141
FT /evidence="ECO:0000250|UniProtKB:P12821"
FT CONFLICT 616
FT /note="P -> S (in Ref. 1; AAA75554)"
FT CONFLICT 749
FT /note="C -> F (in Ref. 1; AAA75554)"
FT CONFLICT 777
FT /note="R -> W (in Ref. 1; AAA75554)"
SQ SEQUENCE 1281 AA; 147239 MW; 8D601B3C85D0A709 CRC64;
MPAALGLLLP WLSLVGALQP GLEPPQSDPT EAGAVFFASE YNSTAEIVLF RSVSASWEYN
TNLTTANAAL QVEASLEEQN FTELWGKKAK ELYGNIWSNF SDPQLKKIIG SIQTLGPSNL
PLDKRQQYNT ILSDMDKIYS TAKVCLDNGT CWDLEPDISD IMATSRSYKK LLYAWEGWHN
AAGNPLRAKY QEFVTLSNEA YQMDGFEDTG SYWRSWYDST TFEDDLEHLY NQLEPLYLNL
HAFVRRKLYD RYGPKYINLK GPIPAHLLGN MWAQQWNNIY DLMVPYPDKP NLDVTNTMVN
QGWNATHMFR VSEEFFTSLG LLEMPPEFWE KSMLEKPADG REVVCHASAW DFYNRKDFRI
KQCTTVTMEQ LFTVHHEMGH VQYYLQYKDQ PVSFRGGANP GFHEAIGDVL SLSVSTPSHL
QKIGLLSSAV EDEESNINYL LKMALEKIAF LPFGYLIDQW RWNVFSGRTP PSRYNYDWWY
LRTKYQGICA PVSRNESNFD PGAKYHIPGN TPYIRYFVSF ILQFQFHKAL CQAANHTGPL
HTCDIYMSKE AGAKLREVLK AGSSKSWQEI LFNLTGTDKM DAGALLEYFS PVTTWLQEQN
NKTNEVLGWP EFDWRPPIPE GYPEGIDKIV DEAQAKEFLS EYNSTAEVVW NAYTEASWEY
NTNITDHNKE VMLEKNLAMS KHTIEYGMRA RQFDPSDFQD ETVTRILNKL SVLERAALPE
DELKEYNTLL SDMETTYSVA KVCRENNTCH PLDPDLTDIL ATSRDYNELL FAWKGWRDAS
GAKIKDKYKR YVELSNKAAV LNGYTDNGAY WRSLYETPTF EEDLERLYLQ LQPLYLNLHA
YVRRALYNKY GAEHISLKGP IPAHLLGNMW AQSWSNIFDL VMPFPDATKV DATPAMKQQG
WTPKMMFEES DRFFTSLGLI PMPQEFWDKS MIEKPADGRE VVCHASAWDF YNRKDFRIKQ
CTVVNMDDLI TVHHEMGHVQ YFLQYMDQPI SFRDGANPGF HEAIGDVMAL SVSTPKHLHS
INLLDQVTEN EESDINYLMS IALDKIAFLP FGYLMDQWRW KVFDGRIKED EYNQQWWNLR
LKYQGLCPPV PRSEDDFDPG AKFHIPANVP YIRYFVSFVI QFQFHQALCK AAGHTGPLHT
CDIYQSKEAG KLLGDAMKLG FSKPWPEAMQ LITGQPNMSA EALMSYFEPL MTWLVKKNTE
NGEVLGWPEY SWTPYAVTEF HAATDTADFL GMSVGTKQAT AGAWVLLALA LVFLITSIFL
GVKLFSSRRK AFKSSSEMEL K
