ID   ENTP1_PIG               Reviewed;         510 AA.
AC   Q9MYU4;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1 {ECO:0000250|UniProtKB:P49961};
DE            EC=3.6.1.5 {ECO:0000269|PubMed:10866813};
DE   AltName: Full=ATP diphosphohydrolase {ECO:0000250|UniProtKB:P49961};
DE            Short=ATP-DPH {ECO:0000250|UniProtKB:P49961};
DE            Short=ATPDase {ECO:0000250|UniProtKB:P49961};
DE   AltName: Full=Ecto-ATP diphosphohydrolase 1 {ECO:0000250|UniProtKB:P49961};
DE            Short=Ecto-ATPDase 1;
DE            Short=Ecto-ATPase 1;
DE   AltName: Full=Ecto-apyrase {ECO:0000250|UniProtKB:P49961};
DE   AltName: Full=Lymphoid cell activation antigen {ECO:0000250|UniProtKB:P49961};
DE   AltName: Full=Nucleoside triphosphate diphosphohydrolase 1 {ECO:0000250|UniProtKB:P97687};
DE            Short=NTPDase1 {ECO:0000250|UniProtKB:P97687};
DE   AltName: CD_antigen=CD39 {ECO:0000303|PubMed:8955160};
DE   Contains:
DE     RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1 27 kDa subunit {ECO:0000305|PubMed:10866813};
DE   Contains:
DE     RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1 54 kDa subunit {ECO:0000305|PubMed:10866813};
GN   Name=ENTPD1 {ECO:0000250|UniProtKB:P49961};
GN   Synonyms=CD39 {ECO:0000303|PubMed:8955160};
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 [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, SUBUNIT,
RP   FUNCTION, CATALYTIC ACTIVITY, AND PTM.
RC   TISSUE=Aortic endothelium;
RX   PubMed=10866813; DOI=10.1046/j.1432-1327.2000.01462.x;
RA   Lemmens R., Vanduffel L., Kittel A., Beaudoin A.R., Benrezzak O.,
RA   Sevigny J.;
RT   "Distribution, cloning, and characterization of porcine nucleoside
RT   triphosphate diphosphohydrolase-1.";
RL   Eur. J. Biochem. 267:4106-4114(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 202-220.
RC   TISSUE=Pancreas;
RX   PubMed=8955160; DOI=10.1074/jbc.271.51.33116;
RA   Kaczmarek E., Koziak K., Sevigny J., Siegel J.B., Anrather J.,
RA   Beaudoin A.R., Bach F.H., Robson S.C.;
RT   "Identification and characterization of CD39/vascular ATP
RT   diphosphohydrolase.";
RL   J. Biol. Chem. 271:33116-33122(1996).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC   TISSUE=Umbilical vein;
RX   PubMed=8996251; DOI=10.1084/jem.185.1.153;
RA   Robson S.C., Kaczmarek E., Siegel J.B., Candinas D., Koziak K., Millan M.,
RA   Hancock W.W., Bach F.H.;
RT   "Loss of ATP diphosphohydrolase activity with endothelial cell
RT   activation.";
RL   J. Exp. Med. 185:153-163(1997).
CC   -!- FUNCTION: Catalyzes the hydrolysis of both di- and triphosphate
CC       nucleotides (NDPs and NTPs) and hydrolyze NTPs to nucleotide
CC       monophosphates (NMPs) in two distinct successive phosphate-releasing
CC       steps, with NDPs as intermediates and participates in the regulation of
CC       extracellular levels of nucleotides (PubMed:10866813, PubMed:8996251).
CC       By hydrolyzing proinflammatory ATP and platelet-activating ADP to AMP,
CC       it blocks platelet aggregation and supports blood flow
CC       (PubMed:8996251). {ECO:0000269|PubMed:10866813,
CC       ECO:0000269|PubMed:8996251}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside
CC         5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5;
CC         Evidence={ECO:0000269|PubMed:10866813};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36796;
CC         Evidence={ECO:0000269|PubMed:10866813};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557;
CC         Evidence={ECO:0000269|PubMed:10866813};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681;
CC         Evidence={ECO:0000269|PubMed:10866813};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-
CC         phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:58043;
CC         Evidence={ECO:0000269|PubMed:10866813, ECO:0000269|PubMed:8996251};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800;
CC         Evidence={ECO:0000269|PubMed:10866813, ECO:0000269|PubMed:8996251};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 2 H2O = AMP + 2 H(+) + 2 phosphate;
CC         Xref=Rhea:RHEA:20988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:10866813};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20989;
CC         Evidence={ECO:0000269|PubMed:10866813};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:10866813};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000269|PubMed:10866813};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:10866813, ECO:0000269|PubMed:8996251};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC         Evidence={ECO:0000269|PubMed:10866813, ECO:0000269|PubMed:8996251};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + 2 H2O = CMP + 2 H(+) + 2 phosphate;
CC         Xref=Rhea:RHEA:64908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:60377;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64909;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + H2O = CDP + H(+) + phosphate; Xref=Rhea:RHEA:29387,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58069;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29388;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP + H2O = CMP + H(+) + phosphate; Xref=Rhea:RHEA:64880,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58069, ChEBI:CHEBI:60377;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + 2 H2O = GMP + 2 H(+) + 2 phosphate;
CC         Xref=Rhea:RHEA:64904, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64905;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58115, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O + ITP = 2 H(+) + IMP + 2 phosphate;
CC         Xref=Rhea:RHEA:77735, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:61402;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77736;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + ITP = H(+) + IDP + phosphate; Xref=Rhea:RHEA:28330,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58280, ChEBI:CHEBI:61402;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28331;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:58280;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O + UTP = 2 H(+) + 2 phosphate + UMP;
CC         Xref=Rhea:RHEA:64896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865;
CC         Evidence={ECO:0000250|UniProtKB:P97687};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64897;
CC         Evidence={ECO:0000250|UniProtKB:P97687};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UTP = H(+) + phosphate + UDP; Xref=Rhea:RHEA:64900,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:58223;
CC         Evidence={ECO:0000250|UniProtKB:P97687};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64901;
CC         Evidence={ECO:0000250|UniProtKB:P97687};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:58223;
CC         Evidence={ECO:0000250|UniProtKB:P97687};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877;
CC         Evidence={ECO:0000250|UniProtKB:P97687};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
CC   -!- ACTIVITY REGULATION: The ATP diphosphohydrolase activity is decreased
CC       by half by sodium azide. {ECO:0000269|PubMed:8996251}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000305|PubMed:10866813}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P49961}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:P49961}. Membrane, caveola
CC       {ECO:0000250|UniProtKB:P49961}.
CC   -!- TISSUE SPECIFICITY: Highest expression found in vascular endothelium,
CC       smooth muscle, spleen and lung (at protein level) (PubMed:10866813).
CC       High expression also found in stomach, duodenum, kidney, lymph node and
CC       aorta (at protein level) (PubMed:10866813).
CC       {ECO:0000269|PubMed:10866813}.
CC   -!- PTM: N-glycosylated. {ECO:0000305|PubMed:10866813}.
CC   -!- PTM: Cleaved into two polypeptides that seem to stay together by non-
CC       covalent interactions. {ECO:0000269|PubMed:10866813}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:P49961}.
CC   -!- PTM: Palmitoylated on Cys-13; which is required for caveola targeting.
CC       {ECO:0000250|UniProtKB:P49961}.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR   EMBL; AJ133746; CAB95871.1; -; mRNA.
DR   RefSeq; NP_999318.1; NM_214153.1.
DR   AlphaFoldDB; Q9MYU4; -.
DR   SMR; Q9MYU4; -.
DR   STRING; 9823.ENSSSCP00000011184; -.
DR   GlyCosmos; Q9MYU4; 7 sites, No reported glycans.
DR   PaxDb; 9823-ENSSSCP00000011184; -.
DR   PeptideAtlas; Q9MYU4; -.
DR   GeneID; 397298; -.
DR   KEGG; ssc:397298; -.
DR   CTD; 953; -.
DR   eggNOG; KOG1386; Eukaryota.
DR   InParanoid; Q9MYU4; -.
DR   OrthoDB; 180318at2759; -.
DR   BRENDA; 3.6.1.5; 6170.
DR   SABIO-RK; Q9MYU4; -.
DR   ChiTaRS; ENTPD1; pig.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043262; F:ADP phosphatase activity; IEA:RHEA.
DR   GO; GO:0004050; F:apyrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0036384; F:CDP phosphatase activity; IEA:RHEA.
DR   GO; GO:0043273; F:CTPase activity; IEA:RHEA.
DR   GO; GO:0004382; F:GDP phosphatase activity; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR   GO; GO:1990003; F:IDP phosphatase activity; IEA:RHEA.
DR   GO; GO:0103023; F:ITPase activity; IEA:RHEA.
DR   GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0045134; F:UDP phosphatase activity; IBA:GO_Central.
DR   GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR   GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR11782:SF32; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 1; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..510
FT                   /note="Ectonucleoside triphosphate diphosphohydrolase 1"
FT                   /id="PRO_0000019905"
FT   CHAIN           1..201
FT                   /note="Ectonucleoside triphosphate diphosphohydrolase 1 27
FT                   kDa subunit"
FT                   /id="PRO_0000019906"
FT   CHAIN           202..510
FT                   /note="Ectonucleoside triphosphate diphosphohydrolase 1 54
FT                   kDa subunit"
FT                   /evidence="ECO:0000269|PubMed:8955160"
FT                   /id="PRO_0000019907"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..477
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        478..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        499..510
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O35795"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        84..108
FT                   /evidence="ECO:0000250|UniProtKB:P97687"
FT   DISULFID        255..300
FT                   /evidence="ECO:0000250|UniProtKB:P97687"
FT   DISULFID        281..324
FT                   /evidence="ECO:0000250|UniProtKB:P97687"
FT   DISULFID        337..342
FT                   /evidence="ECO:0000250|UniProtKB:P97687"
FT   DISULFID        390..413
FT                   /evidence="ECO:0000250|UniProtKB:P97687"
FT   CONFLICT        203
FT                   /note="G -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   510 AA;  57757 MW;  82F86869040D7735 CRC64;
     MEDRRESELK TFCSKNILVI LGFSSIIAVI ALLALGLTQN KPLPENVKFG IVLDAGSSHT
     SLYIYKWPAE KENDTGVVSQ VEECKLKGPG ISEFAKKLGE IDIYLEACME RARTVVPKSQ
     HAETPVYLGA TAGMRLLRMK NENLASKILS TVAESITRYP FDFQGARIIT GQEEGAYGWI
     TINYLLDKFI QKSGWFNLKP RKGDTQETYG ALDLGGASTQ ITFVPQNQVL ESPENTLHFR
     LYGKNYSVYT HSFLCYGKDQ ALLQKLTKDL KNTNGTIHEP CFHSGYQRRM NVSHLYEAPC
     TRRFLTSLPF PELEIQGTGD FQKCQQSIRP LFNTSYCPYS RCSFDGVFLP LPQGDFAAFS
     AFYYVMGFLN LTSEEGSFQS KVTSTLEAFC SRPWAELQMY FGDVKEKYLS EYCFSGTYIL
     TLLLSGYHFT AETWKNIHFM GKVQSTSVGW TLGYMLNLTN MIPSEEPSST RLSHSTYVFL
     MVLFSLILVI VVIIGLFVCH RPSYFWKDMV
//