ID   ENTP1_MOUSE             Reviewed;         510 AA.
AC   P55772;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 1 {ECO:0000305};
DE            Short=NTPDase 1;
DE            EC=3.6.1.5 {ECO:0000250|UniProtKB:P49961};
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:0000303|PubMed:7930580};
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:7930580};
GN   Name=Entpd1 {ECO:0000312|MGI:MGI:102805};
GN   Synonyms=Cd39 {ECO:0000303|PubMed:7930580};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7930580;
RA   Maliszewski C.R., Delespesse G.J.T., Schoenborn M.A., Armitage R.J.,
RA   Fanslow W.C., Nakajima T., Baker E., Sutherland G.R., Poindexter K.,
RA   Birks C., Alpert A., Friend D., Gimpel S.D., Gayle R.B. III;
RT   "The CD39 lymphoid cell activation antigen. Molecular cloning and
RT   structural characterization.";
RL   J. Immunol. 153:3574-3583(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=9730622; DOI=10.1159/000015049;
RA   Schoenborn M.A., Jenkins N.A., Copeland N.G., Gilbert D.J., Gayle R.B. III,
RA   Maliszewski C.R.;
RT   "Gene structure and chromosome location of mouse Cd39 coding for an ecto-
RT   apyrase.";
RL   Cytogenet. Cell Genet. 81:287-289(1998).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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. By hydrolyzing proinflammatory ATP
CC       and platelet-activating ADP to AMP, it blocks platelet aggregation and
CC       supports blood flow. {ECO:0000250|UniProtKB:P49961}.
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36796;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20989;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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:0000250|UniProtKB:P49961};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC         Evidence={ECO:0000250|UniProtKB:P49961};
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   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q9MYU4}.
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   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P97687}.
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; AF037366; AAB92259.1; -; mRNA.
DR   EMBL; AF041818; AAC83203.1; -; Genomic_DNA.
DR   EMBL; AF041812; AAC83203.1; JOINED; Genomic_DNA.
DR   EMBL; AF041813; AAC83203.1; JOINED; Genomic_DNA.
DR   EMBL; AF041814; AAC83203.1; JOINED; Genomic_DNA.
DR   EMBL; AF041815; AAC83203.1; JOINED; Genomic_DNA.
DR   EMBL; AF041816; AAC83203.1; JOINED; Genomic_DNA.
DR   EMBL; AF041817; AAC83203.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS50434.1; -.
DR   RefSeq; NP_033978.1; NM_009848.4.
DR   AlphaFoldDB; P55772; -.
DR   SMR; P55772; -.
DR   STRING; 10090.ENSMUSP00000116285; -.
DR   BindingDB; P55772; -.
DR   ChEMBL; CHEMBL4739681; -.
DR   GlyCosmos; P55772; 6 sites, No reported glycans.
DR   GlyGen; P55772; 6 sites.
DR   iPTMnet; P55772; -.
DR   PhosphoSitePlus; P55772; -.
DR   SwissPalm; P55772; -.
DR   EPD; P55772; -.
DR   jPOST; P55772; -.
DR   PaxDb; 10090-ENSMUSP00000107850; -.
DR   ProteomicsDB; 275457; -.
DR   Antibodypedia; 2888; 1077 antibodies from 43 providers.
DR   DNASU; 12495; -.
DR   Ensembl; ENSMUST00000112231.9; ENSMUSP00000107850.3; ENSMUSG00000048120.17.
DR   GeneID; 12495; -.
DR   KEGG; mmu:12495; -.
DR   UCSC; uc008hlf.2; mouse.
DR   AGR; MGI:102805; -.
DR   CTD; 953; -.
DR   MGI; MGI:102805; Entpd1.
DR   VEuPathDB; HostDB:ENSMUSG00000048120; -.
DR   eggNOG; KOG1386; Eukaryota.
DR   GeneTree; ENSGT01100000263542; -.
DR   HOGENOM; CLU_010246_2_3_1; -.
DR   InParanoid; P55772; -.
DR   OMA; PYSHCAF; -.
DR   OrthoDB; 180318at2759; -.
DR   PhylomeDB; P55772; -.
DR   TreeFam; TF332859; -.
DR   BRENDA; 3.6.1.5; 3474.
DR   Reactome; R-MMU-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR   SABIO-RK; P55772; -.
DR   BioGRID-ORCS; 12495; 1 hit in 63 CRISPR screens.
DR   ChiTaRS; Entpd1; mouse.
DR   PRO; PR:P55772; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P55772; Protein.
DR   Bgee; ENSMUSG00000048120; Expressed in ectoplacental cone and 188 other cell types or tissues.
DR   ExpressionAtlas; P55772; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IMP:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR   GO; GO:0043262; F:ADP phosphatase activity; IMP:MGI.
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; ISO:MGI.
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:0042802; F:identical protein binding; ISO:MGI.
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:MGI.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IDA:MGI.
DR   GO; GO:0045134; F:UDP phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046032; P:ADP catabolic process; IMP:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR   GO; GO:2001170; P:negative regulation of ATP biosynthetic process; ISO:MGI.
DR   GO; GO:0033602; P:negative regulation of dopamine secretion; ISO:MGI.
DR   GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR   GO; GO:0030168; P:platelet activation; IDA:MGI.
DR   GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
DR   GO; GO:0009181; P:purine ribonucleoside diphosphate catabolic process; IDA:MGI.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR11782:SF32; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 1; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
DR   Genevisible; P55772; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Disulfide bond; Glycoprotein; Hydrolase; Magnesium;
KW   Membrane; Nucleotide-binding; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..510
FT                   /note="Ectonucleoside triphosphate diphosphohydrolase 1"
FT                   /id="PRO_0000209903"
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..478
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        479..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        500..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        226
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        428
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        254..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        391..414
FT                   /evidence="ECO:0000250|UniProtKB:P97687"
SQ   SEQUENCE   510 AA;  57205 MW;  8E6A6113D2E13930 CRC64;
     MEDIKDSKVK RFCSKNILII LGFTSILAVI ALIAVGLTQN KPLPENVKYG IVLDAGSSHT
     NLYIYKWPAE KENDTGVVQQ LEECQVKGPG ISKYAQKTDE IGAYLAECME LSTELIPTSK
     HHQTPVYLGA TAGMRLLRME SEQSADEVLA AVSTSLKSYP FDFQGAKIIT GQEEGAYGWI
     TINYLLGRFT QEQSWLSLIS DSQKQETFGA LDLGGASTQI TFVPQNSTIE SPENSLQFRL
     YGEDYTVYTH SFLCYGKDQA LWQKLAKDIQ VSSGGVLKDP CFNPGYEKVV NVSELYGTPC
     TKRFEKKLPF DQFRIQGTGD YEQCHQSILE LFNNSHCPYS QCAFNGVFLP PLHGSFGAFS
     AFYFVMDFFK KVAKNSVISQ EKMTEITKNF CSKSWEETKT SYPSVKEKYL SEYCFSGAYI
     LSLLQGYNFT DSSWEQIHFM GKIKDSNAGW TLGYMLNLTN MIPAEQPLSP PLPHSTYIGL
     MVLFSLLLVA VAITGLFIYS KPSYFWKEAV
//