ATS12_HUMAN
ID ATS12_HUMAN Reviewed; 1594 AA.
AC P58397; A2RRN9; A5D6V6; Q6UWL3;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 12;
DE Short=ADAM-TS 12;
DE Short=ADAM-TS12;
DE Short=ADAMTS-12;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=ADAMTS12; ORFNames=UNQ1918/PRO4389;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP RETRACTED PAPER.
RC TISSUE=Fetal lung;
RX PubMed=11279086; DOI=10.1074/jbc.m100534200;
RA Cal S., Argueelles J.M., Fernandez P.L., Lopez-Otin C.;
RT "Identification, characterization, and intracellular processing of ADAM-
RT TS12, a novel human disintegrin with a complex structural organization
RT involving multiple thrombospondin-1 repeats.";
RL J. Biol. Chem. 276:17932-17940(2001).
RN [5]
RP RETRACTION NOTICE OF PUBMED:11279086.
RX PubMed=30808000; DOI=10.1074/jbc.w118.007323;
RA Cal S., Argueelles J.M., Fernandez P.L., Lopez-Otin C.;
RL J. Biol. Chem. 294:1429-1429(2019).
RN [6]
RP FUNCTION, INTERACTION WITH COMP, PH DEPENDENCE, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=16611630; DOI=10.1074/jbc.m513433200;
RA Liu C.-J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S.,
RA Howell R.D., Di Cesare P.E.;
RT "ADAMTS-12 associates with and degrades cartilage oligomeric matrix
RT protein.";
RL J. Biol. Chem. 281:15800-15808(2006).
RN [7]
RP FUNCTION.
RX PubMed=17895370; DOI=10.1242/jcs.005751;
RA Llamazares M., Obaya A.J., Moncada-Pazos A., Heljasvaara R., Espada J.,
RA Lopez-Otin C., Cal S.;
RT "The ADAMTS12 metalloproteinase exhibits anti-tumorigenic properties
RT through modulation of the Ras-dependent ERK signalling pathway.";
RL J. Cell Sci. 120:3544-3552(2007).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, AND INDUCTION.
RX PubMed=18485748; DOI=10.1016/j.joca.2008.03.017;
RA Luan Y., Kong L., Howell D.R., Ilalov K., Fajardo M., Bai X.-H.,
RA Di Cesare P.E., Goldring M.B., Abramson S.B., Liu C.-J.;
RT "Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage oligomeric
RT matrix protein by alpha-2-macroglobulin.";
RL Osteoarthritis Cartilage 16:1413-1420(2008).
CC -!- FUNCTION: Metalloprotease that may play a role in the degradation of
CC COMP. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-
CC tumorigenic properties. {ECO:0000269|PubMed:16611630,
CC ECO:0000269|PubMed:17895370, ECO:0000269|PubMed:18485748}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by alpha-2 macroglobulin.
CC {ECO:0000269|PubMed:18485748}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is between 7.5 and 9.5 with COMP for substrate.
CC {ECO:0000269|PubMed:16611630};
CC -!- SUBUNIT: Interacts with COMP. {ECO:0000269|PubMed:16611630}.
CC -!- INTERACTION:
CC P58397; P49747: COMP; NbExp=3; IntAct=EBI-9028051, EBI-2531022;
CC P58397; B4DJ51: HEL-S-72; NbExp=3; IntAct=EBI-9028051, EBI-10171450;
CC P58397; P50222: MEOX2; NbExp=3; IntAct=EBI-9028051, EBI-748397;
CC P58397; P60660: MYL6; NbExp=4; IntAct=EBI-9028051, EBI-300817;
CC P58397; Q9R0G6: Comp; Xeno; NbExp=3; IntAct=EBI-9028051, EBI-9028018;
CC P58397-3; P38432: COIL; NbExp=3; IntAct=EBI-12048761, EBI-945751;
CC P58397-3; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-12048761, EBI-8638439;
CC P58397-3; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-12048761, EBI-11952721;
CC P58397-3; Q14142: TRIM14; NbExp=3; IntAct=EBI-12048761, EBI-2820256;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P58397-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P58397-2; Sequence=VSP_013141, VSP_013142;
CC Name=3;
CC IsoId=P58397-3; Sequence=VSP_038151;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle and fat.
CC {ECO:0000269|PubMed:16611630}.
CC -!- INDUCTION: By IFN-alpha and by IL1B/interleukin-1 beta. Up-regulated in
CC articular cartilage and synovium from arthritis patients. Up-regulared
CC in chondrocytes. {ECO:0000269|PubMed:16611630,
CC ECO:0000269|PubMed:18485748}.
CC -!- DOMAIN: The spacer domain and the TSP type-1 domains are important for
CC a tight interaction with the extracellular matrix. {ECO:0000250}.
CC -!- DOMAIN: The C-terminal four TSP1-like repeats are necessary and
CC sufficient for binding COMP.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: The precursor is cleaved by a furin endopeptidase.
CC -!- PTM: Subjected to an intracellular maturation process yielding a 120
CC kDa N-terminal fragment containing the metalloproteinase, disintegrin,
CC one TSP type-1 and the Cys-rich domains and a 83 kDa C-terminal
CC fragment containing the spacer 2 and four TSP type-1 domains.
CC -!- PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a
CC threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-
CC G of the TSP type-1 repeat domains where C1 and C2 are the first and
CC second cysteine residue of the repeat, respectively. Fucosylated
CC repeats can then be further glycosylated by the addition of a beta-1,3-
CC glucose residue by the glucosyltransferase, B3GALTL. Fucosylation
CC mediates the efficient secretion of ADAMTS family members. Can also be
CC C-glycosylated with one or two mannose molecules on tryptophan residues
CC within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated.
CC These other glycosylations can also facilitate secretion (By
CC similarity). {ECO:0000250}.
CC -!- CAUTION: Was reported to be expressed in adult skeletal muscle and fat,
CC in fetal lung, and in gastric carcinomas and cancer cells of diverse
CC origin (PubMed:11279086). However, this paper has been retracted
CC because data in one figure has been falsified (PubMed:30808000).
CC {ECO:0000269|PubMed:11279086, ECO:0000269|PubMed:30808000}.
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DR EMBL; AJ250725; CAC20419.1; -; mRNA.
DR EMBL; AY358745; AAQ89105.1; -; mRNA.
DR EMBL; AC008880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC034232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058841; AAH58841.1; -; mRNA.
DR EMBL; BC131733; AAI31734.1; -; mRNA.
DR EMBL; BC139900; AAI39901.1; -; mRNA.
DR CCDS; CCDS34140.1; -. [P58397-1]
DR CCDS; CCDS87293.1; -. [P58397-3]
DR RefSeq; NP_001311440.1; NM_001324511.1.
DR RefSeq; NP_001311441.1; NM_001324512.1. [P58397-3]
DR RefSeq; NP_112217.2; NM_030955.3. [P58397-1]
DR AlphaFoldDB; P58397; -.
DR SMR; P58397; -.
DR BioGRID; 123584; 48.
DR IntAct; P58397; 18.
DR STRING; 9606.ENSP00000422554; -.
DR MEROPS; M12.237; -.
DR GlyConnect; 996; 5 N-Linked glycans (3 sites).
DR GlyGen; P58397; 15 sites, 5 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P58397; -.
DR PhosphoSitePlus; P58397; -.
DR BioMuta; ADAMTS12; -.
DR DMDM; 259016182; -.
DR CPTAC; CPTAC-2207; -.
DR MassIVE; P58397; -.
DR PaxDb; P58397; -.
DR PeptideAtlas; P58397; -.
DR PRIDE; P58397; -.
DR ProteomicsDB; 57068; -. [P58397-1]
DR ProteomicsDB; 57069; -. [P58397-2]
DR ProteomicsDB; 57070; -. [P58397-3]
DR Antibodypedia; 22743; 143 antibodies from 22 providers.
DR DNASU; 81792; -.
DR Ensembl; ENST00000352040.7; ENSP00000344847.3; ENSG00000151388.11. [P58397-3]
DR Ensembl; ENST00000504830.6; ENSP00000422554.1; ENSG00000151388.11. [P58397-1]
DR GeneID; 81792; -.
DR KEGG; hsa:81792; -.
DR MANE-Select; ENST00000504830.6; ENSP00000422554.1; NM_030955.4; NP_112217.2.
DR UCSC; uc003jia.3; human. [P58397-1]
DR CTD; 81792; -.
DR DisGeNET; 81792; -.
DR GeneCards; ADAMTS12; -.
DR HGNC; HGNC:14605; ADAMTS12.
DR HPA; ENSG00000151388; Low tissue specificity.
DR MIM; 606184; gene.
DR neXtProt; NX_P58397; -.
DR OpenTargets; ENSG00000151388; -.
DR PharmGKB; PA24538; -.
DR VEuPathDB; HostDB:ENSG00000151388; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000155855; -.
DR HOGENOM; CLU_000660_2_1_1; -.
DR InParanoid; P58397; -.
DR OMA; MFNQSEG; -.
DR OrthoDB; 1229120at2759; -.
DR PhylomeDB; P58397; -.
DR TreeFam; TF313537; -.
DR PathwayCommons; P58397; -.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; P58397; -.
DR BioGRID-ORCS; 81792; 13 hits in 1066 CRISPR screens.
DR ChiTaRS; ADAMTS12; human.
DR GeneWiki; ADAMTS12; -.
DR GenomeRNAi; 81792; -.
DR Pharos; P58397; Tbio.
DR PRO; PR:P58397; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P58397; protein.
DR Bgee; ENSG00000151388; Expressed in adrenal tissue and 120 other tissues.
DR ExpressionAtlas; P58397; baseline and differential.
DR Genevisible; P58397; HS.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0016477; P:cell migration; IMP:BHF-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:BHF-UCL.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IDA:BHF-UCL.
DR GO; GO:0071347; P:cellular response to interleukin-1; IMP:BHF-UCL.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:BHF-UCL.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:2001113; P:negative regulation of cellular response to hepatocyte growth factor stimulus; IDA:BHF-UCL.
DR GO; GO:1902548; P:negative regulation of cellular response to vascular endothelial growth factor stimulus; IDA:BHF-UCL.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IDA:BHF-UCL.
DR GO; GO:1902203; P:negative regulation of hepatocyte growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl.
DR GO; GO:0030167; P:proteoglycan catabolic process; IDA:BHF-UCL.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:BHF-UCL.
DR GO; GO:1901509; P:regulation of endothelial tube morphogenesis; IDA:BHF-UCL.
DR GO; GO:0050727; P:regulation of inflammatory response; IDA:BHF-UCL.
DR Gene3D; 2.20.100.10; -; 8.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF19236; ADAM_CR_3; 1.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 8.
DR SUPFAM; SSF82895; SSF82895; 8.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 6.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Zinc; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..240
FT /evidence="ECO:0000250"
FT /id="PRO_0000029186"
FT CHAIN 241..1594
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 12"
FT /id="PRO_0000029187"
FT DOMAIN 246..456
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 465..544
FT /note="Disintegrin"
FT DOMAIN 542..597
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 823..883
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 887..943
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 944..997
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1313..1366
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1368..1422
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1423..1471
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1472..1532
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1535..1575
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 701..827
FT /note="Spacer 1"
FT REGION 997..1316
FT /note="Spacer 2"
FT REGION 1002..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 208..213
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 1002..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1031
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 952
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 322..376
FT /evidence="ECO:0000250"
FT DISULFID 351..358
FT /evidence="ECO:0000250"
FT DISULFID 370..451
FT /evidence="ECO:0000250"
FT DISULFID 409..435
FT /evidence="ECO:0000250"
FT DISULFID 478..501
FT /evidence="ECO:0000250"
FT DISULFID 489..507
FT /evidence="ECO:0000250"
FT DISULFID 496..526
FT /evidence="ECO:0000250"
FT DISULFID 520..531
FT /evidence="ECO:0000250"
FT DISULFID 554..591
FT /evidence="ECO:0000250"
FT DISULFID 558..596
FT /evidence="ECO:0000250"
FT DISULFID 569..581
FT /evidence="ECO:0000250"
FT VAR_SEQ 212..229
FT /note="DSVNISQKQELWREKWER -> GIVTHMSSWVEESVLFFW (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013141"
FT VAR_SEQ 230..1594
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013142"
FT VAR_SEQ 630..714
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038151"
FT VARIANT 110
FT /note="Q -> E (in dbSNP:rs16891862)"
FT /id="VAR_057074"
FT VARIANT 1000
FT /note="R -> Q (in dbSNP:rs13362345)"
FT /id="VAR_057075"
FT VARIANT 1177
FT /note="W -> R (in dbSNP:rs3813474)"
FT /id="VAR_059761"
FT VARIANT 1495
FT /note="T -> I (in dbSNP:rs25754)"
FT /id="VAR_058972"
FT VARIANT 1591
FT /note="S -> P (in dbSNP:rs16891281)"
FT /id="VAR_059762"
FT CONFLICT 1578
FT /note="H -> R (in Ref. 3; AAI31734)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1594 AA; 177676 MW; C88563125F0F90D8 CRC64;
MPCAQRSWLA NLSVVAQLLN FGALCYGRQP QPGPVRFPDR RQEHFIKGLP EYHVVGPVRV
DASGHFLSYG LHYPITSSRR KRDLDGSEDW VYYRISHEEK DLFFNLTVNQ GFLSNSYIME
KRYGNLSHVK MMASSAPLCH LSGTVLQQGT RVGTAALSAC HGLTGFFQLP HGDFFIEPVK
KHPLVEGGYH PHIVYRRQKV PETKEPTCGL KDSVNISQKQ ELWREKWERH NLPSRSLSRR
SISKERWVET LVVADTKMIE YHGSENVESY ILTIMNMVTG LFHNPSIGNA IHIVVVRLIL
LEEEEQGLKI VHHAEKTLSS FCKWQKSINP KSDLNPVHHD VAVLLTRKDI CAGFNRPCET
LGLSHLSGMC QPHRSCNINE DSGLPLAFTI AHELGHSFGI QHDGKENDCE PVGRHPYIMS
RQLQYDPTPL TWSKCSEEYI TRFLDRGWGF CLDDIPKKKG LKSKVIAPGV IYDVHHQCQL
QYGPNATFCQ EVENVCQTLW CSVKGFCRSK LDAAADGTQC GEKKWCMAGK CITVGKKPES
IPGGWGRWSP WSHCSRTCGA GVQSAERLCN NPEPKFGGKY CTGERKRYRL CNVHPCRSEA
PTFRQMQCSE FDTVPYKNEL YHWFPIFNPA HPCELYCRPI DGQFSEKMLD AVIDGTPCFE
GGNSRNVCIN GICKMVGCDY EIDSNATEDR CGVCLGDGSS CQTVRKMFKQ KEGSGYVDIG
LIPKGARDIR VMEIEGAGNF LAIRSEDPEK YYLNGGFIIQ WNGNYKLAGT VFQYDRKGDL
EKLMATGPTN ESVWIQLLFQ VTNPGIKYEY TIQKDGLDND VEQQMYFWQY GHWTECSVTC
GTGIRRQTAH CIKKGRGMVK ATFCDPETQP NGRQKKCHEK ACPPRWWAGE WEACSATCGP
HGEKKRTVLC IQTMVSDEQA LPPTDCQHLL KPKTLLSCNR DILCPSDWTV GNWSECSVSC
GGGVRIRSVT CAKNHDEPCD VTRKPNSRAL CGLQQCPSSR RVLKPNKGTI SNGKNPPTLK
PVPPPTSRPR MLTTPTGPES MSTSTPAISS PSPTTASKEG DLGGKQWQDS STQPELSSRY
LISTGSTSQP ILTSQSLSIQ PSEENVSSSD TGPTSEGGLV ATTTSGSGLS SSRNPITWPV
TPFYNTLTKG PEMEIHSGSG EEREQPEDKD ESNPVIWTKI RVPGNDAPVE STEMPLAPPL
TPDLSRESWW PPFSTVMEGL LPSQRPTTSE TGTPRVEGMV TEKPANTLLP LGGDHQPEPS
GKTANRNHLK LPNNMNQTKS SEPVLTEEDA TSLITEGFLL NASNYKQLTN GHGSAHWIVG
NWSECSTTCG LGAYWRRVEC STQMDSDCAA IQRPDPAKRC HLRPCAGWKV GNWSKCSRNC
SGGFKIREIQ CVDSRDHRNL RPFHCQFLAG IPPPLSMSCN PEPCEAWQVE PWSQCSRSCG
GGVQERGVFC PGGLCDWTKR PTSTMSCNEH LCCHWATGNW DLCSTSCGGG FQKRTVQCVP
SEGNKTEDQD QCLCDHKPRP PEFKKCNQQA CKKSADLLCT KDKLSASFCQ TLKAMKKCSV
PTVRAECCFS CPQTHITHTQ RQRRQRLLQK SKEL
