ATS9_HUMAN
ID ATS9_HUMAN Reviewed; 1935 AA.
AC Q9P2N4; A1L4L0; B7ZVX9; B9ZVN0; Q9NR29;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 4.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 9;
DE Short=ADAM-TS 9;
DE Short=ADAM-TS9;
DE Short=ADAMTS-9;
DE EC=3.4.24.- {ECO:0000269|PubMed:12514189};
DE Flags: Precursor;
GN Name=ADAMTS9; Synonyms=KIAA1312;
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 [MRNA] (ISOFORM 3).
RC TISSUE=Fetus;
RX PubMed=10936055; DOI=10.1006/geno.2000.6246;
RA Clark M.E., Kelner G.S., Turbeville L.A., Boyer A., Arden K.A., Maki R.A.;
RT "ADAMTS 9, a novel member of the ADAM-TS/Metallospondin gene family.";
RL Genomics 67:343-350(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PROTEOLYTIC CLEAVAGE,
RP GLYCOSYLATION, MUTAGENESIS OF ARG-33; ARG-74; ARG-280 AND ARG-287, AND
RP VARIANTS PRO-96 AND GLU-1674.
RX PubMed=12514189; DOI=10.1074/jbc.m211009200;
RA Somerville R.P., Longpre J.-M., Jungers K.A., Engle J.M., Ross M.,
RA Evanko S., Wight T.N., Leduc R., Apte S.S.;
RT "Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily
RT related to Caenorhabditis elegans GON-1.";
RL J. Biol. Chem. 278:9503-9513(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-1935 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [6]
RP FUNCTION IN TRANSPORT, AND SUBCELLULAR LOCATION.
RX PubMed=22419820; DOI=10.1091/mbc.e11-10-0857;
RA Yoshina S., Sakaki K., Yonezumi-Hayashi A., Gengyo-Ando K., Inoue H.,
RA Iino Y., Mitani S.;
RT "Identification of a novel ADAMTS9/GON-1 function for protein transport
RT from the ER to the Golgi.";
RL Mol. Biol. Cell 23:1728-1741(2012).
CC -!- FUNCTION: Cleaves the large aggregating proteoglycans, aggrecan (at the
CC '1838-Glu-|-Ala-1839' site) and versican (at the '1428-Glu-|-Ala-1429'
CC site). Has a protease-independent function in promoting the transport
CC from the endoplasmic reticulum to the Golgi apparatus of a variety of
CC secretory cargos. {ECO:0000269|PubMed:12514189,
CC ECO:0000269|PubMed:22419820}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9UHI8};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UHI8};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:12514189}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:22419820}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=ADAMTS-9B;
CC IsoId=Q9P2N4-3; Sequence=Displayed;
CC Name=2; Synonyms=Long;
CC IsoId=Q9P2N4-1; Sequence=VSP_007548, VSP_007549;
CC Name=3; Synonyms=Short;
CC IsoId=Q9P2N4-2; Sequence=VSP_005499, VSP_005500;
CC Name=4;
CC IsoId=Q9P2N4-4; Sequence=VSP_053399;
CC -!- TISSUE SPECIFICITY: Highly expressed in all fetal tissues. Expressed in
CC a number of adult tissues with highest expression in heart, placenta
CC and skeletal muscle. {ECO:0000269|PubMed:12514189}.
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 ancillary domains, including the TSRs domain, are required
CC for specific extracellular localization and for its versicanase and
CC aggrecanase activities.
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 -!- DOMAIN: The GON domain mediates protease-independent function in ER to
CC Golgi transport.
CC -!- PTM: The precursor is cleaved by a furin endopeptidase.
CC {ECO:0000269|PubMed:12514189}.
CC -!- PTM: N-glycosylated (PubMed:12514189). Can be O-fucosylated by POFUT2
CC on a serine or a threonine residue found within the consensus sequence
CC C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are
CC the first and second cysteine residue of the repeat, respectively.
CC Fucosylated repeats can then be further glycosylated by the addition of
CC a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL.
CC Fucosylation mediates the efficient secretion of ADAMTS family members.
CC Can also be C-glycosylated with one or two mannose molecules on
CC tryptophan residues within the consensus sequence W-X-X-W of the TPRs,
CC and N-glycosylated. These other glycosylations can also facilitate
CC secretion (By similarity). {ECO:0000250|UniProtKB:Q76LX8,
CC ECO:0000269|PubMed:12514189}.
CC -!- MISCELLANEOUS: [Isoform 2]: May result from the retention of an intron
CC in the cDNA leading to a prematurate stop codon. {ECO:0000305}.
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DR EMBL; AF261918; AAF89106.1; -; mRNA.
DR EMBL; AF488803; AAO15765.1; -; mRNA.
DR EMBL; AC096888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC130578; AAI30579.1; -; mRNA.
DR EMBL; BC171764; AAI71764.1; -; mRNA.
DR EMBL; AB037733; BAA92550.1; -; mRNA.
DR CCDS; CCDS2903.1; -. [Q9P2N4-3]
DR CCDS; CCDS82801.1; -. [Q9P2N4-4]
DR RefSeq; NP_001305710.1; NM_001318781.1. [Q9P2N4-4]
DR RefSeq; NP_891550.1; NM_182920.1. [Q9P2N4-3]
DR AlphaFoldDB; Q9P2N4; -.
DR SMR; Q9P2N4; -.
DR BioGRID; 121314; 3.
DR IntAct; Q9P2N4; 1.
DR STRING; 9606.ENSP00000418735; -.
DR MEROPS; M12.021; -.
DR GlyGen; Q9P2N4; 11 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9P2N4; -.
DR PhosphoSitePlus; Q9P2N4; -.
DR BioMuta; ADAMTS9; -.
DR DMDM; 212276516; -.
DR jPOST; Q9P2N4; -.
DR MassIVE; Q9P2N4; -.
DR PaxDb; Q9P2N4; -.
DR PeptideAtlas; Q9P2N4; -.
DR PRIDE; Q9P2N4; -.
DR ProteomicsDB; 7269; -.
DR ProteomicsDB; 83855; -. [Q9P2N4-3]
DR ProteomicsDB; 83856; -. [Q9P2N4-1]
DR ProteomicsDB; 83857; -. [Q9P2N4-2]
DR Antibodypedia; 31780; 102 antibodies from 18 providers.
DR DNASU; 56999; -.
DR Ensembl; ENST00000295903.8; ENSP00000295903.4; ENSG00000163638.13. [Q9P2N4-4]
DR Ensembl; ENST00000498707.5; ENSP00000418735.1; ENSG00000163638.13. [Q9P2N4-3]
DR GeneID; 56999; -.
DR KEGG; hsa:56999; -.
DR MANE-Select; ENST00000498707.5; ENSP00000418735.1; NM_182920.2; NP_891550.1.
DR UCSC; uc003dmg.4; human. [Q9P2N4-3]
DR CTD; 56999; -.
DR DisGeNET; 56999; -.
DR GeneCards; ADAMTS9; -.
DR HGNC; HGNC:13202; ADAMTS9.
DR HPA; ENSG00000163638; Low tissue specificity.
DR MalaCards; ADAMTS9; -.
DR MIM; 605421; gene.
DR neXtProt; NX_Q9P2N4; -.
DR OpenTargets; ENSG00000163638; -.
DR Orphanet; 93592; Juvenile nephronophthisis.
DR PharmGKB; PA24553; -.
DR VEuPathDB; HostDB:ENSG00000163638; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000156409; -.
DR HOGENOM; CLU_000660_0_1_1; -.
DR InParanoid; Q9P2N4; -.
DR OMA; DNDFQFA; -.
DR OrthoDB; 125522at2759; -.
DR PhylomeDB; Q9P2N4; -.
DR TreeFam; TF331949; -.
DR PathwayCommons; Q9P2N4; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q9P2N4; -.
DR BioGRID-ORCS; 56999; 13 hits in 1081 CRISPR screens.
DR ChiTaRS; ADAMTS9; human.
DR GeneWiki; ADAMTS9; -.
DR GenomeRNAi; 56999; -.
DR Pharos; Q9P2N4; Tbio.
DR PRO; PR:Q9P2N4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9P2N4; protein.
DR Bgee; ENSG00000163638; Expressed in omental fat pad and 154 other tissues.
DR ExpressionAtlas; Q9P2N4; baseline and differential.
DR Genevisible; Q9P2N4; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035909; P:aorta morphogenesis; ISS:BHF-UCL.
DR GO; GO:0090673; P:endothelial cell-matrix adhesion; ISS:BHF-UCL.
DR GO; GO:0030198; P:extracellular matrix organization; ISS:BHF-UCL.
DR GO; GO:0003179; P:heart valve morphogenesis; ISS:BHF-UCL.
DR GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISS:BHF-UCL.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISS:BHF-UCL.
DR GO; GO:0045636; P:positive regulation of melanocyte differentiation; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IDA:MGI.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0003229; P:ventricular cardiac muscle tissue development; ISS:BHF-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 13.
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; IPR012314; Pept_M12B_GON-ADAMTSs.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
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; PF08685; GON; 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; 15.
DR SUPFAM; SSF82895; SSF82895; 14.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS51046; GON; 1.
DR PROSITE; PS50092; TSP1; 14.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW Endoplasmic reticulum; ER-Golgi transport; Extracellular matrix;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Protein transport; Reference proteome; Repeat; Secreted; Signal; Transport;
KW Zinc; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..287
FT /evidence="ECO:0000269|PubMed:12514189"
FT /id="PRO_0000029182"
FT CHAIN 288..1935
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 9"
FT /id="PRO_0000029183"
FT DOMAIN 293..499
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 509..587
FT /note="Disintegrin"
FT DOMAIN 588..643
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 878..936
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 939..997
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 998..1049
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1052..1109
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1110..1166
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1182..1240
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1241..1296
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1328..1379
FT /note="TSP type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1382..1440
FT /note="TSP type-1 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1441..1494
FT /note="TSP type-1 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1497..1555
FT /note="TSP type-1 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1556..1611
FT /note="TSP type-1 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1612..1676
FT /note="TSP type-1 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1677..1734
FT /note="TSP type-1 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1735..1935
FT /note="GON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00383"
FT REGION 192..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..877
FT /note="Spacer"
FT REGION 1289..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 221..228
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 1289..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 223
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 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT SITE 287..288
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:12514189"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 368..418
FT /evidence="ECO:0000250"
FT DISULFID 394..400
FT /evidence="ECO:0000250"
FT DISULFID 412..494
FT /evidence="ECO:0000250"
FT DISULFID 450..478
FT /evidence="ECO:0000250"
FT DISULFID 521..543
FT /evidence="ECO:0000250"
FT DISULFID 532..553
FT /evidence="ECO:0000250"
FT DISULFID 538..572
FT /evidence="ECO:0000250"
FT DISULFID 566..577
FT /evidence="ECO:0000250"
FT DISULFID 600..637
FT /evidence="ECO:0000250"
FT DISULFID 604..642
FT /evidence="ECO:0000250"
FT DISULFID 615..627
FT /evidence="ECO:0000250"
FT DISULFID 890..931
FT /evidence="ECO:0000250"
FT DISULFID 894..935
FT /evidence="ECO:0000250"
FT DISULFID 904..918
FT /evidence="ECO:0000250"
FT DISULFID 1250..1290
FT /evidence="ECO:0000250"
FT DISULFID 1254..1295
FT /evidence="ECO:0000250"
FT DISULFID 1265..1278
FT /evidence="ECO:0000250"
FT DISULFID 1624..1670
FT /evidence="ECO:0000250"
FT DISULFID 1628..1675
FT /evidence="ECO:0000250"
FT DISULFID 1639..1659
FT /evidence="ECO:0000250"
FT VAR_SEQ 324..351
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053399"
FT VAR_SEQ 1064..1072
FT /note="CLVTCGKGH -> VRWEGCYFP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10936055"
FT /id="VSP_005499"
FT VAR_SEQ 1073..1935
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10936055"
FT /id="VSP_005500"
FT VAR_SEQ 1624..1629
FT /note="CSVTCG -> VPSWEL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_007548"
FT VAR_SEQ 1630..1935
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_007549"
FT VARIANT 96
FT /note="S -> P (in dbSNP:rs36115950)"
FT /evidence="ECO:0000269|PubMed:12514189"
FT /id="VAR_047081"
FT VARIANT 96
FT /note="S -> T (in dbSNP:rs36115950)"
FT /id="VAR_051592"
FT VARIANT 1579
FT /note="K -> E (in dbSNP:rs17071010)"
FT /id="VAR_047082"
FT VARIANT 1674
FT /note="D -> E (in dbSNP:rs6787633)"
FT /evidence="ECO:0000269|PubMed:12514189"
FT /id="VAR_047083"
FT VARIANT 1740
FT /note="K -> R (in dbSNP:rs17070967)"
FT /id="VAR_047084"
FT VARIANT 1791
FT /note="E -> Q (in dbSNP:rs3796381)"
FT /id="VAR_047085"
FT VARIANT 1921
FT /note="K -> E (in dbSNP:rs17070909)"
FT /id="VAR_051593"
FT VARIANT 1933
FT /note="R -> Q (in dbSNP:rs17070905)"
FT /id="VAR_047086"
FT MUTAGEN 33
FT /note="R->A: No effect on mature form production."
FT /evidence="ECO:0000269|PubMed:12514189"
FT MUTAGEN 74
FT /note="R->A: No effect on mature form production."
FT /evidence="ECO:0000269|PubMed:12514189"
FT MUTAGEN 280
FT /note="R->A: No effect on mature form production."
FT /evidence="ECO:0000269|PubMed:12514189"
FT MUTAGEN 287
FT /note="R->A: No mature form produced."
FT /evidence="ECO:0000269|PubMed:12514189"
FT CONFLICT 46
FT /note="S -> G (in Ref. 1; AAF89106)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="D -> G (in Ref. 2; AAO15765)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="F -> L (in Ref. 1; AAF89106)"
FT /evidence="ECO:0000305"
FT CONFLICT 1117
FT /note="G -> V (in Ref. 2; AAO15765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1935 AA; 216491 MW; 150B78D4C5CC2CCC CRC64;
MQFVSWATLL TLLVRDLAEM GSPDAAAAVR KDRLHPRQVK LLETLSEYEI VSPIRVNALG
EPFPTNVHFK RTRRSINSAT DPWPAFASSS SSSTSSQAHY RLSAFGQQFL FNLTANAGFI
APLFTVTLLG TPGVNQTKFY SEEEAELKHC FYKGYVNTNS EHTAVISLCS GMLGTFRSHD
GDYFIEPLQS MDEQEDEEEQ NKPHIIYRRS APQREPSTGR HACDTSEHKN RHSKDKKKTR
ARKWGERINL AGDVAALNSG LATEAFSAYG NKTDNTREKR THRRTKRFLS YPRFVEVLVV
ADNRMVSYHG ENLQHYILTL MSIVASIYKD PSIGNLINIV IVNLIVIHNE QDGPSISFNA
QTTLKNFCQW QHSKNSPGGI HHDTAVLLTR QDICRAHDKC DTLGLAELGT ICDPYRSCSI
SEDSGLSTAF TIAHELGHVF NMPHDDNNKC KEEGVKSPQH VMAPTLNFYT NPWMWSKCSR
KYITEFLDTG YGECLLNEPE SRPYPLPVQL PGILYNVNKQ CELIFGPGSQ VCPYMMQCRR
LWCNNVNGVH KGCRTQHTPW ADGTECEPGK HCKYGFCVPK EMDVPVTDGS WGSWSPFGTC
SRTCGGGIKT AIRECNRPEP KNGGKYCVGR RMKFKSCNTE PCLKQKRDFR DEQCAHFDGK
HFNINGLLPN VRWVPKYSGI LMKDRCKLFC RVAGNTAYYQ LRDRVIDGTP CGQDTNDICV
QGLCRQAGCD HVLNSKARRD KCGVCGGDNS SCKTVAGTFN TVHYGYNTVV RIPAGATNID
VRQHSFSGET DDDNYLALSS SKGEFLLNGN FVVTMAKREI RIGNAVVEYS GSETAVERIN
STDRIEQELL LQVLSVGKLY NPDVRYSFNI PIEDKPQQFY WNSHGPWQAC SKPCQGERKR
KLVCTRESDQ LTVSDQRCDR LPQPGHITEP CGTDCDLRWH VASRSECSAQ CGLGYRTLDI
YCAKYSRLDG KTEKVDDGFC SSHPKPSNRE KCSGECNTGG WRYSAWTECS KSCDGGTQRR
RAICVNTRND VLDDSKCTHQ EKVTIQRCSE FPCPQWKSGD WSECLVTCGK GHKHRQVWCQ
FGEDRLNDRM CDPETKPTSM QTCQQPECAS WQAGPWGQCS VTCGQGYQLR AVKCIIGTYM
SVVDDNDCNA ATRPTDTQDC ELPSCHPPPA APETRRSTYS APRTQWRFGS WTPCSATCGK
GTRMRYVSCR DENGSVADES ACATLPRPVA KEECSVTPCG QWKALDWSSC SVTCGQGRAT
RQVMCVNYSD HVIDRSECDQ DYIPETDQDC SMSPCPQRTP DSGLAQHPFQ NEDYRPRSAS
PSRTHVLGGN QWRTGPWGAC SSTCAGGSQR RVVVCQDENG YTANDCVERI KPDEQRACES
GPCPQWAYGN WGECTKLCGG GIRTRLVVCQ RSNGERFPDL SCEILDKPPD REQCNTHACP
HDAAWSTGPW SSCSVSCGRG HKQRNVYCMA KDGSHLESDY CKHLAKPHGH RKCRGGRCPK
WKAGAWSQCS VSCGRGVQQR HVGCQIGTHK IARETECNPY TRPESERDCQ GPRCPLYTWR
AEEWQECTKT CGEGSRYRKV VCVDDNKNEV HGARCDVSKR PVDRESCSLQ PCEYVWITGE
WSECSVTCGK GYKQRLVSCS EIYTGKENYE YSYQTTINCP GTQPPSVHPC YLRDCPVSAT
WRVGNWGSCS VSCGVGVMQR SVQCLTNEDQ PSHLCHTDLK PEERKTCRNV YNCELPQNCK
EVKRLKGASE DGEYFLMIRG KLLKIFCAGM HSDHPKEYVT LVHGDSENFS EVYGHRLHNP
TECPYNGSRR DDCQCRKDYT AAGFSSFQKI RIDLTSMQII TTDLQFARTS EGHPVPFATA
GDCYSAAKCP QGRFSINLYG TGLSLTESAR WISQGNYAVS DIKKSPDGTR VVGKCGGYCG
KCTPSSGTGL EVRVL
