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ATS20_HUMAN
ID   ATS20_HUMAN             Reviewed;        1910 AA.
AC   P59510; A6NNC9; J3QT00;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 20;
DE            Short=ADAM-TS 20;
DE            Short=ADAM-TS20;
DE            Short=ADAMTS-20;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=ADAMTS20;
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).
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Liver;
RX   PubMed=12562771; DOI=10.1074/jbc.m211900200;
RA   Llamazares M., Cal S., Quesada V., Lopez-Otin C.;
RT   "Identification and characterization of ADAMTS-20 defines a novel subfamily
RT   of metalloproteinases-disintegrins with multiple thrombospondin-1 repeats
RT   and a unique GON domain.";
RL   J. Biol. Chem. 278:13382-13389(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in tissue-remodeling process occurring in
CC       both normal and pathological conditions. May have a protease-
CC       independent function in the transport from the endoplasmic reticulum to
CC       the Golgi apparatus of secretory cargos, mediated by the GON domain.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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=P59510-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P59510-2; Sequence=VSP_007106, VSP_007107, VSP_007108;
CC       Name=3;
CC         IsoId=P59510-3; Sequence=VSP_047084;
CC   -!- TISSUE SPECIFICITY: Very sparingly expressed, although is detected at
CC       low levels in testis, prostate, ovary, heart, placenta, lung and
CC       pancreas. Overexpressed in several brain, colon and breast carcinomas.
CC   -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
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}.
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DR   EMBL; AF488804; AAO15766.1; -; mRNA.
DR   EMBL; AJ515153; CAD56159.3; -; mRNA.
DR   EMBL; AJ515154; CAD56160.2; -; mRNA.
DR   EMBL; AC090525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC107018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC120104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471111; EAW57861.1; -; Genomic_DNA.
DR   CCDS; CCDS31778.2; -. [P59510-3]
DR   RefSeq; NP_079279.3; NM_025003.4. [P59510-3]
DR   AlphaFoldDB; P59510; -.
DR   SMR; P59510; -.
DR   BioGRID; 123100; 2.
DR   IntAct; P59510; 2.
DR   MINT; P59510; -.
DR   STRING; 9606.ENSP00000374071; -.
DR   MEROPS; M12.246; -.
DR   GlyGen; P59510; 15 sites.
DR   iPTMnet; P59510; -.
DR   PhosphoSitePlus; P59510; -.
DR   BioMuta; ADAMTS20; -.
DR   DMDM; 218511943; -.
DR   MassIVE; P59510; -.
DR   PaxDb; P59510; -.
DR   PeptideAtlas; P59510; -.
DR   PRIDE; P59510; -.
DR   Antibodypedia; 25100; 30 antibodies from 16 providers.
DR   DNASU; 80070; -.
DR   Ensembl; ENST00000389420.8; ENSP00000374071.3; ENSG00000173157.18. [P59510-3]
DR   GeneID; 80070; -.
DR   KEGG; hsa:80070; -.
DR   MANE-Select; ENST00000389420.8; ENSP00000374071.3; NM_025003.5; NP_079279.3. [P59510-3]
DR   UCSC; uc010skx.3; human. [P59510-1]
DR   CTD; 80070; -.
DR   DisGeNET; 80070; -.
DR   GeneCards; ADAMTS20; -.
DR   HGNC; HGNC:17178; ADAMTS20.
DR   HPA; ENSG00000173157; Tissue enriched (brain).
DR   MIM; 611681; gene.
DR   neXtProt; NX_P59510; -.
DR   OpenTargets; ENSG00000173157; -.
DR   PharmGKB; PA134901626; -.
DR   VEuPathDB; HostDB:ENSG00000173157; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   GeneTree; ENSGT00940000158636; -.
DR   HOGENOM; CLU_000660_0_1_1; -.
DR   InParanoid; P59510; -.
DR   OMA; YQECPVL; -.
DR   OrthoDB; 125522at2759; -.
DR   PhylomeDB; P59510; -.
DR   TreeFam; TF331949; -.
DR   PathwayCommons; P59510; -.
DR   Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR   Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR   SignaLink; P59510; -.
DR   BioGRID-ORCS; 80070; 6 hits in 1064 CRISPR screens.
DR   ChiTaRS; ADAMTS20; human.
DR   GenomeRNAi; 80070; -.
DR   Pharos; P59510; Tbio.
DR   PRO; PR:P59510; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P59510; protein.
DR   Bgee; ENSG00000173157; Expressed in placenta and 3 other tissues.
DR   ExpressionAtlas; P59510; baseline and differential.
DR   Genevisible; P59510; HS.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0045636; P:positive regulation of melanocyte differentiation; IEA:Ensembl.
DR   GO; GO:0009967; P:positive regulation of signal transduction; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:Ensembl.
DR   Gene3D; 2.20.100.10; -; 11.
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; 13.
DR   SUPFAM; SSF82895; SSF82895; 12.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS51046; GON; 1.
DR   PROSITE; PS50092; TSP1; 12.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript 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..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..253
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029206"
FT   CHAIN           254..1910
FT                   /note="A disintegrin and metalloproteinase with
FT                   thrombospondin motifs 20"
FT                   /id="PRO_0000029207"
FT   DOMAIN          259..467
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          468..555
FT                   /note="Disintegrin"
FT   DOMAIN          556..611
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          846..904
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          905..961
FT                   /note="TSP type-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          966..1023
FT                   /note="TSP type-1 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1024..1073
FT                   /note="TSP type-1 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1076..1135
FT                   /note="TSP type-1 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1152..1206
FT                   /note="TSP type-1 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1207..1264
FT                   /note="TSP type-1 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1304..1356
FT                   /note="TSP type-1 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1358..1416
FT                   /note="TSP type-1 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1417..1475
FT                   /note="TSP type-1 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1476..1531
FT                   /note="TSP type-1 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1535..1588
FT                   /note="TSP type-1 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1589..1652
FT                   /note="TSP type-1 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1654..1710
FT                   /note="TSP type-1 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1711..1910
FT                   /note="GON"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00383"
FT   REGION          724..846
FT                   /note="Spacer"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         403
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         407
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         413
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        702
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        717
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        728
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        809
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        870
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1061
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1456
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1542
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1572
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1763
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1781
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1852
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        334..387
FT                   /evidence="ECO:0000250"
FT   DISULFID        363..369
FT                   /evidence="ECO:0000250"
FT   DISULFID        381..462
FT                   /evidence="ECO:0000250"
FT   DISULFID        419..446
FT                   /evidence="ECO:0000250"
FT   DISULFID        489..511
FT                   /evidence="ECO:0000250"
FT   DISULFID        500..521
FT                   /evidence="ECO:0000250"
FT   DISULFID        506..540
FT                   /evidence="ECO:0000250"
FT   DISULFID        534..545
FT                   /evidence="ECO:0000250"
FT   DISULFID        568..605
FT                   /evidence="ECO:0000250"
FT   DISULFID        572..610
FT                   /evidence="ECO:0000250"
FT   DISULFID        583..595
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         683..693
FT                   /note="THDICVQGQCM -> SYNIDCNCVLK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12562771"
FT                   /id="VSP_007106"
FT   VAR_SEQ         818..821
FT                   /note="ILIE -> LILQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12514189"
FT                   /id="VSP_047084"
FT   VAR_SEQ         1429..1504
FT                   /note="CSASCGKGRKYREVFCIDQFQRKLEDTNCSQVQKPPTHKACRSVRCPSWKAN
FT                   SWNECSVTCGSGVQQRDVYCRLKG -> EDLKVKLLPQRTIILWELMKNIFCHGKHSHM
FT                   YLINVVTDHLLYPRHCDPETIETYFLSLWSLQFTWGDLKYYKNSL (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:12562771"
FT                   /id="VSP_007107"
FT   VAR_SEQ         1505..1910
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12562771"
FT                   /id="VSP_007108"
FT   VARIANT         876
FT                   /note="K -> M (in dbSNP:rs7302446)"
FT                   /id="VAR_057088"
FT   VARIANT         1000
FT                   /note="R -> H (in dbSNP:rs7297737)"
FT                   /id="VAR_057089"
FT   VARIANT         1273
FT                   /note="S -> F (in dbSNP:rs7310011)"
FT                   /id="VAR_057090"
FT   CONFLICT        152
FT                   /note="T -> V (in Ref. 2; CAD56159/CAD56160)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360
FT                   /note="E -> Y (in Ref. 2; CAD56159/CAD56160)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        371
FT                   /note="M -> T (in Ref. 1; AAO15766)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        456
FT                   /note="D -> E (in Ref. 2; CAD56159/CAD56160)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        648
FT                   /note="I -> V (in Ref. 2; CAD56159/CAD56160)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        792..793
FT                   /note="Missing (in Ref. 2; CAD56159/CAD56160)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        908..912
FT                   /note="WHVIG -> GMLLAK (in Ref. 1; AAO15766)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1315
FT                   /note="S -> Q (in Ref. 2; CAD56159/CAD56160)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1327
FT                   /note="R -> T (in Ref. 1; AAO15766)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1816
FT                   /note="T -> A (in Ref. 2; CAD56159)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1881
FT                   /note="E -> Q (in Ref. 2; CAD56159)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1910 AA;  214721 MW;  D7FFCB0D56F4B6D9 CRC64;
     MWVAKWLTGL LYHLSLFITR SWEVDFHPRQ EALVRTLTSY EVVIPERVNE FGEVFPQSHH
     FSRQKRSSEA LEPMPFRTHY RFTAYGQLFQ LNLTADASFL AAGYTEVHLG TPERGAWESD
     AGPSDLRHCF YRGQVNSQED YKAVVSLCGG LTGTFKGQNG EYFLEPIMKA DGNEYEDGHN
     KPHLIYRQDL NNSFLQTLKY CSVSESQIKE TSLPFHTYSN MNEDLNVMKE RVLGHTSKNV
     PLKDERRHSR KKRLISYPRY IEIMVTADAK VVSAHGSNLQ NYILTLMSIV ATIYKDPSIG
     NLIHIVVVKL VMIHREEEGP VINFDGATTL KNFCSWQQTQ NDLDDVHPSH HDTAVLITRE
     DICSSKEKCN MLGLSYLGTI CDPLQSCFIN EEKGLISAFT IAHELGHTLG VQHDDNPRCK
     EMKVTKYHVM APALSFHMSP WSWSNCSRKY VTEFLDTGYG ECLLDKPDEE IYNLPSELPG
     SRYDGNKQCE LAFGPGSQMC PHINICMHLW CTSTEKLHKG CFTQHVPPAD GTDCGPGMHC
     RHGLCVNKET ETRPVNGEWG PWEPYSSCSR TCGGGIESAT RRCNRPEPRN GGNYCVGRRM
     KFRSCNTDSC PKGTQDFREK QCSDFNGKHL DISGIPSNVR WLPRYSGIGT KDRCKLYCQV
     AGTNYFYLLK DMVEDGTPCG TETHDICVQG QCMAAGCDHV LNSSAKIDKC GVCGGDNSSC
     KTITGVFNSS HYGYNVVVKI PAGATNVDIR QYSYSGQPDD SYLALSDAEG NFLFNGNFLL
     STSKKEINVQ GTRTVIEYSG SNNAVERINS TNRQEKEILI EVLCVGNLYN PDVHYSFNIP
     LEERSDMFTW DPYGPWEGCT KMCQGLQRRN ITCIHKSDHS VVSDKECDHL PLPSFVTQSC
     NTDCELRWHV IGKSECSSQC GQGYRTLDIH CMKYSIHEGQ TVQVDDHYCG DQLKPPTQEL
     CHGNCVFTRW HYSEWSQCSR SCGGGERSRE SYCMNNFGHR LADNECQELS RVTRENCNEF
     SCPSWAASEW SECLVTCGKG TKQRQVWCQL NVDHLSDGFC NSSTKPESLS PCELHTCASW
     QVGPWGPCTT TCGHGYQMRD VKCVNELASA VLEDTECHEA SRPSDRQSCV LTPCSFISKL
     ETALLPTVLI KKMAQWRHGS WTPCSVSCGR GTQARYVSCR DALDRIADES YCAHLPRPAE
     IWDCFTPCGE WQAGDWSPCS ASCGHGKTTR QVLCMNYHQP IDENYCDPEV RPLMEQECSL
     AACPPAHSHF PSSPVQPSYY LSTNLPLTQK LEDNENQVVH PSVRGNQWRT GPWGSCSSSC
     SGGLQHRAVV CQDENGQSAS YCDAASKPPE LQQCGPGPCP QWNYGNWGEC SQTCGGGIKS
     RLVICQFPNG QILEDHNCEI VNKPPSVIQC HMHACPADVS WHQEPWTSCS ASCGKGRKYR
     EVFCIDQFQR KLEDTNCSQV QKPPTHKACR SVRCPSWKAN SWNECSVTCG SGVQQRDVYC
     RLKGVGQVVE EMCDQSTRPC SQRRCWSQDC VQHKGMERGR LNCSTSCERK DSHQRMECTD
     NQIRQVNEIV YNSSTISLTS KNCRNPPCNY IVVTADSSQC ANNCGFSYRQ RITYCTEIPS
     TKKHKLHRLR PIVYQECPVV PSSQVYQCIN SCLHLATWKV GKWSKCSVTC GIGIMKRQVK
     CITKHGLSSD LCLNHLKPGA QKKCYANDCK SFTTCKEIQV KNHIRKDGDY YLNIKGRIIK
     IYCADMYLEN PKEYLTLVQG EENFSEVYGF RLKNPYQCPF NGSRREDCEC DNGHLAAGYT
     VFSKIRIDLT SMQIKTTDLL FSKTIFGNAV PFATAGDCYS AFRCPQGQFS INLSGTGMKI
     SSTAKWLTQG SYTSVSIRRS EDGTRFFGKC GGYCGKCLPH MTTGLPIQVI
 
 
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