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 27-MAR-2024, entry version 179.
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 GlyCosmos; P59510; 15 sites, No reported glycans.
DR GlyGen; P59510; 15 sites.
DR iPTMnet; P59510; -.
DR PhosphoSitePlus; P59510; -.
DR BioMuta; ADAMTS20; -.
DR DMDM; 218511943; -.
DR MassIVE; P59510; -.
DR PaxDb; 9606-ENSP00000374071; -.
DR PeptideAtlas; P59510; -.
DR Antibodypedia; 25100; 33 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 AGR; HGNC:17178; -.
DR DisGeNET; 80070; -.
DR GeneCards; ADAMTS20; -.
DR HGNC; HGNC:17178; ADAMTS20.
DR HPA; ENSG00000173157; Not detected.
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; WPSDLCL; -.
DR OrthoDB; 2910701at2759; -.
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 1139 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 male germ line stem cell (sensu Vertebrata) in testis and 4 other cell types or 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 CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 11.
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 PANTHER; PTHR13723:SF165; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 20; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF08685; GON; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 12.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 13.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 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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