ATS1_HUMAN
ID ATS1_HUMAN Reviewed; 967 AA.
AC Q9UHI8; D3DSD5; Q9NSJ8; Q9P2K0; Q9UH83; Q9UP80;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 1;
DE Short=ADAM-TS 1;
DE Short=ADAM-TS1;
DE Short=ADAMTS-1;
DE EC=3.4.24.-;
DE AltName: Full=METH-1;
DE Flags: Precursor;
GN Name=ADAMTS1; Synonyms=KIAA1346, METH1;
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], AND VARIANT PRO-227.
RA Casas C., Pritchard M.A., Estivill X., Arbones M.L.;
RT "Cloning, characterization and mapping on human chromosome 21 of the
RT orthologue of murine Adamts-1.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-227, AND FUNCTION.
RC TISSUE=Heart;
RX PubMed=10438512; DOI=10.1074/jbc.274.33.23349;
RA Vazquez F., Hastings G., Ortega M.-A., Lane T.F., Oikemus S., Lombardo M.,
RA Iruela-Arispe M.L.;
RT "METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new
RT family of proteins with angio-inhibitory activity.";
RL J. Biol. Chem. 274:23349-23357(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-227.
RC TISSUE=Endothelial cell;
RX PubMed=10785405; DOI=10.1046/j.1432-1327.2000.01325.x;
RA Glienke J., Schmitt A.O., Pilarsky C., Hinzmann B., Weiss B., Rosenthal A.,
RA Thierauch K.H.;
RT "Differential gene expression by endothelial cells in distinct angiogenic
RT states.";
RL Eur. J. Biochem. 267:2820-2830(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 418-967.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 253-548 ALONE AND IN COMPLEX WITH
RP INHIBITOR, ACTIVE SITE, COFACTOR, ZINC-BINDING SITES, CALCIUM-BINDING
RP SITES, AND DISULFIDE BONDS.
RX PubMed=17897672; DOI=10.1016/j.jmb.2007.07.047;
RA Gerhardt S., Hassall G., Hawtin P., McCall E., Flavell L., Minshull C.,
RA Hargreaves D., Ting A., Pauptit R.A., Parker A.E., Abbott W.M.;
RT "Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain
RT and a disintegrin-like domain with a fold homologous to cysteine-rich
RT domains.";
RL J. Mol. Biol. 373:891-902(2007).
CC -!- FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, at the '1938-
CC Glu-|-Leu-1939' site (within the chondroitin sulfate attachment
CC domain), and may be involved in its turnover (By similarity). Has
CC angiogenic inhibitor activity. Active metalloprotease, which may be
CC associated with various inflammatory processes as well as development
CC of cancer cachexia. May play a critical role in follicular rupture.
CC {ECO:0000250, ECO:0000269|PubMed:10438512}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17897672};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17897672};
CC -!- INTERACTION:
CC Q9UHI8; Q6A162: KRT40; NbExp=3; IntAct=EBI-2511802, EBI-10171697;
CC Q9UHI8; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2511802, EBI-10171774;
CC Q9UHI8; O00233: PSMD9; NbExp=3; IntAct=EBI-2511802, EBI-750973;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- DOMAIN: The spacer domain and the TSP type-1 domains are important for
CC a tight interaction with the extracellular matrix.
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. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD48080.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA92584.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ADAMTS1ID574ch21q21.html";
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DR EMBL; AF170084; AAF15317.1; -; mRNA.
DR EMBL; AF060152; AAD48080.1; ALT_INIT; mRNA.
DR EMBL; AF207664; AAF23772.1; -; mRNA.
DR EMBL; AB037767; BAA92584.1; ALT_INIT; mRNA.
DR EMBL; AP001697; BAA95502.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09951.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09952.1; -; Genomic_DNA.
DR EMBL; AL162080; CAB82413.1; -; mRNA.
DR CCDS; CCDS33524.1; -.
DR PIR; T47158; T47158.
DR RefSeq; NP_008919.3; NM_006988.4.
DR PDB; 2JIH; X-ray; 2.10 A; A/B=253-548.
DR PDB; 2V4B; X-ray; 2.00 A; A/B=253-548.
DR PDB; 3Q2G; X-ray; 2.30 A; A/B=256-548.
DR PDB; 3Q2H; X-ray; 2.33 A; A/B=256-548.
DR PDBsum; 2JIH; -.
DR PDBsum; 2V4B; -.
DR PDBsum; 3Q2G; -.
DR PDBsum; 3Q2H; -.
DR AlphaFoldDB; Q9UHI8; -.
DR SMR; Q9UHI8; -.
DR BioGRID; 114888; 80.
DR IntAct; Q9UHI8; 13.
DR STRING; 9606.ENSP00000284984; -.
DR BindingDB; Q9UHI8; -.
DR ChEMBL; CHEMBL5133; -.
DR GuidetoPHARMACOLOGY; 1674; -.
DR MEROPS; M12.222; -.
DR TCDB; 8.A.77.1.6; the sheddase (sheddase) family.
DR CarbonylDB; Q9UHI8; -.
DR GlyGen; Q9UHI8; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UHI8; -.
DR PhosphoSitePlus; Q9UHI8; -.
DR BioMuta; ADAMTS1; -.
DR DMDM; 124053460; -.
DR jPOST; Q9UHI8; -.
DR MassIVE; Q9UHI8; -.
DR MaxQB; Q9UHI8; -.
DR PaxDb; Q9UHI8; -.
DR PeptideAtlas; Q9UHI8; -.
DR PRIDE; Q9UHI8; -.
DR ProteomicsDB; 84361; -.
DR Antibodypedia; 4291; 419 antibodies from 33 providers.
DR DNASU; 9510; -.
DR Ensembl; ENST00000284984.8; ENSP00000284984.2; ENSG00000154734.16.
DR GeneID; 9510; -.
DR KEGG; hsa:9510; -.
DR MANE-Select; ENST00000284984.8; ENSP00000284984.2; NM_006988.5; NP_008919.3.
DR UCSC; uc002ymf.4; human.
DR CTD; 9510; -.
DR DisGeNET; 9510; -.
DR GeneCards; ADAMTS1; -.
DR HGNC; HGNC:217; ADAMTS1.
DR HPA; ENSG00000154734; Tissue enhanced (ovary).
DR MIM; 605174; gene.
DR neXtProt; NX_Q9UHI8; -.
DR NIAGADS; ENSG00000154734; -.
DR OpenTargets; ENSG00000154734; -.
DR PharmGKB; PA24536; -.
DR VEuPathDB; HostDB:ENSG00000154734; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000156815; -.
DR HOGENOM; CLU_000660_3_0_1; -.
DR InParanoid; Q9UHI8; -.
DR OMA; KKHFDTP; -.
DR OrthoDB; 125522at2759; -.
DR PhylomeDB; Q9UHI8; -.
DR TreeFam; TF331949; -.
DR BRENDA; 3.4.24.B11; 2681.
DR BRENDA; 3.4.24.B12; 2681.
DR PathwayCommons; Q9UHI8; -.
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; Q9UHI8; -.
DR SIGNOR; Q9UHI8; -.
DR BioGRID-ORCS; 9510; 8 hits in 1073 CRISPR screens.
DR ChiTaRS; ADAMTS1; human.
DR EvolutionaryTrace; Q9UHI8; -.
DR GeneWiki; ADAMTS1; -.
DR GenomeRNAi; 9510; -.
DR Pharos; Q9UHI8; Tchem.
DR PRO; PR:Q9UHI8; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9UHI8; protein.
DR Bgee; ENSG00000154734; Expressed in right ovary and 191 other tissues.
DR ExpressionAtlas; Q9UHI8; baseline and differential.
DR Genevisible; Q9UHI8; HS.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:MGI.
DR GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0060347; P:heart trabecula formation; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:ProtInc.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IGI:BHF-UCL.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IGI:BHF-UCL.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IGI:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 3.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
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; IPR013274; Pept_M12B_ADAM-TS1.
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; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01858; ADAMTS1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF82895; SSF82895; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 3.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cleavage on pair of basic residues; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Heparin-binding; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..49
FT /evidence="ECO:0000255"
FT PROPEP 50..252
FT /evidence="ECO:0000250"
FT /id="PRO_0000029150"
FT CHAIN 253..967
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 1"
FT /id="PRO_0000029151"
FT DOMAIN 258..467
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 476..559
FT /note="Disintegrin"
FT DOMAIN 559..614
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 854..905
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 908..967
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..849
FT /note="Spacer"
FT MOTIF 196..203
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 234..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:17897672"
FT BINDING 198
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 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17897672"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17897672"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17897672"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17897672"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17897672"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17897672"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17897672"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17897672"
FT BINDING 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17897672"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17897672"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17897672"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 333..385
FT /evidence="ECO:0000269|PubMed:17897672"
FT DISULFID 362..367
FT /evidence="ECO:0000269|PubMed:17897672"
FT DISULFID 379..462
FT /evidence="ECO:0000269|PubMed:17897672"
FT DISULFID 417..446
FT /evidence="ECO:0000269|PubMed:17897672"
FT DISULFID 488..511
FT /evidence="ECO:0000269|PubMed:17897672"
FT DISULFID 499..521
FT /evidence="ECO:0000269|PubMed:17897672"
FT DISULFID 506..540
FT /evidence="ECO:0000269|PubMed:17897672"
FT DISULFID 534..545
FT /evidence="ECO:0000269|PubMed:17897672"
FT DISULFID 571..608
FT /evidence="ECO:0000250"
FT DISULFID 575..613
FT /evidence="ECO:0000250"
FT DISULFID 586..598
FT /evidence="ECO:0000250"
FT VARIANT 227
FT /note="A -> P (in dbSNP:rs428785)"
FT /evidence="ECO:0000269|PubMed:10438512,
FT ECO:0000269|PubMed:10785405, ECO:0000269|Ref.1"
FT /id="VAR_030001"
FT CONFLICT 468
FT /note="Q -> H (in Ref. 1; AAF15317)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="S -> N (in Ref. 1; AAF15317)"
FT /evidence="ECO:0000305"
FT STRAND 258..266
FT /evidence="ECO:0007829|PDB:2V4B"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:2V4B"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:2V4B"
FT HELIX 278..293
FT /evidence="ECO:0007829|PDB:2V4B"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2V4B"
FT STRAND 302..311
FT /evidence="ECO:0007829|PDB:2V4B"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:2V4B"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:2V4B"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:2V4B"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:2V4B"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:2V4B"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:2V4B"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:2V4B"
FT HELIX 395..406
FT /evidence="ECO:0007829|PDB:2V4B"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:2V4B"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:2V4B"
FT HELIX 445..456
FT /evidence="ECO:0007829|PDB:2V4B"
FT TURN 457..460
FT /evidence="ECO:0007829|PDB:2V4B"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:2V4B"
FT HELIX 478..481
FT /evidence="ECO:0007829|PDB:2V4B"
FT HELIX 484..492
FT /evidence="ECO:0007829|PDB:2V4B"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:2JIH"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:2JIH"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:2V4B"
FT STRAND 544..548
FT /evidence="ECO:0007829|PDB:2V4B"
SQ SEQUENCE 967 AA; 105358 MW; 334119D6310A05A7 CRC64;
MQRAVPEGFG RRKLGSDMGN AERAPGSRSF GPVPTLLLLA AALLAVSDAL GRPSEEDEEL
VVPELERAPG HGTTRLRLHA FDQQLDLELR PDSSFLAPGF TLQNVGRKSG SETPLPETDL
AHCFYSGTVN GDPSSAAALS LCEGVRGAFY LLGEAYFIQP LPAASERLAT AAPGEKPPAP
LQFHLLRRNR QGDVGGTCGV VDDEPRPTGK AETEDEDEGT EGEDEGAQWS PQDPALQGVG
QPTGTGSIRK KRFVSSHRYV ETMLVADQSM AEFHGSGLKH YLLTLFSVAA RLYKHPSIRN
SVSLVVVKIL VIHDEQKGPE VTSNAALTLR NFCNWQKQHN PPSDRDAEHY DTAILFTRQD
LCGSQTCDTL GMADVGTVCD PSRSCSVIED DGLQAAFTTA HELGHVFNMP HDDAKQCASL
NGVNQDSHMM ASMLSNLDHS QPWSPCSAYM ITSFLDNGHG ECLMDKPQNP IQLPGDLPGT
SYDANRQCQF TFGEDSKHCP DAASTCSTLW CTGTSGGVLV CQTKHFPWAD GTSCGEGKWC
INGKCVNKTD RKHFDTPFHG SWGMWGPWGD CSRTCGGGVQ YTMRECDNPV PKNGGKYCEG
KRVRYRSCNL EDCPDNNGKT FREEQCEAHN EFSKASFGSG PAVEWIPKYA GVSPKDRCKL
ICQAKGIGYF FVLQPKVVDG TPCSPDSTSV CVQGQCVKAG CDRIIDSKKK FDKCGVCGGN
GSTCKKISGS VTSAKPGYHD IITIPTGATN IEVKQRNQRG SRNNGSFLAI KAADGTYILN
GDYTLSTLEQ DIMYKGVVLR YSGSSAALER IRSFSPLKEP LTIQVLTVGN ALRPKIKYTY
FVKKKKESFN AIPTFSAWVI EEWGECSKSC ELGWQRRLVE CRDINGQPAS ECAKEVKPAS
TRPCADHPCP QWQLGEWSSC SKTCGKGYKK RSLKCLSHDG GVLSHESCDP LKKPKHFIDF
CTMAECS
