ATS5_HUMAN
ID ATS5_HUMAN Reviewed; 930 AA.
AC Q9UNA0; Q52LV4; Q9UKP2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 5;
DE Short=ADAM-TS 5;
DE Short=ADAM-TS5;
DE Short=ADAMTS-5;
DE EC=3.4.24.-;
DE AltName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 11;
DE Short=ADAM-TS 11;
DE Short=ADAMTS-11;
DE AltName: Full=ADMP-2;
DE AltName: Full=Aggrecanase-2;
DE Flags: Precursor;
GN Name=ADAMTS5; Synonyms=ADAMTS11, ADMP2;
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 VARIANTS ALA-138 AND PRO-692.
RC TISSUE=Liver;
RX PubMed=10438522; DOI=10.1074/jbc.274.33.23443;
RA Abbaszade I., Liu R.-Q., Yang F., Rosenfeld S.A., Ross O.H., Link J.R.,
RA Ellis D.M., Tortorella M.D., Pratta M.A., Hollis J.M., Wynn R., Duke J.L.,
RA George H.J., Hillman M.C. Jr., Murphy K., Wiswall B.H., Copeland R.A.,
RA Decicco C.P., Bruckner R., Nagase H., Ito Y., Newton R.C., Magolda R.L.,
RA Trzaskos J.M., Hollis G.F., Arner E.C., Burn T.C.;
RT "Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS
RT family.";
RL J. Biol. Chem. 274:23443-23450(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-138 AND PRO-692.
RC TISSUE=Colon;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 413-930, AND VARIANTS HIS-614 AND PRO-692.
RC TISSUE=Fetal brain;
RX PubMed=10464288; DOI=10.1074/jbc.274.36.25555;
RA Hurskainen T.L., Hirohata S., Seldin M.F., Apte S.S.;
RT "ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc
RT metalloproteases.";
RL J. Biol. Chem. 274:25555-25563(1999).
RN [5]
RP FUNCTION.
RX PubMed=16133547; DOI=10.1007/s00401-005-1032-6;
RA Nakada M., Miyamori H., Kita D., Takahashi T., Yamashita J., Sato H.,
RA Miura R., Yamaguchi Y., Okada Y.;
RT "Human glioblastomas overexpress ADAMTS-5 that degrades brevican.";
RL Acta Neuropathol. 110:239-246(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, CLEAVAGE, AND MUTAGENESIS OF GLU-411.
RX PubMed=18992360; DOI=10.1016/j.biocel.2008.10.008;
RA Longpre J.M., McCulloch D.R., Koo B.H., Alexander J.P., Apte S.S.,
RA Leduc R.;
RT "Characterization of proADAMTS5 processing by proprotein convertases.";
RL Int. J. Biochem. Cell Biol. 41:1116-1126(2009).
RN [7]
RP GLYCOSYLATION AT TRP-570; TRP-573 AND SER-582, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19671700; DOI=10.1074/jbc.m109.038059;
RA Wang L.W., Leonhard-Melief C., Haltiwanger R.S., Apte S.S.;
RT "Post-translational modification of thrombospondin type-1 repeats in
RT ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.";
RL J. Biol. Chem. 284:30004-30015(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 262-628 IN COMPLEX WITH INHIBITOR,
RP ACTIVE SITE, COFACTOR, ZINC-BINDING SITES, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-498.
RX PubMed=18042673; DOI=10.1110/ps.073287008;
RA Mosyak L., Georgiadis K., Shane T., Svenson K., Hebert T., McDonagh T.,
RA Mackie S., Olland S., Lin L., Zhong X., Kriz R., Reifenberg E.L.,
RA Collins-Racie L.A., Corcoran C., Freeman B., Zollner R., Marvell T.,
RA Vera M., Sum P.E., Lavallie E.R., Stahl M., Somers W.;
RT "Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4
RT and ADAMTS5.";
RL Protein Sci. 17:16-21(2008).
CC -!- FUNCTION: Metalloproteinase that plays an important role in connective
CC tissue organization, development, inflammation and cell migration.
CC Extracellular matrix (ECM) degrading enzyme that show proteolytic
CC activity toward the hyalectan group of chondroitin sulfate
CC proteoglycans (CSPGs) including ACAN, VCAN, BCAN and NCAN
CC (PubMed:16133547, PubMed:18992360). Cleavage within the hyalectans
CC occurs at Glu-Xaa recognition motifs. Plays a role in embryonic
CC development, including limb and cardiac morphogenesis, and skeletal
CC muscle development through its VCAN remodeling properties. Cleaves VCAN
CC in the pericellular matrix surrounding myoblasts, facilitating myoblast
CC contact and fusion which is required for skeletal muscle development
CC and regeneration (By similarity). Participates in development of brown
CC adipose tissue and browning of white adipose tissue (By similarity).
CC Plays an important role for T-lymphocyte migration from draining lymph
CC nodes following viral infection. {ECO:0000250|UniProtKB:Q9R001,
CC ECO:0000269|PubMed:16133547, ECO:0000269|PubMed:18992360}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:18042673};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18042673};
CC -!- INTERACTION:
CC Q9UNA0; P13608: ACAN; Xeno; NbExp=2; IntAct=EBI-2808663, EBI-6259246;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:18992360}.
CC -!- TISSUE SPECIFICITY: Expressed at low level in placenta primarily but
CC also detected in heart and brain, cervix, uterus, bladder, esophagus,
CC rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from
CC an arthritic patient.
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 furin and PCSK7 outside of the cell.
CC {ECO:0000269|PubMed:18992360}.
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; AF142099; AAD49577.1; -; mRNA.
DR EMBL; AP001698; BAA95504.1; -; Genomic_DNA.
DR EMBL; AP001697; BAA95503.1; -; Genomic_DNA.
DR EMBL; BC093775; AAH93775.1; -; mRNA.
DR EMBL; BC093777; AAH93777.1; -; mRNA.
DR EMBL; AF141293; AAF02493.1; -; mRNA.
DR CCDS; CCDS13579.1; -.
DR RefSeq; NP_008969.2; NM_007038.4.
DR PDB; 2RJQ; X-ray; 2.60 A; A=262-628.
DR PDB; 3B8Z; X-ray; 1.40 A; A/B=264-480.
DR PDB; 3HY7; X-ray; 1.69 A; A/B=262-480.
DR PDB; 3HY9; X-ray; 2.02 A; A/B=262-480.
DR PDB; 3HYG; X-ray; 1.40 A; A/B=262-480.
DR PDB; 3LJT; X-ray; 1.60 A; A=264-480.
DR PDB; 6YJM; X-ray; 2.25 A; A/B=264-481.
DR PDBsum; 2RJQ; -.
DR PDBsum; 3B8Z; -.
DR PDBsum; 3HY7; -.
DR PDBsum; 3HY9; -.
DR PDBsum; 3HYG; -.
DR PDBsum; 3LJT; -.
DR PDBsum; 6YJM; -.
DR AlphaFoldDB; Q9UNA0; -.
DR SMR; Q9UNA0; -.
DR BioGRID; 116277; 1.
DR IntAct; Q9UNA0; 4.
DR STRING; 9606.ENSP00000284987; -.
DR BindingDB; Q9UNA0; -.
DR ChEMBL; CHEMBL2285; -.
DR DrugBank; DB06837; (2R)-N~4~-hydroxy-2-(3-hydroxybenzyl)-N~1~-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide.
DR DrugBank; DB03880; Batimastat.
DR DrugBank; DB06945; N-hydroxy-4-({4-[4-(trifluoromethyl)phenoxy]phenyl}sulfonyl)tetrahydro-2H-pyran-4-carboxamide.
DR GuidetoPHARMACOLOGY; 1678; -.
DR MEROPS; M12.225; -.
DR GlyConnect; 2006; 1 O-Linked glycan (1 site).
DR GlyGen; Q9UNA0; 9 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q9UNA0; -.
DR PhosphoSitePlus; Q9UNA0; -.
DR BioMuta; ADAMTS5; -.
DR DMDM; 317373326; -.
DR jPOST; Q9UNA0; -.
DR MassIVE; Q9UNA0; -.
DR PaxDb; Q9UNA0; -.
DR PeptideAtlas; Q9UNA0; -.
DR PRIDE; Q9UNA0; -.
DR ProteomicsDB; 85273; -.
DR ABCD; Q9UNA0; 30 sequenced antibodies.
DR Antibodypedia; 986; 434 antibodies from 34 providers.
DR DNASU; 11096; -.
DR Ensembl; ENST00000284987.6; ENSP00000284987.5; ENSG00000154736.6.
DR GeneID; 11096; -.
DR KEGG; hsa:11096; -.
DR MANE-Select; ENST00000284987.6; ENSP00000284987.5; NM_007038.5; NP_008969.2.
DR UCSC; uc002ymg.4; human.
DR CTD; 11096; -.
DR DisGeNET; 11096; -.
DR GeneCards; ADAMTS5; -.
DR HGNC; HGNC:221; ADAMTS5.
DR HPA; ENSG00000154736; Tissue enhanced (placenta).
DR MIM; 605007; gene.
DR neXtProt; NX_Q9UNA0; -.
DR OpenTargets; ENSG00000154736; -.
DR VEuPathDB; HostDB:ENSG00000154736; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000159090; -.
DR HOGENOM; CLU_000660_3_0_1; -.
DR InParanoid; Q9UNA0; -.
DR OMA; TPCPPNG; -.
DR OrthoDB; 125522at2759; -.
DR PhylomeDB; Q9UNA0; -.
DR TreeFam; TF331949; -.
DR BRENDA; 3.4.24.B12; 2681.
DR PathwayCommons; Q9UNA0; -.
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; Q9UNA0; -.
DR SIGNOR; Q9UNA0; -.
DR BioGRID-ORCS; 11096; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; ADAMTS5; human.
DR EvolutionaryTrace; Q9UNA0; -.
DR GeneWiki; ADAMTS5; -.
DR GenomeRNAi; 11096; -.
DR Pharos; Q9UNA0; Tchem.
DR PRO; PR:Q9UNA0; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9UNA0; protein.
DR Bgee; ENSG00000154736; Expressed in mammary duct and 181 other tissues.
DR ExpressionAtlas; Q9UNA0; baseline and differential.
DR Genevisible; Q9UNA0; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; TAS:ProtInc.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISS:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0007520; P:myoblast fusion; ISS:UniProtKB.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR GO; GO:0044691; P:tooth eruption; IEA:Ensembl.
DR DisProt; DP02607; -.
DR Gene3D; 2.20.100.10; -; 2.
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; IPR013276; Pept_M12B_ADAM-TS5.
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; PR01860; ADAMTS5.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 2.
DR SUPFAM; SSF82895; SSF82895; 2.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 2.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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..16
FT /evidence="ECO:0000255"
FT PROPEP 17..261
FT /evidence="ECO:0000269|PubMed:18992360"
FT /id="PRO_0000029170"
FT CHAIN 262..930
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 5"
FT /id="PRO_0000029171"
FT DOMAIN 267..476
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 485..566
FT /note="Disintegrin"
FT DOMAIN 567..622
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 875..929
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 24..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..874
FT /note="Spacer"
FT MOTIF 207..214
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 46..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:18042673"
FT BINDING 209
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 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18042673"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18042673"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18042673"
FT SITE 261
FT /note="Cleavage; by furin and PCSK7"
FT /evidence="ECO:0000269|PubMed:18992360"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18042673"
FT CARBOHYD 570
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:19671700"
FT CARBOHYD 573
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:19671700"
FT CARBOHYD 582
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:19671700"
FT CARBOHYD 728
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 342..394
FT /evidence="ECO:0000269|PubMed:18042673"
FT DISULFID 371..376
FT /evidence="ECO:0000269|PubMed:18042673"
FT DISULFID 388..471
FT /evidence="ECO:0000269|PubMed:18042673"
FT DISULFID 426..455
FT /evidence="ECO:0000269|PubMed:18042673"
FT DISULFID 497..519
FT /evidence="ECO:0000269|PubMed:18042673"
FT DISULFID 508..529
FT /evidence="ECO:0000269|PubMed:18042673"
FT DISULFID 514..548
FT /evidence="ECO:0000269|PubMed:18042673"
FT DISULFID 542..553
FT /evidence="ECO:0000269|PubMed:18042673"
FT DISULFID 579..616
FT /evidence="ECO:0000250"
FT DISULFID 583..621
FT /evidence="ECO:0000250"
FT DISULFID 594..606
FT /evidence="ECO:0000250"
FT VARIANT 138
FT /note="G -> A (in dbSNP:rs457947)"
FT /evidence="ECO:0000269|PubMed:10438522,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_028199"
FT VARIANT 614
FT /note="R -> H (in dbSNP:rs2830585)"
FT /evidence="ECO:0000269|PubMed:10464288"
FT /id="VAR_021849"
FT VARIANT 692
FT /note="L -> P (in dbSNP:rs226794)"
FT /evidence="ECO:0000269|PubMed:10438522,
FT ECO:0000269|PubMed:10464288, ECO:0000269|PubMed:15489334"
FT /id="VAR_028200"
FT MUTAGEN 411
FT /note="E->A: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:18992360"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:3B8Z"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:3B8Z"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3B8Z"
FT HELIX 287..302
FT /evidence="ECO:0007829|PDB:3B8Z"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:3B8Z"
FT STRAND 311..320
FT /evidence="ECO:0007829|PDB:3B8Z"
FT TURN 323..326
FT /evidence="ECO:0007829|PDB:3HYG"
FT HELIX 334..348
FT /evidence="ECO:0007829|PDB:3B8Z"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:3LJT"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:3B8Z"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:3B8Z"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:3B8Z"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:3B8Z"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:3B8Z"
FT HELIX 404..415
FT /evidence="ECO:0007829|PDB:3B8Z"
FT HELIX 424..430
FT /evidence="ECO:0007829|PDB:3B8Z"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:3B8Z"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:2RJQ"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:3LJT"
FT HELIX 454..465
FT /evidence="ECO:0007829|PDB:3B8Z"
FT TURN 466..469
FT /evidence="ECO:0007829|PDB:3B8Z"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:3B8Z"
FT HELIX 487..490
FT /evidence="ECO:0007829|PDB:2RJQ"
FT HELIX 493..501
FT /evidence="ECO:0007829|PDB:2RJQ"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:2RJQ"
FT TURN 513..515
FT /evidence="ECO:0007829|PDB:2RJQ"
FT STRAND 519..523
FT /evidence="ECO:0007829|PDB:2RJQ"
FT STRAND 526..530
FT /evidence="ECO:0007829|PDB:2RJQ"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:2RJQ"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:2RJQ"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:2RJQ"
SQ SEQUENCE 930 AA; 101718 MW; 8CCE448A15A29CE8 CRC64;
MLLGWASLLL CAFRLPLAAV GPAATPAQDK AGQPPTAAAA AQPRRRQGEE VQERAEPPGH
PHPLAQRRRS KGLVQNIDQL YSGGGKVGYL VYAGGRRFLL DLERDGSVGI AGFVPAGGGT
SAPWRHRSHC FYRGTVDGSP RSLAVFDLCG GLDGFFAVKH ARYTLKPLLR GPWAEEEKGR
VYGDGSARIL HVYTREGFSF EALPPRASCE TPASTPEAHE HAPAHSNPSG RAALASQLLD
QSALSPAGGS GPQTWWRRRR RSISRARQVE LLLVADASMA RLYGRGLQHY LLTLASIANR
LYSHASIENH IRLAVVKVVV LGDKDKSLEV SKNAATTLKN FCKWQHQHNQ LGDDHEEHYD
AAILFTREDL CGHHSCDTLG MADVGTICSP ERSCAVIEDD GLHAAFTVAH EIGHLLGLSH
DDSKFCEETF GSTEDKRLMS SILTSIDASK PWSKCTSATI TEFLDDGHGN CLLDLPRKQI
LGPEELPGQT YDATQQCNLT FGPEYSVCPG MDVCARLWCA VVRQGQMVCL TKKLPAVEGT
PCGKGRICLQ GKCVDKTKKK YYSTSSHGNW GSWGSWGQCS RSCGGGVQFA YRHCNNPAPR
NNGRYCTGKR AIYRSCSLMP CPPNGKSFRH EQCEAKNGYQ SDAKGVKTFV EWVPKYAGVL
PADVCKLTCR AKGTGYYVVF SPKVTDGTEC RLYSNSVCVR GKCVRTGCDG IIGSKLQYDK
CGVCGGDNSS CTKIVGTFNK KSKGYTDVVR IPEGATHIKV RQFKAKDQTR FTAYLALKKK
NGEYLINGKY MISTSETIID INGTVMNYSG WSHRDDFLHG MGYSATKEIL IVQILATDPT
KPLDVRYSFF VPKKSTPKVN SVTSHGSNKV GSHTSQPQWV TGPWLACSRT CDTGWHTRTV
QCQDGNRKLA KGCPLSQRPS AFKQCLLKKC
