UBS3B_HUMAN
ID UBS3B_HUMAN Reviewed; 649 AA.
AC Q8TF42; Q53GT5; Q53GT8; Q8NBV7; Q96IG9; Q96NZ2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ubiquitin-associated and SH3 domain-containing protein B;
DE EC=3.1.3.48;
DE AltName: Full=Cbl-interacting protein p70;
DE AltName: Full=Suppressor of T-cell receptor signaling 1;
DE Short=STS-1;
DE AltName: Full=T-cell ubiquitin ligand 2;
DE Short=TULA-2;
DE AltName: Full=Tyrosine-protein phosphatase STS1/TULA2;
GN Name=UBASH3B; Synonyms=KIAA1959, STS1;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-68.
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 PROTEIN SEQUENCE OF 89-112; 188-199; 230-237 AND 417-428, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 116-649.
RA Engel M., Seifert M., Maschlanka M., Welter C.;
RT "A novel SH3 containing protein is phosphorylated by the nm23-H1 protein
RT kinase activity in vitro and shows reduced mRNA expression in human
RT tumors.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP FUNCTION, INTERACTION WITH CBL AND UBIQUITIN, AND IDENTIFICATION IN A
RP COMPLEX WITH EGFR.
RX PubMed=15159412; DOI=10.1074/jbc.m403759200;
RA Kowanetz K., Crosetto N., Haglund K., Schmidt M.H., Heldin C.-H., Dikic I.;
RT "Suppressors of T-cell receptor signaling Sts-1 and Sts-2 bind to Cbl and
RT inhibit endocytosis of receptor tyrosine kinases.";
RL J. Biol. Chem. 279:32786-32795(2004).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17880946; DOI=10.1016/j.febslet.2007.08.077;
RA Raguz J., Wagner S., Dikic I., Hoeller D.;
RT "Suppressor of T-cell receptor signalling 1 and 2 differentially regulate
RT endocytosis and signalling of receptor tyrosine kinases.";
RL FEBS Lett. 581:4767-4772(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-23, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP INTERACTION WITH ZAP70.
RX PubMed=26903241; DOI=10.1084/jem.20151426;
RA Hu H., Wang H., Xiao Y., Jin J., Chang J.H., Zou Q., Xie X., Cheng X.,
RA Sun S.C.;
RT "Otud7b facilitates T cell activation and inflammatory responses by
RT regulating Zap70 ubiquitination.";
RL J. Exp. Med. 213:399-414(2016).
RN [12]
RP STRUCTURE BY NMR OF 26-76.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-031, a UBA domain from human cDNA.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [13]
RP STRUCTURE BY NMR OF 248-328.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of SH3 domain in suppressor of T-cell receptor
RT signaling 1.";
RL Submitted (JUN-2007) to the PDB data bank.
CC -!- FUNCTION: Interferes with CBL-mediated down-regulation and degradation
CC of receptor-type tyrosine kinases. Promotes accumulation of activated
CC target receptors, such as T-cell receptors and EGFR, on the cell
CC surface. Exhibits tyrosine phosphatase activity toward several
CC substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins
CC that are dually modified by both protein tyrosine phosphorylation and
CC ubiquitination. {ECO:0000269|PubMed:15159412,
CC ECO:0000269|PubMed:17880946}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:17880946};
CC -!- SUBUNIT: Homodimer. Interacts with JAK2 (in vitro) (By similarity).
CC Interacts with CBL (PubMed:15159412). Part of a complex containing CBL
CC and activated EGFR (PubMed:15159412). Interacts with ubiquitin and with
CC mono-ubiquitinated proteins (PubMed:15159412). Interacts with ZAP70
CC (ubiquitinated form) (PubMed:26903241). {ECO:0000250|UniProtKB:Q8BGG7,
CC ECO:0000269|PubMed:15159412, ECO:0000269|PubMed:26903241}.
CC -!- INTERACTION:
CC Q8TF42; Q96PG8: BBC3; NbExp=3; IntAct=EBI-1380492, EBI-17289784;
CC Q8TF42; Q13191: CBLB; NbExp=6; IntAct=EBI-1380492, EBI-744027;
CC Q8TF42; Q96LY2-2: CCDC74B; NbExp=3; IntAct=EBI-1380492, EBI-17967022;
CC Q8TF42; Q15038: DAZAP2; NbExp=6; IntAct=EBI-1380492, EBI-724310;
CC Q8TF42; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-1380492, EBI-11988027;
CC Q8TF42; Q9P1A6-3: DLGAP2; NbExp=3; IntAct=EBI-1380492, EBI-12019838;
CC Q8TF42; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-1380492, EBI-9679045;
CC Q8TF42; Q14183: DOC2A; NbExp=5; IntAct=EBI-1380492, EBI-20861623;
CC Q8TF42; Q8N9I9: DTX3; NbExp=3; IntAct=EBI-1380492, EBI-2340258;
CC Q8TF42; O43281-2: EFS; NbExp=3; IntAct=EBI-1380492, EBI-11525448;
CC Q8TF42; Q92567: FAM168A; NbExp=4; IntAct=EBI-1380492, EBI-7957930;
CC Q8TF42; P14652: HOXB2; NbExp=3; IntAct=EBI-1380492, EBI-5329558;
CC Q8TF42; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1380492, EBI-6509505;
CC Q8TF42; Q92993: KAT5; NbExp=3; IntAct=EBI-1380492, EBI-399080;
CC Q8TF42; O60341: KDM1A; NbExp=3; IntAct=EBI-1380492, EBI-710124;
CC Q8TF42; Q5T749: KPRP; NbExp=5; IntAct=EBI-1380492, EBI-10981970;
CC Q8TF42; P25791-3: LMO2; NbExp=3; IntAct=EBI-1380492, EBI-11959475;
CC Q8TF42; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-1380492, EBI-741037;
CC Q8TF42; O75928-2: PIAS2; NbExp=3; IntAct=EBI-1380492, EBI-348567;
CC Q8TF42; P0CG20: PRR35; NbExp=3; IntAct=EBI-1380492, EBI-11986293;
CC Q8TF42; P20618: PSMB1; NbExp=3; IntAct=EBI-1380492, EBI-372273;
CC Q8TF42; Q16825: PTPN21; NbExp=3; IntAct=EBI-1380492, EBI-2860264;
CC Q8TF42; Q96PM5: RCHY1; NbExp=6; IntAct=EBI-1380492, EBI-947779;
CC Q8TF42; Q04864-2: REL; NbExp=3; IntAct=EBI-1380492, EBI-10829018;
CC Q8TF42; Q9NWF9: RNF216; NbExp=3; IntAct=EBI-1380492, EBI-723313;
CC Q8TF42; Q6ZT89: SLC25A48; NbExp=3; IntAct=EBI-1380492, EBI-10255185;
CC Q8TF42; O43597: SPRY2; NbExp=3; IntAct=EBI-1380492, EBI-742487;
CC Q8TF42; P43405: SYK; NbExp=2; IntAct=EBI-1380492, EBI-78302;
CC Q8TF42; P15884-3: TCF4; NbExp=3; IntAct=EBI-1380492, EBI-13636688;
CC Q8TF42; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-1380492, EBI-11139477;
CC Q8TF42; O95271: TNKS; NbExp=3; IntAct=EBI-1380492, EBI-1105254;
CC Q8TF42; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-1380492, EBI-11952721;
CC Q8TF42; Q8TF42: UBASH3B; NbExp=4; IntAct=EBI-1380492, EBI-1380492;
CC Q8TF42; Q9H9H4: VPS37B; NbExp=6; IntAct=EBI-1380492, EBI-4400866;
CC Q8TF42; O00401: WASL; NbExp=3; IntAct=EBI-1380492, EBI-957615;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL16953.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB85545.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB075839; BAB85545.1; ALT_INIT; mRNA.
DR EMBL; AK075203; BAC11468.1; -; mRNA.
DR EMBL; AK222843; BAD96563.1; -; mRNA.
DR EMBL; AK222846; BAD96566.1; -; mRNA.
DR EMBL; BC007541; AAH07541.2; -; mRNA.
DR EMBL; AF425252; AAL16953.1; ALT_INIT; mRNA.
DR CCDS; CCDS31694.1; -.
DR RefSeq; NP_116262.2; NM_032873.4.
DR PDB; 2CPW; NMR; -; A=26-76.
DR PDB; 2E5K; NMR; -; A=248-328.
DR PDB; 5VR6; X-ray; 1.87 A; A/B=384-649.
DR PDB; 5W5G; X-ray; 2.48 A; A/B/C=383-644.
DR PDBsum; 2CPW; -.
DR PDBsum; 2E5K; -.
DR PDBsum; 5VR6; -.
DR PDBsum; 5W5G; -.
DR AlphaFoldDB; Q8TF42; -.
DR BMRB; Q8TF42; -.
DR SMR; Q8TF42; -.
DR BioGRID; 124390; 146.
DR IntAct; Q8TF42; 65.
DR MINT; Q8TF42; -.
DR STRING; 9606.ENSP00000284273; -.
DR DEPOD; UBASH3B; -.
DR GlyGen; Q8TF42; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TF42; -.
DR PhosphoSitePlus; Q8TF42; -.
DR BioMuta; UBASH3B; -.
DR DMDM; 110287974; -.
DR EPD; Q8TF42; -.
DR jPOST; Q8TF42; -.
DR MassIVE; Q8TF42; -.
DR MaxQB; Q8TF42; -.
DR PaxDb; Q8TF42; -.
DR PeptideAtlas; Q8TF42; -.
DR PRIDE; Q8TF42; -.
DR ProteomicsDB; 74552; -.
DR Antibodypedia; 32801; 145 antibodies from 26 providers.
DR DNASU; 84959; -.
DR Ensembl; ENST00000284273.6; ENSP00000284273.5; ENSG00000154127.10.
DR GeneID; 84959; -.
DR KEGG; hsa:84959; -.
DR MANE-Select; ENST00000284273.6; ENSP00000284273.5; NM_032873.5; NP_116262.2.
DR UCSC; uc001pyi.5; human.
DR CTD; 84959; -.
DR DisGeNET; 84959; -.
DR GeneCards; UBASH3B; -.
DR HGNC; HGNC:29884; UBASH3B.
DR HPA; ENSG00000154127; Tissue enhanced (brain, lymphoid tissue, placenta).
DR MIM; 609201; gene.
DR neXtProt; NX_Q8TF42; -.
DR OpenTargets; ENSG00000154127; -.
DR PharmGKB; PA162407840; -.
DR VEuPathDB; HostDB:ENSG00000154127; -.
DR eggNOG; KOG3734; Eukaryota.
DR GeneTree; ENSGT00940000156097; -.
DR HOGENOM; CLU_016516_1_0_1; -.
DR InParanoid; Q8TF42; -.
DR OMA; PNFMGFF; -.
DR OrthoDB; 243749at2759; -.
DR PhylomeDB; Q8TF42; -.
DR TreeFam; TF313334; -.
DR PathwayCommons; Q8TF42; -.
DR SignaLink; Q8TF42; -.
DR SIGNOR; Q8TF42; -.
DR BioGRID-ORCS; 84959; 14 hits in 1077 CRISPR screens.
DR ChiTaRS; UBASH3B; human.
DR EvolutionaryTrace; Q8TF42; -.
DR GeneWiki; STS-1_(gene); -.
DR GenomeRNAi; 84959; -.
DR Pharos; Q8TF42; Tbio.
DR PRO; PR:Q8TF42; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8TF42; protein.
DR Bgee; ENSG00000154127; Expressed in pons and 148 other tissues.
DR Genevisible; Q8TF42; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0045779; P:negative regulation of bone resorption; IBA:GO_Central.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; IEA:Ensembl.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0009968; P:negative regulation of signal transduction; IBA:GO_Central.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IBA:GO_Central.
DR GO; GO:0070527; P:platelet aggregation; IBA:GO_Central.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IBA:GO_Central.
DR GO; GO:0043393; P:regulation of protein binding; IEA:Ensembl.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR CDD; cd07067; HP_PGM_like; 1.
DR CDD; cd11936; SH3_UBASH3B; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR035632; UBASH3B_SH3.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus;
KW Phosphoprotein; Protein phosphatase; Reference proteome; SH3 domain.
FT CHAIN 1..649
FT /note="Ubiquitin-associated and SH3 domain-containing
FT protein B"
FT /id="PRO_0000245508"
FT DOMAIN 27..76
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 254..319
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 380..649
FT /note="Protein tyrosine phosphatase"
FT /evidence="ECO:0000250"
FT ACT_SITE 390
FT /evidence="ECO:0000250"
FT ACT_SITE 391
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 576
FT /evidence="ECO:0000250"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 23
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 68
FT /note="A -> T (in dbSNP:rs12790613)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_052676"
FT VARIANT 569
FT /note="N -> S (in dbSNP:rs35343548)"
FT /id="VAR_061923"
FT CONFLICT 465
FT /note="H -> R (in Ref. 3; BAD96563/BAD96566)"
FT /evidence="ECO:0000305"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2CPW"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:2CPW"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:2CPW"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:2CPW"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:2CPW"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2E5K"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:2E5K"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:2E5K"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:2E5K"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:2E5K"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:2E5K"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:2E5K"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:2E5K"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:2E5K"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:2E5K"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 395..399
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 403..407
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 432..437
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 443..458
FT /evidence="ECO:0007829|PDB:5VR6"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 472..485
FT /evidence="ECO:0007829|PDB:5VR6"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:5VR6"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:5VR6"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 517..522
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 537..539
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 546..564
FT /evidence="ECO:0007829|PDB:5VR6"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:5W5G"
FT STRAND 569..575
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 579..582
FT /evidence="ECO:0007829|PDB:5VR6"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 595..602
FT /evidence="ECO:0007829|PDB:5VR6"
FT STRAND 610..615
FT /evidence="ECO:0007829|PDB:5VR6"
FT TURN 617..619
FT /evidence="ECO:0007829|PDB:5VR6"
FT STRAND 622..625
FT /evidence="ECO:0007829|PDB:5VR6"
FT HELIX 642..645
FT /evidence="ECO:0007829|PDB:5VR6"
SQ SEQUENCE 649 AA; 72696 MW; 70ED9F50EA20BF43 CRC64;
MAQYGHPSPL GMAAREELYS KVTPRRNRQQ RPGTIKHGSA LDVLLSMGFP RARAQKALAS
TGGRSVQAAC DWLFSHVGDP FLDDPLPREY VLYLRPTGPL AQKLSDFWQQ SKQICGKNKA
HNIFPHITLC QFFMCEDSKV DALGEALQTT VSRWKCKFSA PLPLELYTSS NFIGLFVKED
SAEVLKKFAA DFAAEAASKT EVHVEPHKKQ LHVTLAYHFQ ASHLPTLEKL AQNIDVKLGC
DWVATIFSRD IRFANHETLQ VIYPYTPQND DELELVPGDF IFMSPMEQTS TSEGWIYGTS
LTTGCSGLLP ENYITKADEC STWIFHGSYS ILNTSSSNSL TFGDGVLERR PYEDQGLGET
TPLTIICQPM QPLRVNSQPG PQKRCLFVCR HGERMDVVFG KYWLSQCFDA KGRYIRTNLN
MPHSLPQRSG GFRDYEKDAP ITVFGCMQAR LVGEALLESN TIIDHVYCSP SLRCVQTAHN
ILKGLQQENH LKIRVEPGLF EWTKWVAGST LPAWIPPSEL AAANLSVDTT YRPHIPISKL
VVSESYDTYI SRSFQVTKEI ISECKSKGNN ILIVAHASSL EACTCQLQGL SPQNSKDFVQ
MVRKIPYLGF CSCEELGETG IWQLTDPPIL PLTHGPTGGF NWRETLLQE
