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   27-MAR-2024, entry version 164.
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};
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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; 149.
DR   IntAct; Q8TF42; 66.
DR   MINT; Q8TF42; -.
DR   STRING; 9606.ENSP00000284273; -.
DR   DEPOD; UBASH3B; -.
DR   GlyCosmos; Q8TF42; 1 site, 1 glycan.
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; 9606-ENSP00000284273; -.
DR   PeptideAtlas; Q8TF42; -.
DR   ProteomicsDB; 74552; -.
DR   Pumba; Q8TF42; -.
DR   Antibodypedia; 32801; 152 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   AGR; HGNC:29884; -.
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; NMPKEIP; -.
DR   OrthoDB; 5484137at2759; -.
DR   PhylomeDB; Q8TF42; -.
DR   TreeFam; TF313334; -.
DR   PathwayCommons; Q8TF42; -.
DR   SignaLink; Q8TF42; -.
DR   SIGNOR; Q8TF42; -.
DR   BioGRID-ORCS; 84959; 22 hits in 1172 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 149 other cell types or tissues.
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:0009968; P:negative regulation of signal transduction; 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: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   CDD; cd14301; UBA_UBS3B; 1.
DR   Gene3D; 3.90.1140.10; Cyclic phosphodiesterase; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 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   PANTHER; PTHR16469; UBIQUITIN-ASSOCIATED AND SH3 DOMAIN-CONTAINING BA-RELATED; 1.
DR   PANTHER; PTHR16469:SF29; UBIQUITIN-ASSOCIATED AND SH3 DOMAIN-CONTAINING PROTEIN B; 1.
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; SSF53254; Phosphoglycerate mutase-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   Genevisible; Q8TF42; HS.
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
//