ID   UN45B_XENTR             Reviewed;         927 AA.
AC   D7REX8; Q68ER3;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Protein unc-45 homolog B {ECO:0000250|UniProtKB:Q8IWX7};
DE            Short=Unc-45B {ECO:0000250|UniProtKB:Q8IWX7};
GN   Name=unc45b {ECO:0000312|EMBL:ADH10457.1,
GN   ECO:0000312|Xenbase:XB-GENE-971729};
GN   Synonyms=cmya4 {ECO:0000312|EMBL:AAH80138.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ADH10457.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP   OF CYS-779.
RC   TISSUE=Embryo {ECO:0000269|PubMed:20637071};
RX   PubMed=20637071; DOI=10.1186/1471-213x-10-75;
RA   Geach T.J., Zimmerman L.B.;
RT   "Paralysis and delayed Z-disc formation in the Xenopus tropicalis unc45b
RT   mutant dicky ticker.";
RL   BMC Dev. Biol. 10:75-75(2010).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAH80138.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-751.
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH80138.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a co-chaperone for HSP90 and is required for proper
CC       folding of the myosin motor domain (By similarity). Plays a role in
CC       sarcomere formation during muscle cell development. Is necessary for
CC       normal early lens development. {ECO:0000250|UniProtKB:Q6DGE9,
CC       ECO:0000250|UniProtKB:Q8CGY6, ECO:0000269|PubMed:20637071}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC       {ECO:0000250|UniProtKB:Q6DGE9}. Cytoplasm, myofibril, sarcomere, A band
CC       {ECO:0000250|UniProtKB:Q8IWX7}. Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q6DGE9}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q8CGY6}. Note=Expressed at the Z line and in the
CC       perinuclear region of myofibrils. Translocates to the A band in
CC       response to stress conditions and fibril damage.
CC       {ECO:0000250|UniProtKB:Q6DGE9}.
CC   -!- TISSUE SPECIFICITY: Detected initially throughout the somites and the
CC       heart and gradually also expressed in the jaw, branchial arches and
CC       body wall muscles at later embryonic stages.
CC       {ECO:0000269|PubMed:20637071}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH80138.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; HM053434; ADH10457.1; -; mRNA.
DR   EMBL; BC080138; AAH80138.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001172057.1; NM_001185128.1.
DR   AlphaFoldDB; D7REX8; -.
DR   SMR; D7REX8; -.
DR   PaxDb; D7REX8; -.
DR   GeneID; 493194; -.
DR   KEGG; xtr:493194; -.
DR   CTD; 146862; -.
DR   Xenbase; XB-GENE-971729; unc45b.
DR   eggNOG; KOG4151; Eukaryota.
DR   HOGENOM; CLU_007331_0_0_1; -.
DR   InParanoid; D7REX8; -.
DR   OMA; AMHEDPE; -.
DR   OrthoDB; 1059433at2759; -.
DR   PhylomeDB; D7REX8; -.
DR   TreeFam; TF314096; -.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000013482; Expressed in heart and 15 other tissues.
DR   GO; GO:0031672; C:A band; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR   GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR   GO; GO:0002088; P:lens development in camera-type eye; ISS:UniProtKB.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; -; 2.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR024660; UCS_central_dom.
DR   Pfam; PF11701; UNC45-central; 1.
DR   SMART; SM00185; ARM; 4.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48371; SSF48371; 2.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; Developmental protein; Differentiation; Myogenesis;
KW   Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..927
FT                   /note="Protein unc-45 homolog B"
FT                   /id="PRO_0000410949"
FT   REPEAT          4..37
FT                   /note="TPR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          41..74
FT                   /note="TPR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          76..108
FT                   /note="TPR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          167..206
FT                   /note="ARM 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          209..248
FT                   /note="ARM 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          746..785
FT                   /note="ARM 3"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         779
FT                   /note="C->R: In dicky ticker (dit) mutant; impairs
FT                   sarcomere formation. Causes paralysis and loss of
FT                   heartbeat."
FT                   /evidence="ECO:0000269|PubMed:20637071"
SQ   SEQUENCE   927 AA;  103537 MW;  2EBA213797B3FE80 CRC64;
     MEDPVQLKEE GNKYFQSNEY GQAIQCYSKA LKLITDKKMQ AVLYRNRSAC YLKQDNYVQA
     AADASKAIDV DASDIKALFR RCQALEKLGK LDQAYKDVQR CATLEPKNRT FLETLHRLGT
     NIQEKLHVQF STDSRVHKMF EILLDKNSEK EKREKAANNL IVLGREDAGA EQIFQNNGVN
     LLMQLIESKD PEMILSAIRT LSGMCTGHRA RATAIVHLVG INKICSIMAV DNEEIALAAC
     NLLQNIVDSL TGEDKKAHGK QEALVLDTKK DLKIITTHLL DMLVSKKVSG HGRDQALNLL
     NKNIPRYDLK NKDNSKSLFV VDAGLKKILK VLGQVPELPN CLPLTPNTRL NASVLVNKLY
     DDLRCDPERD NFRIICEEYI TGSFDPKDME KNLHAIQTVS GILQGPFDLG NKLLSLQGVM
     EMMVALTGSE NEVDQLVAVE ALIHASTKLS RASFIITNGV SLLKDIYKKT KNEKIKIRAL
     VGLCKLGSAG GTDYALRQFA EGSTDKLAKQ CRKWLCNPSL DIQTRKWAVE GLAYLTLDAD
     VKDEFVEDEQ SLKAMFELSK TSDKTILYSV ATTLVNCTNS YDVKEVIPEM VQLAKFSKQH
     VPEQHPKDKK DFVEKRVKRL LKADVISALS CMVKADNSIL TDQTKEQLSR VFLALCEDPK
     DRGIIVAQGG GKAMIPLALE GTDVGKIKAS HGLAKIAAVS NPDIAFPGER VYEVVRPLVS
     LLNTERDGIQ NFEALLALTN LSGKNDKLRQ KIIKEKALPE IENYMFENHE QIRQAATECM
     CNLALNKEVK ERFMAEGNDR LKLIILLCGE EDEVKLQRAA AGTLAMLTGA EKKLCHKMTE
     VTTQWMEILQ RLCLSEDLQV QHRGVVIAYN LINADKELAK KLVESEMLEI LTVIGKQADV
     PNKQHIINAA REALVKCLDY GFIKTVS