UN45B_DANRE
ID UN45B_DANRE Reviewed; 934 AA.
AC Q6DGE9; Q8UVX6;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein unc-45 homolog B {ECO:0000250|UniProtKB:Q8IWX7, ECO:0000312|EMBL:AAH76400.1};
DE Short=Unc-45B {ECO:0000250|UniProtKB:Q8IWX7};
DE AltName: Full=UNC45-related protein {ECO:0000312|EMBL:AAL57031.1};
GN Name=unc45b {ECO:0000312|ZFIN:ZDB-GENE-020919-3};
GN Synonyms=unc45r {ECO:0000312|ZFIN:ZDB-GENE-020919-3};
GN ORFNames=si:ch211-204d2.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL57031.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:12203738};
RX PubMed=12203738; DOI=10.1002/dvdy.10123;
RA Etheridge L., Diiorio P., Sagerstrom C.G.;
RT "A zebrafish unc-45-related gene expressed during muscle development.";
RL Dev. Dyn. 224:457-460(2002).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=AB {ECO:0000269|PubMed:17189627};
RX PubMed=17189627; DOI=10.1016/j.ydbio.2006.11.027;
RA Wohlgemuth S.L., Crawford B.D., Pilgrim D.B.;
RT "The myosin co-chaperone UNC-45 is required for skeletal and cardiac muscle
RT function in zebrafish.";
RL Dev. Biol. 303:483-492(2007).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH HSP90A1; HSP90A2
RP AND HSP90AB.
RC TISSUE=Embryo {ECO:0000269|PubMed:17586488};
RX PubMed=17586488; DOI=10.1016/j.ydbio.2007.05.014;
RA Etard C., Behra M., Fischer N., Hutcheson D., Geisler R., Strahle U.;
RT "The UCS factor Steif/Unc-45b interacts with the heat shock protein Hsp90a
RT during myofibrillogenesis.";
RL Dev. Biol. 308:133-143(2007).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MYOSIN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18347070; DOI=10.1083/jcb.200709128;
RA Etard C., Roostalu U., Strahle U.;
RT "Shuttling of the chaperones Unc45b and Hsp90a between the A band and the Z
RT line of the myofibril.";
RL J. Cell Biol. 180:1163-1175(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [6] {ECO:0000312|EMBL:CAP19503.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH76400.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=20849610; DOI=10.1186/1471-2121-11-70;
RA Bernick E.P., Zhang P.J., Du S.;
RT "Knockdown and overexpression of Unc-45b result in defective myofibril
RT organization in skeletal muscles of zebrafish embryos.";
RL BMC Cell Biol. 11:70-70(2010).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH APOBEC2A AND APOBEC2B, AND SUBCELLULAR LOCATION.
RX PubMed=20440001; DOI=10.1083/jcb.200912125;
RA Etard C., Roostalu U., Strahle U.;
RT "Lack of Apobec2-related proteins causes a dystrophic muscle phenotype in
RT zebrafish embryos.";
RL J. Cell Biol. 189:527-539(2010).
RN [9]
RP FUNCTION.
RX PubMed=24549050; DOI=10.1038/ejhg.2014.21;
RA Hansen L., Comyn S., Mang Y., Lind-Thomsen A., Myhre L., Jean F.,
RA Eiberg H., Tommerup N., Rosenberg T., Pilgrim D.;
RT "The myosin chaperone UNC45B is involved in lens development and autosomal
RT dominant juvenile cataract.";
RL Eur. J. Hum. Genet. 22:1290-1297(2014).
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. Required for
CC myoseptal integrity, myofiber attachment, motility and craniofacial
CC development (PubMed:17189627, PubMed:17586488, PubMed:20440001,
CC PubMed:20849610). Is necessary for normal early lens development
CC (PubMed:24549050). {ECO:0000250|UniProtKB:Q8CGY6,
CC ECO:0000269|PubMed:17189627, ECO:0000269|PubMed:17586488,
CC ECO:0000269|PubMed:20440001, ECO:0000269|PubMed:20849610,
CC ECO:0000269|PubMed:24549050}.
CC -!- SUBUNIT: Interacts with apobec2a, apobec2b, hsp90a.1, hsp90a.2,
CC hsp90ab1 and myosin. {ECO:0000269|PubMed:17586488,
CC ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}. Cytoplasm,
CC myofibril, sarcomere, A band {ECO:0000269|PubMed:18347070,
CC ECO:0000269|PubMed:20440001}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}.
CC Note=Expressed at the Z line and in the perinuclear region of
CC myofibrils. Translocates to the A band in response to stress conditions
CC and fibril damage. {ECO:0000269|PubMed:18347070,
CC ECO:0000269|PubMed:20440001}.
CC -!- TISSUE SPECIFICITY: Expressed in striated muscle tissue including
CC somites, heart and craniofacial muscle. Detected in mesoderm adjacent
CC to the dorsal midline during the late gastrula stages and in somitic
CC mesoderm during development of trunk skeletal muscle. Also expressed in
CC cranial skeletal muscle and in cardiac and smooth muscle. Detected in
CC somitic muscle and heart primordium of 24 hour embryos. At later
CC stages, expressed in muscles of pectoral fins, jaw, branchial arches
CC and eye. {ECO:0000269|PubMed:12203738, ECO:0000269|PubMed:17189627}.
CC -!- DEVELOPMENTAL STAGE: First detected at the late gastrula stages around
CC 9 hours post-fertilization (hpf). Expression intensifies by the end of
CC gastrulation around 10 hpf, continues into early somitogenesis stages
CC around 12 hpf and persists in the somites until 96 hpf when the somites
CC give rise to the trunk skeletal muscle. {ECO:0000269|PubMed:12203738,
CC ECO:0000269|PubMed:17189627}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH76400.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF330001; AAL57031.1; -; mRNA.
DR EMBL; CR847826; CAP19503.1; -; Genomic_DNA.
DR EMBL; BC076400; AAH76400.1; ALT_INIT; mRNA.
DR RefSeq; NP_705959.1; NM_153673.2.
DR RefSeq; XP_017212759.1; XM_017357270.1.
DR AlphaFoldDB; Q6DGE9; -.
DR SMR; Q6DGE9; -.
DR STRING; 7955.ENSDARP00000023678; -.
DR PaxDb; Q6DGE9; -.
DR PRIDE; Q6DGE9; -.
DR Ensembl; ENSDART00000002164; ENSDARP00000023678; ENSDARG00000008433.
DR GeneID; 266640; -.
DR KEGG; dre:266640; -.
DR CTD; 146862; -.
DR ZFIN; ZDB-GENE-020919-3; unc45b.
DR eggNOG; KOG4151; Eukaryota.
DR GeneTree; ENSGT00940000157654; -.
DR HOGENOM; CLU_007331_0_0_1; -.
DR InParanoid; Q6DGE9; -.
DR OMA; CDPERAN; -.
DR OrthoDB; 1059433at2759; -.
DR PhylomeDB; Q6DGE9; -.
DR TreeFam; TF314096; -.
DR PRO; PR:Q6DGE9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000008433; Expressed in somite and 45 other tissues.
DR ExpressionAtlas; Q6DGE9; baseline.
DR GO; GO:0031672; C:A band; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IDA:ZFIN.
DR GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:ZFIN.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0002088; P:lens development in camera-type eye; IMP:UniProtKB.
DR GO; GO:0030239; P:myofibril assembly; IMP:ZFIN.
DR GO; GO:0060538; P:skeletal muscle organ development; IMP:ZFIN.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:ZFIN.
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; 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..934
FT /note="Protein unc-45 homolog B"
FT /id="PRO_0000412996"
FT REPEAT 9..42
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 48..81
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 83..115
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 174..213
FT /note="ARM 1"
FT /evidence="ECO:0000255"
FT REPEAT 216..255
FT /note="ARM 2"
FT /evidence="ECO:0000255"
FT REPEAT 753..792
FT /note="ARM 3"
FT /evidence="ECO:0000255"
SQ SEQUENCE 934 AA; 103847 MW; 8B30BCCD33EDC562 CRC64;
MTMGEIGDSV QLKEEGNKHF QAGEIDQAID CYTKAIKTCK KEDKKALAVI YRNRSACFLK
KENYSNAASD ATKAIDVDAA DIKALYRRCQ AFEKLGKLDM AFKDVQRCAT IEPKNKTFLE
TLRRLGAEIQ QKLKTTFSTD SRVQNMFDIL FSDEPDKEKR EKAANNLIVL AREDAGAERI
FQNNGVPLLM QLIDTGKPEM ILAAIRTLSG MCTGHRARAT AIIHSVGISK LCSIMAVDNE
EIALATANLF QCVNDSLSGG DKRNYGKEEA LVLDSSKDLK DILLALLEMI ASKNVSGHGR
DQALNLLTKN VPRQNKKSTD NSKCLFTIDH GLKKILKVCG QVPDLPDQLP MTENTQLIAS
VLLSKLYDDL RCDPERDQFR DICDDYIKSK FDPNDMDKNI HAINTLSGIL QGPFDLGNVL
AGRQGVMEMM VALCGSEREV DQLVAVEALI HASTKTSKAS FFISNGVSLL KEMYKKTKNE
KIKIRALVGL CKLGSAGGDD YSMRQFAEGS TEKLAKQCRK WLCNPTLDVR TRKWAIEGLA
YLTNDADVKD DFAEDEPAMR AMFELTKSND KTILYAVACT LVNCTNSYDK KEIIPEMVQL
AKFSKQHVPE QHPKDKKDFI VRRVKRLLKA GVTSALAVMV KADNSILTDQ TKEMLARVFL
ALTEDVKDRG IIVAQGGGKA LIPLALEGTD KGKIKASHAL AKIAAVSNPE IAFPGERIYE
VVRPLVSLLG TDRDGMENFE ALRGLTNLAG LNDKLRVKIL KEKALPEIEN YMFEDHEQIR
QAATECMCNL VCCKEVQDRY LEDGNDKLKL LVLLCGEDEE KLQRAAAGAL AMLTAAQKKL
AVKMTKVTEQ WLEILQRLCI HDNPEIQHRG LVTVFNMLDA DDQLAKKLVE SDMLEILTYV
AKLEDNPKKQ NAIDAARACL SKAMDNGLIK PFSN
