UN45B_MOUSE
ID UN45B_MOUSE Reviewed; 931 AA.
AC Q8CGY6; Q5XG72; Q8BHC5; Q8BWK3;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein unc-45 homolog B;
DE Short=Unc-45B;
GN Name=Unc45b; Synonyms=Cmya4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=12356907; DOI=10.1242/jcs.00108;
RA Price M.G., Landsverk M.L., Barral J.M., Epstein H.F.;
RT "Two mammalian UNC-45 isoforms are related to distinct cytoskeletal and
RT muscle-specific functions.";
RL J. Cell Sci. 115:4013-4023(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic eye, Embryonic head, and Embryonic heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 FUNCTION, AND INTERACTION WITH HSP90.
RX PubMed=18326487; DOI=10.1074/jbc.m800757200;
RA Liu L., Srikakulam R., Winkelmann D.A.;
RT "Unc45 activates Hsp90-dependent folding of the myosin motor domain.";
RL J. Biol. Chem. 283:13185-13193(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HSP90.
RX PubMed=18478096; DOI=10.1371/journal.pone.0002137;
RA Srikakulam R., Liu L., Winkelmann D.A.;
RT "Unc45b forms a cytosolic complex with Hsp90 and targets the unfolded
RT myosin motor domain.";
RL PLoS ONE 3:E2137-E2137(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as a co-chaperone for HSP90 and is required for proper
CC folding of the myosin motor domain. Plays a role in sarcomere formation
CC during muscle cell development (PubMed:12356907, PubMed:18326487,
CC PubMed:18478096). Is necessary for normal early lens development (By
CC similarity). {ECO:0000250|UniProtKB:Q6DGE9,
CC ECO:0000269|PubMed:12356907, ECO:0000269|PubMed:18326487,
CC ECO:0000269|PubMed:18478096}.
CC -!- SUBUNIT: Interacts with HSP90 in an ATP-independent manner
CC (PubMed:18326487, PubMed:18478096). Interacts with UBE4B; the
CC interaction may target UNC45B for proteasomal degradation (By
CC similarity). {ECO:0000250|UniProtKB:Q8IWX7,
CC ECO:0000269|PubMed:18326487, ECO:0000269|PubMed:18478096}.
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:0000269|PubMed:18478096}. 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CGY6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CGY6-2; Sequence=VSP_020588;
CC -!- TISSUE SPECIFICITY: Highly expressed in adult skeletal muscle and
CC heart. Detected at intermediate levels in lung. Highly expressed in
CC embryonic heart. {ECO:0000269|PubMed:12356907}.
CC -!- DEVELOPMENTAL STAGE: Detected in fusing myoblasts during muscle cell
CC differentiation. Highly expressed in young myotubes that are in the
CC process of assembling and remodeling myofibrils. Subsequently, levels
CC decrease during myotube maturation.
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DR EMBL; AF539793; AAO13383.1; -; mRNA.
DR EMBL; AK052294; BAC34921.1; -; mRNA.
DR EMBL; AK081821; BAC38342.1; -; mRNA.
DR EMBL; AK084418; BAC39178.1; -; mRNA.
DR EMBL; AL603745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC084585; AAH84585.1; -; mRNA.
DR CCDS; CCDS36251.1; -. [Q8CGY6-2]
DR RefSeq; NP_848795.3; NM_178680.4. [Q8CGY6-2]
DR AlphaFoldDB; Q8CGY6; -.
DR SMR; Q8CGY6; -.
DR BioGRID; 229832; 2.
DR IntAct; Q8CGY6; 2.
DR STRING; 10090.ENSMUSP00000103795; -.
DR iPTMnet; Q8CGY6; -.
DR PhosphoSitePlus; Q8CGY6; -.
DR CPTAC; non-CPTAC-4069; -.
DR MaxQB; Q8CGY6; -.
DR PaxDb; Q8CGY6; -.
DR PeptideAtlas; Q8CGY6; -.
DR PRIDE; Q8CGY6; -.
DR ProteomicsDB; 300085; -. [Q8CGY6-1]
DR ProteomicsDB; 300086; -. [Q8CGY6-2]
DR Antibodypedia; 2894; 164 antibodies from 28 providers.
DR DNASU; 217012; -.
DR Ensembl; ENSMUST00000018989; ENSMUSP00000018989; ENSMUSG00000018845. [Q8CGY6-2]
DR Ensembl; ENSMUST00000108160; ENSMUSP00000103795; ENSMUSG00000018845. [Q8CGY6-1]
DR Ensembl; ENSMUST00000164945; ENSMUSP00000129405; ENSMUSG00000018845. [Q8CGY6-1]
DR GeneID; 217012; -.
DR KEGG; mmu:217012; -.
DR UCSC; uc007knu.2; mouse. [Q8CGY6-2]
DR UCSC; uc007knw.1; mouse. [Q8CGY6-1]
DR CTD; 146862; -.
DR MGI; MGI:2443377; Unc45b.
DR VEuPathDB; HostDB:ENSMUSG00000018845; -.
DR eggNOG; KOG4151; Eukaryota.
DR GeneTree; ENSGT00940000157654; -.
DR HOGENOM; CLU_007331_0_0_1; -.
DR InParanoid; Q8CGY6; -.
DR OMA; CDPERAN; -.
DR OrthoDB; 1059433at2759; -.
DR PhylomeDB; Q8CGY6; -.
DR TreeFam; TF314096; -.
DR BioGRID-ORCS; 217012; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q8CGY6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8CGY6; protein.
DR Bgee; ENSMUSG00000018845; Expressed in interventricular septum and 129 other tissues.
DR Genevisible; Q8CGY6; MM.
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; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:MGI.
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; 3.
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 Alternative splicing; Chaperone; Cytoplasm; Developmental protein;
KW Differentiation; Myogenesis; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..931
FT /note="Protein unc-45 homolog B"
FT /id="PRO_0000249893"
FT REPEAT 6..39
FT /note="TPR 1"
FT REPEAT 43..76
FT /note="TPR 2"
FT REPEAT 77..110
FT /note="TPR 3"
FT REPEAT 169..208
FT /note="ARM 1"
FT REPEAT 211..250
FT /note="ARM 2"
FT REPEAT 751..790
FT /note="ARM 3"
FT VAR_SEQ 564..565
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12356907,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_020588"
FT CONFLICT 176
FT /note="F -> L (in Ref. 4; AAH84585)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="S -> I (in Ref. 2; BAC34921)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 931 AA; 103638 MW; 664CE68C55031578 CRC64;
MAEAEAAQLK EEGNRHFQLQ DYKAATKSYS QALKLTKDKA LLATLYRNRA ACGLKMESYA
QAASDASRAI DINSADIKAL YRRCQALEHL GKLDQAFKDV QRCATLEPRN QNFQETLRRL
NTSIQEQLRV QFSTDSRVQT MFEILLNENS EADKREKAAN NLIVLGREEA GAERIFQSNG
VALLLQLMNT QRPELLLAAV RTLSGMCSGH RARATAILHA VRIDRICSLM ALENEEMSLA
VCNLLQAIID SLSGEDKREH RGKEEALVLD TKKDLKQITS HLLDMLVSKK VSGQGRDQAL
NLLNKNVPRK DLSIHDNSRT IYVVDNGLRK ILKVVGQVPD LPSCLPLTDN TRMLASILIN
KLYDDLRCDP ERDHFRKICE EYITSKFDPQ DMDKNVNAIQ TVSGILQGPF DLGNQLLGMK
GVMEMMVALC GSEREADQLV AVEALIHAST KLSRATFIIT NGVTLLKQIY KTTKNEKIKI
RTLVGLCKLG SAGGSDYGLR QFAEGSTEKL AKQCRKWLCN TAIDTRTRRW AVEGLAYLTL
DADVKDDFVQ DIPALQAMFE LAKARTSDKT ILYSVANTLV NCTNSYDVKE VVPELVQLAK
FSKQHVPEEH PKDKKDFVDL RVKRLLKAGV ISALACMVKA DSAILTDQTK ELLARVFLAL
CDNPKDRGTI VAQGGGKALI PLALEGTDVG KVKAAHGLAK IAAVSNPDIA FPGERVYEVV
RPLVSLLDTQ RDGLQNYEAL LGLTNLSGRS DKLRQKIFKE KALPDIENYM FENHDQLRQA
ATECMCNMVL NKEVQERFLA DGNDRLKLVV LLCGEDDHKL QNAAAGALAM LTAAHKKLCL
KMTEVTTQWL EILQRLCLHD QLSVQHRGLV IAHNLLSADA ELARKLVESE LLEILTVVGK
QEPDEKRAAV VQTARECLIK CMDYGFIKPV S
