ID UN45A_MOUSE Reviewed; 944 AA.
AC Q99KD5; Q3TKV6; Q8BFT3; Q8C157;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 24-JAN-2024, entry version 157.
DE RecName: Full=Protein unc-45 homolog A;
DE Short=Unc-45A;
DE AltName: Full=Stromal membrane-associated protein 1;
DE Short=SMAP-1;
GN Name=Unc45a; Synonyms=Smap1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Blastocyst, Cerebellum, and Skin;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9209433;
RA Yanai N., Sato Y., Obinata M.;
RT "A new type-II membrane protein in erythropoietic organs enhances
RT erythropoiesis.";
RL Leukemia 11:484-485(1997).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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: May act as co-chaperone for HSP90 (Potential). Prevents the
CC stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in
CC promoting PGR function in the cell (By similarity). May be necessary
CC for proper folding of myosin (Potential). Necessary for normal cell
CC proliferation. Necessary for normal myotube formation and myosin
CC accumulation during muscle cell development. May play a role in
CC erythropoiesis in stroma cells in the spleen. {ECO:0000250,
CC ECO:0000269|PubMed:12356907, ECO:0000269|PubMed:9209433, ECO:0000305}.
CC -!- SUBUNIT: Interacts with PGR isoforms A and B as well as with NR3C1 in
CC the absence of ligand, and with HSP90AB1. Binding to HSP90AB1 involves
CC 2 UNC45A monomers per HSP90AB1 dimer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominant in the
CC perinuclear region. Little protein in the nucleus (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in spleen, bone marrow, lung and ovary,
CC and at lower levels in testis, kidney, heart and brain (at protein
CC level). Ubiquitous. Detected in uterus, large intestine, kidney,
CC spleen, lung, brain, liver and ovary. {ECO:0000269|PubMed:12356907,
CC ECO:0000269|PubMed:9209433}.
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DR EMBL; AK028912; BAC26192.1; -; mRNA.
DR EMBL; AK047292; BAC33017.1; -; mRNA.
DR EMBL; AK047476; BAC33070.1; -; mRNA.
DR EMBL; AK166809; BAE39037.1; -; mRNA.
DR EMBL; BC004717; AAH04717.1; -; mRNA.
DR CCDS; CCDS21395.1; -.
DR RefSeq; NP_598713.2; NM_133952.2.
DR RefSeq; XP_011249076.1; XM_011250774.1.
DR AlphaFoldDB; Q99KD5; -.
DR SMR; Q99KD5; -.
DR BioGRID; 221742; 5.
DR STRING; 10090.ENSMUSP00000032748; -.
DR iPTMnet; Q99KD5; -.
DR PhosphoSitePlus; Q99KD5; -.
DR EPD; Q99KD5; -.
DR MaxQB; Q99KD5; -.
DR PaxDb; 10090-ENSMUSP00000102991; -.
DR PeptideAtlas; Q99KD5; -.
DR ProteomicsDB; 300084; -.
DR Pumba; Q99KD5; -.
DR Antibodypedia; 28924; 128 antibodies from 25 providers.
DR DNASU; 101869; -.
DR Ensembl; ENSMUST00000032748.15; ENSMUSP00000032748.9; ENSMUSG00000030533.17.
DR GeneID; 101869; -.
DR KEGG; mmu:101869; -.
DR UCSC; uc009iam.3; mouse.
DR AGR; MGI:2142246; -.
DR CTD; 55898; -.
DR MGI; MGI:2142246; Unc45a.
DR VEuPathDB; HostDB:ENSMUSG00000030533; -.
DR eggNOG; KOG4151; Eukaryota.
DR GeneTree; ENSGT00940000159320; -.
DR HOGENOM; CLU_007331_0_0_1; -.
DR InParanoid; Q99KD5; -.
DR OMA; LDQKHED; -.
DR OrthoDB; 1094381at2759; -.
DR PhylomeDB; Q99KD5; -.
DR TreeFam; TF314096; -.
DR BioGRID-ORCS; 101869; 18 hits in 79 CRISPR screens.
DR ChiTaRS; Unc45a; mouse.
DR PRO; PR:Q99KD5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q99KD5; Protein.
DR Bgee; ENSMUSG00000030533; Expressed in external carotid artery and 263 other cell types or tissues.
DR ExpressionAtlas; Q99KD5; baseline and differential.
DR Genevisible; Q99KD5; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; 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:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR024660; UCS_central_dom.
DR PANTHER; PTHR45994; FI21225P1; 1.
DR PANTHER; PTHR45994:SF3; PROTEIN UNC-45 HOMOLOG A; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13181; TPR_8; 1.
DR Pfam; PF11701; UNC45-central; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Developmental protein; Differentiation;
KW Myogenesis; Nucleus; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..944
FT /note="Protein unc-45 homolog A"
FT /id="PRO_0000249889"
FT REPEAT 21..54
FT /note="TPR 1"
FT REPEAT 58..91
FT /note="TPR 2"
FT REPEAT 92..125
FT /note="TPR 3"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3U1"
FT MOD_RES 483
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3U1"
FT CONFLICT 86
FT /note="E -> G (in Ref. 1; BAC26192)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="N -> S (in Ref. 2; AAH04717)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="D -> G (in Ref. 1; BAC33017/BAC33070)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="A -> T (in Ref. 2; AAH04717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 944 AA; 103447 MW; 61E15C6DE421242D CRC64;
MTVSGPETPE PRPSDPGASS AEQLRKEGNE LFKCGDYEGA LTAYTQALSL GATPQDQAIL
HRNRAACHLK LEDYSKAESE ASKAIEKDGG DVKALYRRSQ ALEKLGRLDQ AVLDLKRCVS
LEPKNKVFQE SLRNIGGQIQ EKVRYMSSTD AKVEQMFQIL LDPKEKGTEK KQKASQNLVV
LAREDAGAEK IFRSNGVQLL QRLLDTEETD LMLAALRTLV GICSEHQSRT VATLSVLGTR
RVVSILGVEN QAVSLAACHL LQVIFDALKE GVKKGFRGKE GAIIVDPARE LKVLINSLLE
LLTEVGVSGQ GRDNALTLLI KMVPRKSPKD PNNSLTLWVI DQGLKKILEV GGSLQDAAGE
LTVTANSRMS ASILLSKLFD DLKCDAEREN FHRLCENYIR NWFEGHGLAG KLRAIQTVSC
LLQGPCDAGN RALELSGVME SVIALCASER EEEQLVAVEA LIHAAGKAKR ASFITANGVS
LLKDLYKGSE RDSIRIRALV GLCKLGSAGG TDFSMKQFAE GSTLKLAKQC RKWLCNDQID
AGTRRWAVEG LAYLTFDADV KEEFVEDEAA LKALFQLSRS EERSVLFAVG SALVNCTNSY
DYEEPDPKMV ELAKYAKQHV PEQHPKDKPS FVRARVKKLL AAGVVSAMTC MVKTESPVLT
NSCRELLSRV FLALVEEVED RGTVVAQGGG KALLPLALEG TDVGQTKAAQ ALAKLTITSN
PEMTFPGERI YEVVRPLVSL LHLSCSGLQN FEALMALTNL AGISERLRQK ILKEKAVPMI
EGYMFEEHEM IRRAATECMC NLAMSKEVQD LFEAQGNDRL KLLVLYSGED DELLRRAAAG
GLAMLTSMRP ALCSRIPQVT THWLEILQAL LLSPNQELQH RGTVVVLNMM QSSKEIAGTL
MESEVLEILS VLAKGEESPV TRAAAACLEK AVEYRLIQPN QDGE
//
