UN45A_RAT
ID UN45A_RAT Reviewed; 944 AA.
AC Q32PZ3;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein unc-45 homolog A;
DE Short=Unc-45A;
DE AltName: Full=Smooth muscle cell-associated protein 1;
DE Short=SMAP-1;
GN Name=Unc45a; Synonyms=Smap1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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 (By similarity).
CC {ECO:0000250, 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}.
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DR EMBL; BC107919; AAI07920.1; -; mRNA.
DR RefSeq; NP_001032736.1; NM_001037647.1.
DR RefSeq; XP_017444655.1; XM_017589166.1.
DR AlphaFoldDB; Q32PZ3; -.
DR SMR; Q32PZ3; -.
DR BioGRID; 259130; 1.
DR IntAct; Q32PZ3; 1.
DR STRING; 10116.ENSRNOP00000017407; -.
DR PhosphoSitePlus; Q32PZ3; -.
DR jPOST; Q32PZ3; -.
DR PaxDb; Q32PZ3; -.
DR PRIDE; Q32PZ3; -.
DR Ensembl; ENSRNOT00000017407; ENSRNOP00000017407; ENSRNOG00000012357.
DR GeneID; 308759; -.
DR KEGG; rno:308759; -.
DR UCSC; RGD:1305357; rat.
DR CTD; 55898; -.
DR RGD; 1305357; Unc45a.
DR eggNOG; KOG4151; Eukaryota.
DR GeneTree; ENSGT00940000159320; -.
DR HOGENOM; CLU_007331_0_0_1; -.
DR InParanoid; Q32PZ3; -.
DR OMA; DHLYLTR; -.
DR OrthoDB; 1059433at2759; -.
DR PhylomeDB; Q32PZ3; -.
DR TreeFam; TF314096; -.
DR PRO; PR:Q32PZ3; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000012357; Expressed in thymus and 19 other tissues.
DR Genevisible; Q32PZ3; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:RGD.
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; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR024660; UCS_central_dom.
DR Pfam; PF13181; TPR_8; 1.
DR Pfam; PF11701; UNC45-central; 1.
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 2: Evidence at transcript 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_0000249891"
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"
SQ SEQUENCE 944 AA; 103241 MW; D6F6CFB451E76952 CRC64;
MTVSGPGTPE PRPSDPGASS AEELRKEGNE LFKCGDYEGA LTAYTQALSL GATPQDQAIL
HRNRAACHLK LEDYSKAESE ASKAIEKDGG DVKALYRRSQ ALEKLGRLDQ AVLDLKRCVS
LEPKNKVFQE SLRNIGGQIQ EKVRYMSSTD AKVEQMFQIL LDPKEKGTEK KQKASQNLVV
LAREDAGAEK IFRSNGVQLL QRLLDTGETD LMLAALRTLV GICSEHQSRT VATLSVLGTR
RVVSILGVEN QAVSLAACHL LQVMFDALKE GVKKGFRGKE GAIIVDPARE LKVLISNLLE
LLTEIGVSGQ GRDNALTLLI KMVPRKSPKD PNNSLTLWVI DQGLKKILEV GGSVPEAAGE
LTVTANSRMS ASILLSKLFD DLKCDAEREN FHRLCENYIR SWFEGQGLAG KLRAIQTVSC
LLQGPCDAGN RALELSGVME SVIALCASEQ EEEQLVAVEA LIHAAGKAKR ASFITANGVA
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 SLCSRIPQVT THWLEILQAL LLSPNPELQH RGTVVVLNMM ESSKEIASTL
MESEVLEILS VLAKGEESPV TRAAAACLEK AVEYRLIQPN QDGE
