HSPB7_MOUSE
ID HSPB7_MOUSE Reviewed; 169 AA.
AC P35385; Q5FW72; Q8CDI0; Q9QUS2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Heat shock protein beta-7;
DE Short=HspB7;
DE AltName: Full=Cardiovascular heat shock protein;
DE Short=cvHsp;
DE AltName: Full=Heat shock protein 25 kDa 2;
DE AltName: Full=Protein p19/6.8;
GN Name=Hspb7; Synonyms=Cvhsp, Hsp25-2;
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].
RC TISSUE=Heart;
RX PubMed=10593960; DOI=10.1074/jbc.274.51.36592;
RA Krief S., Faivre J.-F., Robert P., Le Douarin B., Brument-Larignon N.,
RA Lefrere I., Bouzyk M.M., Anderson K.M., Greller L.D., Tobin F.L.,
RA Souchet M., Bril A.;
RT "Identification and characterization of cvHsp. A novel human small stress
RT protein selectively expressed in cardiovascular and insulin-sensitive
RT tissues.";
RL J. Biol. Chem. 274:36592-36600(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [6]
RP PROTEIN SEQUENCE OF 43-61 AND 76-87.
RC TISSUE=Muscle;
RA Kluxen F.-W., Vandekerckhove J., Schoeffl F., Jockusch H.;
RL Mouse News Lett. 84:76-77(1989).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 -!- SUBUNIT: Interacts with C-terminal domain of actin-binding protein 280.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Nucleus, Cajal body {ECO:0000250}. Note=Resides in sub-nuclear
CC structures known as SC35 speckles or nuclear splicing speckles.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Found in both cardiac and slow skeletal (soleus)
CC muscle.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; AJ243192; CAB63266.1; -; mRNA.
DR EMBL; AF155909; AAF20023.1; -; mRNA.
DR EMBL; AK030025; BAC26743.1; -; mRNA.
DR EMBL; AL670285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466615; EDL13373.1; -; Genomic_DNA.
DR EMBL; BC089584; AAH89584.1; -; mRNA.
DR CCDS; CCDS18873.1; -.
DR RefSeq; NP_038896.2; NM_013868.4.
DR AlphaFoldDB; P35385; -.
DR SMR; P35385; -.
DR STRING; 10090.ENSMUSP00000099544; -.
DR iPTMnet; P35385; -.
DR PhosphoSitePlus; P35385; -.
DR PaxDb; P35385; -.
DR PeptideAtlas; P35385; -.
DR PRIDE; P35385; -.
DR ProteomicsDB; 273391; -.
DR Antibodypedia; 29049; 271 antibodies from 30 providers.
DR DNASU; 29818; -.
DR Ensembl; ENSMUST00000102486; ENSMUSP00000099544; ENSMUSG00000006221.
DR GeneID; 29818; -.
DR KEGG; mmu:29818; -.
DR UCSC; uc008voj.1; mouse.
DR CTD; 27129; -.
DR MGI; MGI:1352494; Hspb7.
DR VEuPathDB; HostDB:ENSMUSG00000006221; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00390000010674; -.
DR HOGENOM; CLU_124226_0_0_1; -.
DR InParanoid; P35385; -.
DR OMA; DPPMDKA; -.
DR OrthoDB; 1362331at2759; -.
DR PhylomeDB; P35385; -.
DR TreeFam; TF350564; -.
DR BioGRID-ORCS; 29818; 5 hits in 73 CRISPR screens.
DR PRO; PR:P35385; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P35385; protein.
DR Bgee; ENSMUSG00000006221; Expressed in interventricular septum and 118 other tissues.
DR Genevisible; P35385; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IPI:MGI.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031005; F:filamin binding; IDA:MGI.
DR GO; GO:0007507; P:heart development; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; ISO:MGI.
DR CDD; cd06479; ACD_HspB7_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR037885; ACD_HspB7.
DR InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR Pfam; PF00011; HSP20; 1.
DR PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Direct protein sequencing; Nucleus;
KW Reference proteome; Stress response.
FT CHAIN 1..169
FT /note="Heat shock protein beta-7"
FT /id="PRO_0000125942"
FT DOMAIN 61..169
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 1..70
FT /note="Required for localization to SC35 splicing speckles"
FT /evidence="ECO:0000250"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 23
FT /note="S -> P (in Ref. 1; CAB63266/AAF20023)"
FT /evidence="ECO:0000305"
FT CONFLICT 60..61
FT /note="EP -> GD (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="H -> N (in Ref. 1; CAB63266/AAF20023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 169 AA; 18635 MW; 15E45C854BF09E7C CRC64;
MSHRTSSAFR AERSFRSSSS SSSSSSSSAS RALPAQDPPM EKALSMFSDD FGSFMLPHSE
PLAFPARPGG QGNIKTLGDA YEFTVDMRDF SPEDIIVTTF NNHIEVRAEK LAADGTVMNT
FAHKCQLPED VDPTSVTSAL REDGSLTIRA RRHPHTEHVQ QTFRTEIKI
