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Database: UniProt
Entry: F6PQ65_MACMU
LinkDB: F6PQ65_MACMU
Original site: F6PQ65_MACMU 
ID   F6PQ65_MACMU            Unreviewed;       160 AA.
AC   F6PQ65; F6PQ95; G7NM68;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Heat shock protein beta-6 {ECO:0000313|EMBL:AFE76660.1};
DE   SubName: Full=Heat shock protein family B (small) member 6 {ECO:0000313|Ensembl:ENSMMUP00000003208.1};
GN   Name=HSPB6 {ECO:0000313|EMBL:AFE76660.1,
GN   ECO:0000313|Ensembl:ENSMMUP00000003208.1,
GN   ECO:0000313|VGNC:VGNC:110635};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000003208.1, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|EMBL:AFE76660.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Caudate {ECO:0000313|EMBL:AFE76660.1}, and Testis
RC   {ECO:0000313|EMBL:AFI36250.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA   Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA   Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA   Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
RN   [3] {ECO:0000313|Ensembl:ENSMMUP00000003208.1}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000003208.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000256|PROSITE-ProRule:PRU00285, ECO:0000256|RuleBase:RU003616}.
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DR   EMBL; JU332905; AFE76660.1; -; mRNA.
DR   EMBL; JV046179; AFI36250.1; -; mRNA.
DR   RefSeq; NP_001181037.1; NM_001194108.1.
DR   RefSeq; XP_014979054.1; XM_015123568.1.
DR   RefSeq; XP_014979055.1; XM_015123569.1.
DR   STRING; 9544.ENSMMUP00000003204; -.
DR   PaxDb; 9544-ENSMMUP00000003208; -.
DR   Ensembl; ENSMMUT00000003392.3; ENSMMUP00000003204.3; ENSMMUG00000002389.3.
DR   Ensembl; ENSMMUT00000003396.3; ENSMMUP00000003208.1; ENSMMUG00000002389.3.
DR   GeneID; 710760; -.
DR   KEGG; mcc:710760; -.
DR   CTD; 126393; -.
DR   VEuPathDB; HostDB:ENSMMUG00000002389; -.
DR   VGNC; VGNC:110635; HSPB6.
DR   eggNOG; ENOG502QV4J; Eukaryota.
DR   eggNOG; KOG3591; Eukaryota.
DR   GeneTree; ENSGT00940000161100; -.
DR   HOGENOM; CLU_090128_0_0_1; -.
DR   HOGENOM; CLU_095001_2_0_1; -.
DR   OMA; PVQPTWL; -.
DR   OrthoDB; 3014506at2759; -.
DR   TreeFam; TF105049; -.
DR   Proteomes; UP000006718; Chromosome 19.
DR   Bgee; ENSMMUG00000002389; Expressed in hindlimb stylopod muscle and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IEA:Ensembl.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR   GO; GO:0005212; F:structural constituent of eye lens; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR   CDD; cd06478; ACD_HspB4-5-6; 1.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR   InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR   InterPro; IPR003090; Alpha-crystallin_N.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   PANTHER; PTHR45640:SF2; HEAT SHOCK PROTEIN BETA-6; 1.
DR   PANTHER; PTHR45640; HEAT SHOCK PROTEIN HSP-12.2-RELATED; 1.
DR   Pfam; PF00525; Crystallin; 1.
DR   Pfam; PF00011; HSP20; 1.
DR   PRINTS; PR00299; ACRYSTALLIN.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   PROSITE; PS01031; SHSP; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Stress response {ECO:0000313|EMBL:AFE76660.1}.
FT   DOMAIN          55..160
FT                   /note="SHSP"
FT                   /evidence="ECO:0000259|PROSITE:PS01031"
SQ   SEQUENCE   160 AA;  17166 MW;  3BEB1EFB5877F2E7 CRC64;
     MEIPVPVQPS WLRRASAPLP GLSAPGRLFD QRFGEGLLEA ELAALCPTTL APYYLRAPSV
     ALPVAQVPTD PGHFSVLLDV KHFSPEEIAV KVVGEHVEVH ARHEERPDEH GFVAREFHRR
     YRLPPGVDPA AVTSALSPEG VLSIQAAPAS TQAPPPAAAK
//
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