GenomeNet

Database: UniProt
Entry: G1MSW3_MELGA
LinkDB: G1MSW3_MELGA
Original site: G1MSW3_MELGA 
ID   G1MSW3_MELGA            Unreviewed;       646 AA.
AC   G1MSW3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Heat shock protein family A (Hsp70) member 8 {ECO:0000313|Ensembl:ENSMGAP00000001450.1};
GN   Name=HSPA8 {ECO:0000313|Ensembl:ENSMGAP00000001450.1};
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000001450.1, ECO:0000313|Proteomes:UP000001645};
RN   [1] {ECO:0000313|Ensembl:ENSMGAP00000001450.1, ECO:0000313|Proteomes:UP000001645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA   Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA   Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA   Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA   Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA   Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA   Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA   Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA   Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA   Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA   Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA   Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA   Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA   Zhang Y., Reed K.M.;
RT   "Multi-platform next-generation sequencing of the domestic turkey
RT   (Meleagris gallopavo): genome assembly and analysis.";
RL   PLoS Biol. 8:E1000475-E1000475(2010).
RN   [2] {ECO:0000313|Ensembl:ENSMGAP00000001450.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR   RefSeq; XP_003212746.1; XM_003212698.3.
DR   AlphaFoldDB; G1MSW3; -.
DR   SMR; G1MSW3; -.
DR   Ensembl; ENSMGAT00000002110.2; ENSMGAP00000001450.1; ENSMGAG00000001929.2.
DR   GeneID; 100551334; -.
DR   KEGG; mgp:100551334; -.
DR   CTD; 3312; -.
DR   GeneTree; ENSGT00950000183206; -.
DR   HOGENOM; CLU_005965_3_0_1; -.
DR   InParanoid; G1MSW3; -.
DR   OMA; KANPIMM; -.
DR   OrthoDB; 143at2759; -.
DR   TreeFam; TF105042; -.
DR   Proteomes; UP000001645; Chromosome 26.
DR   Bgee; ENSMGAG00000001929; Expressed in brain and 17 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0098690; C:glycinergic synapse; IEA:Ensembl.
DR   GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0098684; C:photoreceptor ribbon synapse; IEA:Ensembl.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; IEA:Ensembl.
DR   GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR   GO; GO:0101031; C:protein folding chaperone complex; IEA:Ensembl.
DR   GO; GO:0000974; C:Prp19 complex; IEA:Ensembl.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR   GO; GO:0140545; F:ATP-dependent protein disaggregase activity; IEA:Ensembl.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0055131; F:C3HC4-type RING finger domain binding; IEA:Ensembl.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IEA:Ensembl.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR   GO; GO:0001786; F:phosphatidylserine binding; IEA:Ensembl.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
DR   GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:Ensembl.
DR   GO; GO:0072318; P:clathrin coat disassembly; IEA:Ensembl.
DR   GO; GO:0061738; P:late endosomal microautophagy; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; IEA:Ensembl.
DR   GO; GO:1902904; P:negative regulation of supramolecular fiber organization; IEA:Ensembl.
DR   GO; GO:0044829; P:positive regulation by host of viral genome replication; IEA:Ensembl.
DR   GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR   GO; GO:0042026; P:protein refolding; IEA:Ensembl.
DR   GO; GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; IEA:Ensembl.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR   GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl.
DR   GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR   CDD; cd10233; HSPA1-2_6-8-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375:SF379; HEAT SHOCK COGNATE 71 KDA PROTEIN; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001645}.
FT   REGION          614..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  70871 MW;  EDDD8CB1E52A6EFC CRC64;
     MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
     MNPTNTVFDA KRLIGRRFDD SVVQSDMKHW PFTVVNDAGR PKVQVEYKGE TKSFYPEEIS
     SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA
     IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH
     FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
     RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN
     KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI
     PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI
     DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN
     SLESYAFNMK ATVEDEKLQG KISDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE
     KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
//
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