ID A0A2K6STJ6_SAIBB Unreviewed; 601 AA.
AC A0A2K6STJ6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Heat shock-related 70 kDa protein 2 {ECO:0000256|ARBA:ARBA00039557};
GN Name=HSPA2 {ECO:0000313|Ensembl:ENSSBOP00000010708.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000010708.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000010708.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6STJ6; -.
DR STRING; 39432.ENSSBOP00000010708; -.
DR Ensembl; ENSSBOT00000027486.1; ENSSBOP00000010708.1; ENSSBOG00000022183.1.
DR GeneTree; ENSGT00940000154813; -.
DR OMA; SYAYNIK; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0036128; C:CatSper complex; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0072687; C:meiotic spindle; IEA:Ensembl.
DR GO; GO:0000795; C:synaptonemal complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0051861; F:glycolipid binding; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; IEA:Ensembl.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0042026; P:protein refolding; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR GO; GO:0070194; P:synaptonemal complex disassembly; IEA:Ensembl.
DR CDD; cd10233; HSPA1-2_6-8-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 3.
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; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF382; HEAT SHOCK-RELATED 70 KDA PROTEIN 2; 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:UP000233220}.
FT REGION 581..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 601 AA; 66077 MW; A0C02908CEF8203D CRC64;
MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV
AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVMKEIA EAYLGGKVHS AVITVPAYFN
DSQRQATKDA GTITGLNVLR IINEPTAAAI AYGLDKKGCA GGEKNVLIFD LGGGTFDVSI
LTIEDGIFEV KSTAGDTHLG GEDFDNRMVS HLAEEFKRKH KKDIGPNKRA VRRLRTACER
AKRTLSSSTQ ASIEIDSLYE GVDFYTSITR ARFEELNADL FRGTLEPVEK ALRDAKLDKG
QIQEIVLVGG STRIPKIQKL LQDFFNGKEL NKSINPDEAV AYGAAVQAAI LIGDKSENVQ
DLLLLDVTPL SLGIETAGGV MTPLIKRNTT IPTKQTQTFT TYSDNQSSVL VQVYEGERAM
TKDNNLLGKF DLTGIPPAPR GVPQIEVTFD IDANGILNVT AADKSTGKEN KITITNDKGR
LSKDDIDRMV QEAERYKSED EANRDRVAAK NAVESYTYNI KQTVEDEKLR GKISEQDKNK
ILDKCQEVIN WLDRNQMAEK DEFEHKQKEL ERICNPIISK LYQGGPGGSG ASGGPTIEEV
D
//