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Heat shock-related 70 kDa protein 2 (Heat shock protein 70.2)

 HSP72_MOUSE             Reviewed;         633 AA.
P17156; Q99KD7;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
23-MAY-2018, entry version 158.
RecName: Full=Heat shock-related 70 kDa protein 2;
Short=Heat shock protein 70.2;
Name=Hspa2; Synonyms=Hcp70.2, Hsp70-2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=3405224; DOI=10.1128/MCB.8.7.2925;
Zakeri Z.F., Wolgemuth D.J., Hunt C.R.;
"Identification and sequence analysis of a new member of the mouse
HSP70 gene family and characterization of its unique cellular and
developmental pattern of expression in the male germ line.";
Mol. Cell. Biol. 8:2925-2932(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH ZNF541.
PubMed=18849567; DOI=10.1074/jbc.M805590200;
Choi E., Han C., Park I., Lee B., Jin S., Choi H., Kim do H.,
Park Z.Y., Eddy E.M., Cho C.;
"A novel germ cell-specific protein, SHIP1, forms a complex with
chromatin remodeling activity during spermatogenesis.";
J. Biol. Chem. 283:35283-35294(2008).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
INTERACTION WITH MOV10L1.
PubMed=20547853; DOI=10.1073/pnas.1007158107;
Frost R.J., Hamra F.K., Richardson J.A., Qi X., Bassel-Duby R.,
Olson E.N.;
"MOV10L1 is necessary for protection of spermatocytes against
retrotransposons by Piwi-interacting RNAs.";
Proc. Natl. Acad. Sci. U.S.A. 107:11847-11852(2010).
[7]
IDENTIFICATION IN THE CATSPER COMPLEX.
STRAIN=C57BL/6J;
PubMed=21224844; DOI=10.1038/ncomms1153;
Chung J.J., Navarro B., Krapivinsky G., Krapivinsky L., Clapham D.E.;
"A novel gene required for male fertility and functional CATSPER
channel formation in spermatozoa.";
Nat. Commun. 2:153-153(2011).
[8]
INTERACTION WITH RABL2, AND TISSUE SPECIFICITY.
PubMed=23055941; DOI=10.1371/journal.pgen.1002969;
Lo J.C., Jamsai D., O'Connor A.E., Borg C., Clark B.J.,
Whisstock J.C., Field M.C., Adams V., Ishikawa T., Aitken R.J.,
Whittle B., Goodnow C.C., Ormandy C.J., O'Bryan M.K.;
"RAB-like 2 has an essential role in male fertility, sperm intra-
flagellar transport, and tail assembly.";
PLoS Genet. 8:E1002969-E1002969(2012).
[9]
FUNCTION, INTERACTION WITH SHCBP1L, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=24557841; DOI=10.1093/molehr/gau014;
Liu M., Shi X., Bi Y., Qi L., Guo X., Wang L., Zhou Z., Sha J.;
"SHCBP1L, a conserved protein in mammals, is predominantly expressed
in male germ cells and maintains spindle stability during meiosis in
testis.";
Mol. Hum. Reprod. 20:463-475(2014).
-!- FUNCTION: Molecular chaperone implicated in a wide variety of
cellular processes, including protection of the proteome from
stress, folding and transport of newly synthesized polypeptides,
activation of proteolysis of misfolded proteins and the formation
and dissociation of protein complexes. Plays a pivotal role in the
protein quality control system, ensuring the correct folding of
proteins, the re-folding of misfolded proteins and controlling the
targeting of proteins for subsequent degradation. This is achieved
through cycles of ATP binding, ATP hydrolysis and ADP release,
mediated by co-chaperones. The affinity for polypeptides is
regulated by its nucleotide bound state. In the ATP-bound form, it
has a low affinity for substrate proteins. However, upon
hydrolysis of the ATP to ADP, it undergoes a conformational change
that increases its affinity for substrate proteins. It goes
through repeated cycles of ATP hydrolysis and nucleotide exchange,
which permits cycles of substrate binding and release (By
similarity). Plays a role in spermatogenesis (PubMed:24557841). In
association with SHCBP1L may participate in the maintenance of
spindle integrity during meiosis in male germ cells
(PubMed:24557841). {ECO:0000250|UniProtKB:P54652,
ECO:0000269|PubMed:24557841}.
-!- SUBUNIT: Interacts with FKBP6 (By similarity). Interacts with
ZNF541 (PubMed:18849567). Component of the CatSper complex
(PubMed:21224844). Interacts with RABL2/RABL2A; binds
preferentially to GTP-bound RABL2 (PubMed:23055941). Interacts
with SHCBP1L; this interaction may promote the recruitment of
HSPA2 to the spindle (PubMed:24557841). Interacts with MOV10L1
(PubMed:20547853). {ECO:0000250|UniProtKB:P54652,
ECO:0000269|PubMed:18849567, ECO:0000269|PubMed:20547853,
ECO:0000269|PubMed:21224844, ECO:0000269|PubMed:23055941,
ECO:0000269|PubMed:24557841}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:24557841}. Note=Colocalizes with SHCBP1L at
spindle during the meiosis process (PubMed:24557841).
{ECO:0000269|PubMed:24557841}.
-!- TISSUE SPECIFICITY: Expressed in male germ cells (at protein
level) (PubMed:24557841, PubMed:23055941, PubMed:3405224).
{ECO:0000269|PubMed:23055941, ECO:0000269|PubMed:24557841,
ECO:0000269|PubMed:3405224}.
-!- DEVELOPMENTAL STAGE: Specifically expressed in prophage stage of
meiosis (PubMed:3405224). {ECO:0000269|PubMed:3405224}.
-!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known
as the ATPase domain) is responsible for binding and hydrolyzing
ATP. The C-terminal substrate-binding domain (SBD) (also known as
peptide-binding domain) binds to the client/substrate proteins.
The two domains are allosterically coupled so that, when ATP is
bound to the NBD, the SBD binds relatively weakly to clients. When
ADP is bound in the NBD, a conformational change enhances the
affinity of the SBD for client proteins.
{ECO:0000250|UniProtKB:P54652}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M20567; AAA37859.1; -; Genomic_DNA.
EMBL; CH466526; EDL36460.1; -; Genomic_DNA.
EMBL; BC004714; AAH04714.1; -; mRNA.
EMBL; BC052350; AAH52350.1; -; mRNA.
CCDS; CCDS25993.1; -.
PIR; S10859; S10859.
RefSeq; NP_001002012.1; NM_001002012.1.
RefSeq; NP_032327.2; NM_008301.4.
RefSeq; XP_006515547.1; XM_006515484.3.
UniGene; Mm.296181; -.
ProteinModelPortal; P17156; -.
SMR; P17156; -.
BioGrid; 200453; 11.
CORUM; P17156; -.
DIP; DIP-42071N; -.
ELM; P17156; -.
IntAct; P17156; 7.
MINT; P17156; -.
STRING; 10090.ENSMUSP00000079306; -.
iPTMnet; P17156; -.
PhosphoSitePlus; P17156; -.
SwissPalm; P17156; -.
REPRODUCTION-2DPAGE; IPI00331546; -.
REPRODUCTION-2DPAGE; P17156; -.
UCD-2DPAGE; P17156; -.
EPD; P17156; -.
MaxQB; P17156; -.
PaxDb; P17156; -.
PeptideAtlas; P17156; -.
PRIDE; P17156; -.
Ensembl; ENSMUST00000080449; ENSMUSP00000079306; ENSMUSG00000059970.
Ensembl; ENSMUST00000219555; ENSMUSP00000151408; ENSMUSG00000059970.
GeneID; 15512; -.
KEGG; mmu:15512; -.
UCSC; uc007nyf.1; mouse.
CTD; 3306; -.
MGI; MGI:96243; Hspa2.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00910000144045; -.
HOGENOM; HOG000228135; -.
HOVERGEN; HBG051845; -.
InParanoid; P17156; -.
KO; K03283; -.
OMA; EAYLGCK; -.
OrthoDB; EOG091G03SF; -.
TreeFam; TF105042; -.
Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-MMU-3371568; Attenuation phase.
PRO; PR:P17156; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000059970; -.
CleanEx; MM_HSPA2; -.
Genevisible; P17156; MM.
GO; GO:0036128; C:CatSper complex; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
GO; GO:0072687; C:meiotic spindle; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0051861; F:glycolipid binding; IDA:MGI.
GO; GO:0048156; F:tau protein binding; IEA:Ensembl.
GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
GO; GO:0007141; P:male meiosis I; IMP:MGI.
GO; GO:0007140; P:male meiotic nuclear division; IMP:MGI.
GO; GO:0090084; P:negative regulation of inclusion body assembly; ISO:MGI.
GO; GO:0032781; P:positive regulation of ATPase activity; IMP:CACAO.
GO; GO:1901896; P:positive regulation of calcium-transporting ATPase activity; IMP:CACAO.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
GO; GO:0042026; P:protein refolding; ISO:MGI.
GO; GO:0009409; P:response to cold; ISS:AgBase.
GO; GO:0009408; P:response to heat; ISS:AgBase.
GO; GO:0007286; P:spermatid development; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
GO; GO:0070194; P:synaptonemal complex disassembly; IMP:MGI.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
PANTHER; PTHR19375; PTHR19375; 1.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
ATP-binding; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton;
Differentiation; Methylation; Nucleotide-binding; Phosphoprotein;
Reference proteome; Spermatogenesis; Stress response.
CHAIN 1 633 Heat shock-related 70 kDa protein 2.
/FTId=PRO_0000078259.
NP_BIND 13 16 ATP. {ECO:0000250}.
NP_BIND 205 207 ATP. {ECO:0000250}.
NP_BIND 271 278 ATP. {ECO:0000250}.
NP_BIND 342 345 ATP. {ECO:0000250}.
REGION 2 389 Nucleotide-binding domain (NBD).
{ECO:0000250|UniProtKB:P11142}.
REGION 397 512 Substrate-binding domain (SBD).
{ECO:0000250|UniProtKB:P11142}.
BINDING 72 72 ATP. {ECO:0000250}.
MOD_RES 403 403 Phosphoserine.
{ECO:0000250|UniProtKB:P14659}.
MOD_RES 408 408 Phosphothreonine.
{ECO:0000250|UniProtKB:P14659}.
MOD_RES 414 414 Phosphothreonine.
{ECO:0000250|UniProtKB:P14659}.
MOD_RES 564 564 N6,N6,N6-trimethyllysine; by METTL21A; in
vitro. {ECO:0000250|UniProtKB:P54652}.
CONFLICT 71 71 A -> R (in Ref. 1; AAA37859).
{ECO:0000305}.
CONFLICT 222 222 V -> L (in Ref. 1; AAA37859).
{ECO:0000305}.
SEQUENCE 633 AA; 69642 MW; 6F65773C7EFFA69F CRC64;
MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV
AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG KPKVQVEYKG EMKTFFPEEI
SSMVLTKMKE IAEAYLGGKV QSAVITVPAY FNDSQRQATK DAGTITGLNV LRIINEPTAA
AIAYGLDKKG CAGGEKNVLI FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM
VSHLAEEFKR KHKKDIGPNK RAVRRLRTAC ERAKRTLSSS TQASIEIDSL YEGVDFYTSI
TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ KLLQDFFNGK
ELNKSINPDE AVAYGAAVQA AILIGDKSEN VQDLLLLDVT PLSLGIETAG GVMTPLIKRN
TTIPTKQTQT FTTYSDNQSS VLVQVYEGER AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT
FDIDANGILN VTAADKSTGK ENKITITNDK GRLSKDDIDR MVQEAERYKS EDEANRDRVA
AKNAVESYTY NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK
ELERVCNPII SKLYQGGPGG GGSSGGPTIE EVD


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