HSP13_RAT
ID HSP13_RAT Reviewed; 471 AA.
AC O35162; Q6IRE1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Heat shock 70 kDa protein 13;
DE AltName: Full=Microsomal stress-70 protein ATPase core;
DE AltName: Full=Stress-70 protein chaperone microsome-associated 60 kDa protein;
DE Flags: Precursor;
GN Name=Hspa13; Synonyms=Stch;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8131751; DOI=10.1002/j.1460-2075.1994.tb06371.x;
RA Otterson G.A., Flynn G.C., Kratzke R.A., Coxon A., Johnston P.G.,
RA Kaye F.J.;
RT "Stch encodes the 'ATPase core' of a microsomal stress 70 protein.";
RL EMBO J. 13:1216-1225(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9358068; DOI=10.1016/s0378-1119(97)00383-1;
RA Otterson G.A., Kaye F.J.;
RT "A 'core ATPase', Hsp70-like structure is conserved in human, rat, and C.
RT elegans STCH proteins.";
RL Gene 199:287-292(1997).
RN [3]
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Has peptide-independent ATPase activity. {ECO:0000250}.
CC -!- SUBUNIT: Binds UBQLN2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AF006617; AAB88258.1; -; mRNA.
DR EMBL; BC070954; AAH70954.1; -; mRNA.
DR RefSeq; NP_062144.2; NM_019271.2.
DR AlphaFoldDB; O35162; -.
DR SMR; O35162; -.
DR STRING; 10116.ENSRNOP00000049545; -.
DR GlyGen; O35162; 1 site, 4 N-linked glycans (1 site).
DR iPTMnet; O35162; -.
DR jPOST; O35162; -.
DR PaxDb; O35162; -.
DR PRIDE; O35162; -.
DR Ensembl; ENSRNOT00000109029; ENSRNOP00000095281; ENSRNOG00000060979.
DR GeneID; 29734; -.
DR KEGG; rno:29734; -.
DR UCSC; RGD:3775; rat.
DR CTD; 6782; -.
DR RGD; 3775; Hspa13.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00890000139503; -.
DR HOGENOM; CLU_005965_0_3_1; -.
DR InParanoid; O35162; -.
DR OMA; LRKTNFN; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; O35162; -.
DR TreeFam; TF105047; -.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:O35162; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000060979; Expressed in Ammon's horn and 19 other tissues.
DR ExpressionAtlas; O35162; baseline and differential.
DR Genevisible; O35162; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd10237; HSPA13-like_NBD; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR InterPro; IPR042048; HSPA13.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 2.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Endoplasmic reticulum; Glycoprotein; Microsome;
KW Nucleotide-binding; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..471
FT /note="Heat shock 70 kDa protein 13"
FT /id="PRO_0000013561"
FT REGION 316..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CONFLICT 355
FT /note="G -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="S -> C (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 51795 MW; 24134E56E195FCDC CRC64;
MAGEMTILGS AVLTLLLAGY LAQQYLPLPT PKVIGIDLGT TYCSVGVFFP GTGKVKVIPD
ENGHISIPSM VSFTDGDVYV GYESLELADS NPQNTIYDAK RFIGKIFTPE ELEAEIGRYP
FKVLHKNGMA EFSVTSNETI IVSPEYVGSR LLLKLKEMAE KYLGMPVANA VISVPAEFDL
QQRNSTIQAA NLAGLKILRV INEPTAAAMA YGLHKVDVFY VLVIDLGGGT LDVSLLNKQG
GMFLTRAMSG NNKLGGQDFN QRLLQYLYKE IYQTYGFLPS RKEEIHRLRQ AVEMVKLNLT
LHQSAQVSVL LTVEENDSQK PQNADSKLPE DQLTPGDGHH VNRVFRPGLS DSTSGKSQVL
FETEVSRKLF NTLNEDLFQK ILVPIQQVLK EGLLDKTEID EVVLVGGSTR IPRIRQVIQE
FFGKDPNTSV DPDLAVVTGV AIQAGIDGGS WPLQVSALEI PNKHLQKTNF N
