HSP13_PONAB
ID HSP13_PONAB Reviewed; 471 AA.
AC Q5R8D9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Heat shock 70 kDa protein 13;
DE AltName: Full=Stress-70 protein chaperone microsome-associated 60 kDa protein;
DE Flags: Precursor;
GN Name=HSPA13; Synonyms=STCH;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR859814; CAH91971.1; -; mRNA.
DR RefSeq; NP_001126142.1; NM_001132670.1.
DR AlphaFoldDB; Q5R8D9; -.
DR SMR; Q5R8D9; -.
DR GeneID; 100173100; -.
DR KEGG; pon:100173100; -.
DR CTD; 6782; -.
DR InParanoid; Q5R8D9; -.
DR OrthoDB; 288077at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding; Endoplasmic reticulum; Microsome; Nucleotide-binding;
KW 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_0000013560"
FT REGION 314..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 51941 MW; E5E0ADDB2BB89CB8 CRC64;
MAREMTILGS AVLTLLLAGY LAQQYLPLPT PKVIGIDLGT TYCSVGVFFP GTGKVKVIPD
ENGHISIPSM VSFTDNDVYV GYESVELADS NPQNTIYDAK RFIGKIFTPE ELEAEIGRYP
FKVLNKNGMV EFSVTSNETI TVSPEYVGSR LLLKLKEMAE AYLGMPVANA VISVPAEFDL
KQRNSTIEAA NLAGLKILRV INEPTAAAMA YGLHKADVFH VLVIDLGGGT LDVSLLNKQG
GMFLTRAMSG NNKLGGQDFN QRLLQYLYKQ IYQTYGFVPS RKEEIHRLRQ SVEMVKLNLT
LHQSAQLSAL LTVEEQDRKE PHSSDTELPK DKLSSADDHR VNSGFGRGLS DKKSGESQVL
FETEISRKLF DTLNEDLFQK ILVPIQQVLK EGHLEKTEID EVVLVGGSTR IPRIRQVIQE
FFGKDPNTSV DPDLAVVTGV AIQAGIDGGS WPLQVSALEI PNKHLQKTNF N