Legends: 1, INIT_MET Removed. {ECO:0000250|UniProtKB:P0DMV8}; 2, BINDING ATP. {ECO:0000250}; 3, N-acetylalanine. {ECO:0000250|UniProtKB:P0DMV8}; 4, N6-acetyllysine. {ECO:0000250|UniProtKB:P0DMV8}; 5, Omega-N-methylarginine. {ECO:0000250|UniProtKB:P0DMV8}; 6, N6,N6,N6-trimethyllysine; by METTL21A; alternate. {ECO:0000250}; 7, N6,N6-dimethyllysine; alternate. {ECO:0000250|UniProtKB:P0DMV8}; 8, Phosphoserine. {ECO:0000250|UniProtKB:P0DMV8}; 9, Phosphothreonine. {ECO:0000250|UniProtKB:P0DMV8}; 10, CONFLICT I -> N (in Ref. 1; CAH91519). {ECO:0000305}; 11, CONFLICT L -> P (in Ref. 1; CAH91519). {ECO:0000305}; 12, NP_BIND ATP. {ECO:0000250}; 13, ipat:HSP70_2 [T]; 14, ipat:HSP70_1 [T]; 15, ipat:HSP70_3 [T].
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ID HSP71_PONAB Reviewed; 641 AA.
AC Q5R7D3; Q5R9P1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 30-NOV-2016, entry version 85.
DE RecName: Full=Heat shock 70 kDa protein 1;
GN Name=HSPA1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
CC preexistent proteins against aggregation and mediate the folding
CC of newly translated polypeptides in the cytosol as well as within
CC organelles. These chaperones participate in all these processes
CC through their ability to recognize nonnative conformations of
CC other proteins. They bind extended peptide segments with a net
CC hydrophobic character exposed by polypeptides during translation
CC and membrane translocation, or following stress-induced damage.
CC Essential for STUB1-mediated ubiquitination and degradation of
CC FOXP3 in regulatory T-cells (Treg) during inflammation.
CC {ECO:0000250|UniProtKB:P08107}.
CC -!- SUBUNIT: Component of the CatSper complex (By similarity).
CC Identified in a IGF2BP1-dependent mRNP granule complex containing
CC untranslated mRNAs. Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C
CC and TSC2. Interacts with TERT; the interaction occurs in the
CC absence of the RNA component, TERC, and dissociates once the TERT
CC complex has formed. Interacts with TRIM5 (via B30.2/SPRY domain).
CC Interacts with PARK2. Interacts with FOXP3. Interacts with DNAJC9
CC (via J domain). {ECO:0000250|UniProtKB:P08107,
CC ECO:0000250|UniProtKB:P0DMV8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000305}.
DR EMBL; CR859344; CAH91519.1; -; mRNA.
DR EMBL; CR860185; CAH92327.1; -; mRNA.
DR RefSeq; NP_001125893.1; NM_001132421.2.
DR ProteinModelPortal; Q5R7D3; -.
DR SMR; Q5R7D3; -.
DR STRING; 9601.ENSPPYP00000018408; -.
DR PRIDE; Q5R7D3; -.
DR Ensembl; ENSPPYT00000019143; ENSPPYP00000018408; ENSPPYG00000016463.
DR GeneID; 100172826; -.
DR KEGG; pon:100172826; -.
DR CTD; 3303; -.
DR eggNOG; KOG0101; Eukaryota.
DR eggNOG; COG0443; LUCA.
DR GeneTree; ENSGT00820000127001; -.
DR HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG051845; -.
DR InParanoid; Q5R7D3; -.
DR KO; K03283; -.
DR OMA; SCREQAG; -.
DR OrthoDB; EOG091G03SF; -.
DR TreeFam; TF105042; -.
DR Proteomes; UP000001595; Chromosome 6.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C.
DR InterPro; IPR029047; HSP70_peptide-bd.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
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 Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Methylation; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Stress response.
FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P0DMV8}.
FT CHAIN 2 641 Heat shock 70 kDa protein 1.
FT /FTId=PRO_0000314292.
FT NP_BIND 12 15 ATP. {ECO:0000250}.
FT NP_BIND 202 204 ATP. {ECO:0000250}.
FT NP_BIND 268 275 ATP. {ECO:0000250}.
FT NP_BIND 339 342 ATP. {ECO:0000250}.
FT BINDING 71 71 ATP. {ECO:0000250}.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 108 108 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 246 246 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 348 348 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 469 469 Omega-N-methylarginine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A;
FT alternate. {ECO:0000250}.
FT MOD_RES 561 561 N6,N6-dimethyllysine; alternate.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 631 631 Phosphoserine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 633 633 Phosphoserine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT MOD_RES 636 636 Phosphothreonine.
FT {ECO:0000250|UniProtKB:P0DMV8}.
FT CONFLICT 95 95 I -> N (in Ref. 1; CAH91519).
FT {ECO:0000305}.
FT CONFLICT 461 461 L -> P (in Ref. 1; CAH91519).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 197 210 ipat:HSP70_2 [T]
FT MYHIT 6 611 ipfam:HSP70 [T]
FT MYHIT 9 16 ipat:HSP70_1 [T]
FT MYHIT 334 348 ipat:HSP70_3 [T]
SQ SEQUENCE 641 AA; 70052 MW; 78F513118C96DE66 CRC64;
MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS
SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN
ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE
QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D
//
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