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78 kDa glucose-regulated protein (GRP-78) (Heat shock 70 kDa protein 5) (Immunoglobulin heavy chain-binding protein) (BiP)

 BIP_MOUSE               Reviewed;         655 AA.
P20029; O35642; Q3UFF2; Q61630;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 3.
18-JUL-2018, entry version 193.
RecName: Full=Endoplasmic reticulum chaperone BiP {ECO:0000305};
EC=3.6.4.10 {ECO:0000250|UniProtKB:P11021};
AltName: Full=78 kDa glucose-regulated protein {ECO:0000303|PubMed:7607546};
Short=GRP-78 {ECO:0000303|PubMed:7607546};
AltName: Full=Binding-immunoglobulin protein {ECO:0000303|PubMed:2895472};
Short=BiP {ECO:0000303|PubMed:2895472};
AltName: Full=Heat shock protein 70 family protein 5 {ECO:0000305};
Short=HSP70 family protein 5 {ECO:0000305};
AltName: Full=Heat shock protein family A member 5 {ECO:0000312|MGI:MGI:95835};
AltName: Full=Immunoglobulin heavy chain-binding protein {ECO:0000303|PubMed:2895472};
Flags: Precursor;
Name=Hspa5 {ECO:0000312|MGI:MGI:95835};
Synonyms=Grp78 {ECO:0000303|PubMed:7607546};
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 [MRNA].
TISSUE=Liver;
PubMed=2895472; DOI=10.1073/pnas.85.7.2250;
Haas I.G., Meo T.;
"cDNA cloning of the immunoglobulin heavy chain binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 85:2250-2254(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-46.
PubMed=2559088;
Kozutsumi Y., Normington K., Press E., Slaughter C., Sambrook J.,
Gething M.J.;
"Identification of immunoglobulin heavy chain binding protein as
glucose-regulated protein 78 on the basis of amino acid sequence,
immunological cross-reactivity, and functional activity.";
J. Cell Sci. Suppl. 11:115-137(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=8645260; DOI=10.1006/bbrc.1996.0313;
Kajiwara K., Nagawawa H., Shimizu-Nishikawa K., Ookura T., Kimura M.,
Sugaya E.;
"Molecular characterization of seizure-related genes isolated by
differential screening.";
Biochem. Biophys. Res. Commun. 219:795-799(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
STRAIN=C3B10RF1; TISSUE=Liver;
PubMed=7607546; DOI=10.1016/0378-1119(95)00083-I;
Tillman J.B., Mote P.L., Walford R.L., Spindler S.R.;
"Structure and regulation of the mouse GRP78 (BiP) promoter by glucose
and calcium ionophore.";
Gene 158:225-229(1995).
[7]
PROTEIN SEQUENCE OF 20-36.
TISSUE=Fibroblast;
PubMed=7523108; DOI=10.1002/elps.11501501101;
Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
"Separation and sequencing of familiar and novel murine proteins using
preparative two-dimensional gel electrophoresis.";
Electrophoresis 15:735-745(1994).
[8]
PROTEIN SEQUENCE OF 51-75; 140-153; 156-164; 166-182; 187-215;
308-337; 354-368; 449-493; 525-541 AND 623-634, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Klug S., Friebe K., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 488-655.
PubMed=2583523; DOI=10.1016/0378-1119(89)90054-1;
Parfett C.L.J., Hofbauer R., Brudzynski K., Edwards D.R.,
Denhardt D.T.;
"Differential screening of a cDNA library with cDNA probes amplified
in a heterologous host: isolation of murine GRP78 (BiP) and other
serum-regulated low-abundance mRNAs.";
Gene 82:291-303(1989).
[10]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[11]
INTERACTION WITH DNAJC1.
PubMed=12065409; DOI=10.1093/emboj/cdf315;
Dudek J., Volkmer J., Bies C., Guth S., Mueller A., Lerner M.,
Feick P., Schaefer K.-H., Morgenstern E., Hennessy F., Blatch G.L.,
Janoscheck K., Heim N., Scholtes P., Frien M., Nastainczyk W.,
Zimmermann R.;
"A novel type of co-chaperone mediates transmembrane recruitment of
DnaK-like chaperones to ribosomes.";
EMBO J. 21:2958-2967(2002).
[12]
INTERACTION WITH DNAJB9.
PubMed=11836248; DOI=10.1074/jbc.M112214200;
Shen Y., Meunier L., Hendershot L.M.;
"Identification and characterization of a novel endoplasmic reticulum
(ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro
and is induced by ER stress.";
J. Biol. Chem. 277:15947-15956(2002).
[13]
FUNCTION, AND INTERACTION WITH DNAJC10.
PubMed=12411443; DOI=10.1074/jbc.M206995200;
Cunnea P.M., Miranda-Vizuete A., Bertoli G., Simmen T.,
Damdimopoulos A.E., Hermann S., Leinonen S., Huikko M.P.,
Gustafsson J.-A., Sitia R., Spyrou G.;
"ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ
and thioredoxin domains, is expressed in secretory cells or following
ER stress.";
J. Biol. Chem. 278:1059-1066(2003).
[14]
NITRATION [LARGE SCALE ANALYSIS] AT TYR-161, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16800626; DOI=10.1021/bi060474w;
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
Squier T.C., Bigelow D.J.;
"Endogenously nitrated proteins in mouse brain: links to
neurodegenerative disease.";
Biochemistry 45:8009-8022(2006).
[15]
IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CELF1; CALR;
CALR3 AND HSP90B1.
PubMed=16931514; DOI=10.1074/jbc.M605701200;
Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H.,
Hershey J.W., Timchenko N.A.;
"Age-specific CUGBP1-eIF2 complex increases translation of
CCAAT/enhancer-binding protein beta in old liver.";
J. Biol. Chem. 281:32806-32819(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-644; THR-649 AND
SER-650, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, 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).
[19]
SUBCELLULAR LOCATION, AND INTERACTION WITH MX1.
PubMed=21992152; DOI=10.1089/jir.2010.0132;
Numajiri Haruki A., Naito T., Nishie T., Saito S., Nagata K.;
"Interferon-inducible antiviral protein MxA enhances cell death
triggered by endoplasmic reticulum stress.";
J. Interferon Cytokine Res. 31:847-856(2011).
[20]
METHYLATION AT LYS-586.
PubMed=23921388; DOI=10.1074/jbc.M113.483248;
Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S.,
Melki R., Falnes P.O.;
"Identification and characterization of a novel human
methyltransferase modulating Hsp70 function through lysine
methylation.";
J. Biol. Chem. 288:27752-27763(2013).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126; LYS-214; LYS-327 AND
LYS-354, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-448, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Endoplasmic reticulum chaperone that plays a key role in
protein folding and quality control in the endoplasmic reticulum
lumen (PubMed:12411443, PubMed:12475965). Involved in the correct
folding of proteins and degradation of misfolded proteins via its
interaction with DNAJC10/ERdj5, probably to facilitate the release
of DNAJC10/ERdj5 from its substrate (PubMed:12411443). Acts as a
key repressor of the ERN1/IRE1-mediated unfolded protein response
(UPR) (By similarity). In the unstressed endoplasmic reticulum,
recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1,
leading to disrupt the dimerization of ERN1/IRE1, thereby
inactivating ERN1/IRE1 (By similarity). Accumulation of misfolded
protein in the endoplasmic reticulum causes release of HSPA5/BiP
from ERN1/IRE1, allowing homodimerization and subsequent
activation of ERN1/IRE1 (By similarity).
{ECO:0000250|UniProtKB:G3I8R9, ECO:0000250|UniProtKB:P11021,
ECO:0000269|PubMed:12411443, ECO:0000269|PubMed:12475965}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000250|UniProtKB:G3I8R9}.
-!- ENZYME REGULATION: The chaperone activity is regulated by ATP-
induced allosteric coupling of the nucleotide-binding (NBD) and
substrate-binding (SBD) domains (By similarity). In the ADP-bound
and nucleotide-free (apo) states, the two domains have little
interaction (By similarity). In contrast, in the ATP-bound state
the two domains are tightly coupled, which results in drastically
accelerated kinetics in both binding and release of polypeptide
substrates (By similarity). J domain-containing co-chaperones
(DNAJB9/ERdj4 or DNAJC10/ERdj5) stimulate the ATPase activity and
are required for efficient substrate recognition by HSPA5/BiP.
Homooligomerization inactivates participating HSPA5/BiP protomers
and probably act as reservoirs to store HSPA5/BiP molecules when
they are not needed by the cell (By similarity).
{ECO:0000250|UniProtKB:G3I8R9, ECO:0000250|UniProtKB:P11021}.
-!- SUBUNIT: Monomer and homooligomer; homooligomerization via the
interdomain linker inactivates the chaperone activity and acts as
a storage of HSPA5/BiP molecules (By similarity). Interacts with
DNAJC1 (via J domain) (PubMed:12065409). Component of an EIF2
complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1,
EIF2S2, HSP90B1 and HSPA5 (PubMed:16931514). Part of a large
chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5,
HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small
amounts of ERP29, but not, or at very low levels, CALR nor CANX
(PubMed:12475965). Interacts with TMEM132A and TRIM21 (By
similarity). May form a complex with ERLEC1, OS9, SEL1L and SYVN1
(By similarity). Interacts with DNAJC10 (PubMed:12411443).
Interacts with DNAJB9/ERdj4; leading to recruit HSPA5/BiP to
ERN1/IRE1 (PubMed:11836248). Interacts with ERN1/IRE1; interaction
takes place following interaction with DNAJB9/ERdj4 and leads to
inactivate ERN1/IRE1 (By similarity). Interacts with MX1
(PubMed:21992152). Interacts with METTL23 (By similarity).
Interacts with CEMIP; the interaction induces calcium leakage from
the endoplasmic reticulum and cell migration (By similarity).
Interacts with PCSK4 form; the interaction takes place in the
endoplasmic reticulum (By similarity). Interacts with CIPC (By
similarity). Interacts with CCDC88B (via C-terminus); the
interaction opposes ERN1-mediated JNK activation, protecting
against apoptosis (By similarity). Interacts with INPP5K;
necessary for INPP5K localization at the endoplasmic reticulum (By
similarity). Interacts with MANF; the interaction is direct (By
similarity). Interacts with LOXL2; leading to activate the
ERN1/IRE1-XBP1 pathway of the unfolded protein response (By
similarity). {ECO:0000250|UniProtKB:G3I8R9,
ECO:0000250|UniProtKB:P11021, ECO:0000269|PubMed:11836248,
ECO:0000269|PubMed:12065409, ECO:0000269|PubMed:12411443,
ECO:0000269|PubMed:12475965, ECO:0000269|PubMed:16931514,
ECO:0000269|PubMed:21992152}.
-!- INTERACTION:
O35451:Atf6b; NbExp=2; IntAct=EBI-772325, EBI-8361741;
Q99KV1:Dnajb11; NbExp=4; IntAct=EBI-772325, EBI-8328260;
O75460:ERN1 (xeno); NbExp=2; IntAct=EBI-772325, EBI-371750;
P00441:SOD1 (xeno); NbExp=7; IntAct=EBI-772325, EBI-990792;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000255|PROSITE-ProRule:PRU10138,
ECO:0000269|PubMed:21992152}. Cytoplasm
{ECO:0000269|PubMed:21992152}.
-!- DOMAIN: The interdomain linker regulates the chaperone activity by
mediating the formation of homooligomers. Homooligomers are formed
by engagement of the interdomain linker of one HSPA5/BiP molecule
as a typical substrate of an adjacent HSPA5/BiP molecule.
HSPA5/BiP oligomerization inactivates participating HSPA5/BiP
protomers. HSPA5/BiP oligomers probably act as reservoirs to store
HSPA5/BiP molecules when they are not needed by the cell. When the
levels of unfolded proteins rise, cells can rapidly break up these
oligomers to make active monomers. {ECO:0000250|UniProtKB:G3I8R9}.
-!- PTM: In unstressed cells, AMPylation at Thr-519 by FICD
inactivates the chaperome activity: AMPylated form is locked in a
relatively inert state and only weakly stimulated by J domain-
containing proteins. In response to endoplasmic reticulum stress,
de-AMPylation by the same protein, FICD, restores the chaperone
activity. {ECO:0000250|UniProtKB:G3I8R9}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
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EMBL; AJ002387; CAA05361.1; -; mRNA.
EMBL; M19351; AAA37315.1; -; mRNA.
EMBL; D78645; BAA11462.1; -; mRNA.
EMBL; AK076079; BAC36166.1; -; mRNA.
EMBL; AK146647; BAE27328.1; -; mRNA.
EMBL; AK148539; BAE28609.1; -; mRNA.
EMBL; AK151647; BAE30576.1; -; mRNA.
EMBL; AK152020; BAE30882.1; -; mRNA.
EMBL; AK166739; BAE38982.1; -; mRNA.
EMBL; AK169034; BAE40825.1; -; mRNA.
EMBL; BC050927; AAH50927.1; -; mRNA.
EMBL; U16277; AAA76734.1; -; Genomic_DNA.
EMBL; M30779; AAA37742.1; -; mRNA.
CCDS; CCDS15950.1; -.
PIR; A37048; A37048.
RefSeq; NP_001156906.1; NM_001163434.1.
RefSeq; NP_071705.3; NM_022310.3.
UniGene; Mm.330160; -.
UniGene; Mm.470180; -.
UniGene; Mm.474909; -.
ProteinModelPortal; P20029; -.
SMR; P20029; -.
BioGrid; 200078; 44.
CORUM; P20029; -.
DIP; DIP-32341N; -.
IntAct; P20029; 34.
MINT; P20029; -.
STRING; 10090.ENSMUSP00000028222; -.
CarbonylDB; P20029; -.
iPTMnet; P20029; -.
PhosphoSitePlus; P20029; -.
SwissPalm; P20029; -.
COMPLUYEAST-2DPAGE; P20029; -.
REPRODUCTION-2DPAGE; IPI00319992; -.
REPRODUCTION-2DPAGE; P20029; -.
SWISS-2DPAGE; P20029; -.
UCD-2DPAGE; P20029; -.
EPD; P20029; -.
MaxQB; P20029; -.
PaxDb; P20029; -.
PeptideAtlas; P20029; -.
PRIDE; P20029; -.
TopDownProteomics; P20029; -.
Ensembl; ENSMUST00000028222; ENSMUSP00000028222; ENSMUSG00000026864.
Ensembl; ENSMUST00000100171; ENSMUSP00000097747; ENSMUSG00000026864.
GeneID; 14828; -.
KEGG; mmu:14828; -.
UCSC; uc008jis.2; mouse.
CTD; 3309; -.
MGI; MGI:95835; Hspa5.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00910000144045; -.
HOGENOM; HOG000228135; -.
HOVERGEN; HBG051845; -.
InParanoid; P20029; -.
KO; K09490; -.
OMA; CVGVMQK; -.
OrthoDB; EOG091G0352; -.
PhylomeDB; P20029; -.
TreeFam; TF105044; -.
Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
ChiTaRS; Hspa5; mouse.
PRO; PR:P20029; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026864; -.
CleanEx; MM_HSPA5; -.
ExpressionAtlas; P20029; baseline and differential.
Genevisible; P20029; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IDA:ParkinsonsUK-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:BHF-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0030496; C:midbody; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0051787; F:misfolded protein binding; IDA:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0043022; F:ribosome binding; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl.
GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0042149; P:cellular response to glucose starvation; ISO:MGI.
GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
GO; GO:0071287; P:cellular response to manganese ion; IEA:Ensembl.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:BHF-UCL.
GO; GO:0021589; P:cerebellum structural organization; IMP:BHF-UCL.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:BHF-UCL.
GO; GO:0006983; P:ER overload response; IDA:MGI.
GO; GO:0035437; P:maintenance of protein localization in endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; ISS:UniProtKB.
GO; GO:0090074; P:negative regulation of protein homodimerization activity; ISS:UniProtKB.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IGI:MGI.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0040019; P:positive regulation of embryonic development; TAS:BHF-UCL.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:BHF-UCL.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:BHF-UCL.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:MGI.
GO; GO:1904313; P:response to methamphetamine hydrochloride; IEA:Ensembl.
GO; GO:0097501; P:stress response to metal ion; IEA:Ensembl.
GO; GO:1901998; P:toxin transport; 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; PS00014; ER_TARGET; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Endoplasmic reticulum; Hydrolase;
Isopeptide bond; Methylation; Nitration; Nucleotide-binding;
Phosphoprotein; Reference proteome; Signal; Ubl conjugation.
SIGNAL 1 19 {ECO:0000269|PubMed:2559088,
ECO:0000269|PubMed:7523108}.
CHAIN 20 655 Endoplasmic reticulum chaperone BiP.
/FTId=PRO_0000013568.
NP_BIND 37 40 ATP. {ECO:0000250|UniProtKB:P11021}.
NP_BIND 228 230 ATP. {ECO:0000250|UniProtKB:P11021}.
NP_BIND 294 301 ATP. {ECO:0000250|UniProtKB:P11021}.
NP_BIND 365 368 ATP. {ECO:0000250|UniProtKB:P11021}.
REGION 126 281 Nucleotide-binding (NBD).
{ECO:0000250|UniProtKB:P11021}.
REGION 410 420 Interdomain linker.
{ECO:0000250|UniProtKB:G3I8R9}.
REGION 421 501 Substrate-binding (SBD).
{ECO:0000250|UniProtKB:P11021}.
MOTIF 652 655 Prevents secretion from ER.
BINDING 97 97 ATP. {ECO:0000250|UniProtKB:P11021}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:P06761}.
MOD_RES 126 126 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 161 161 Nitrated tyrosine.
{ECO:0000244|PubMed:16800626}.
MOD_RES 214 214 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 272 272 N6-acetyllysine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 327 327 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 354 354 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 448 448 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 493 493 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 519 519 O-AMP-threonine; alternate.
{ECO:0000250|UniProtKB:G3I8R9}.
MOD_RES 519 519 Phosphothreonine; alternate.
{ECO:0000250|UniProtKB:P11021}.
MOD_RES 586 586 N6,N6,N6-trimethyllysine; by METTL21A; in
vitro. {ECO:0000269|PubMed:23921388}.
MOD_RES 586 586 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P11021}.
MOD_RES 586 586 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P11021}.
MOD_RES 592 592 N6-methyllysine.
{ECO:0000250|UniProtKB:P11021}.
MOD_RES 644 644 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 649 649 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 650 650 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
CROSSLNK 353 353 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11021}.
CROSSLNK 354 354 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P11021}.
CONFLICT 43 43 V -> F (in Ref. 3; BAA11462).
{ECO:0000305}.
CONFLICT 245 245 V -> W (in Ref. 3; BAA11462).
{ECO:0000305}.
CONFLICT 329 329 E -> G (in Ref. 3; BAA11462).
{ECO:0000305}.
CONFLICT 361 361 V -> A (in Ref. 3; BAA11462).
{ECO:0000305}.
CONFLICT 474 474 T -> R (in Ref. 1; CAA05361).
{ECO:0000305}.
CONFLICT 591 591 D -> G (in Ref. 9; AAA37742).
{ECO:0000305}.
CONFLICT 596 596 E -> K (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 655 AA; 72422 MW; AFB795D15E20FAC2 CRC64;
MMKFTVVAAA LLLLGAVRAE EEDKKEDVGT VVGIDLGTTY SCVGVFKNGR VEIIANDQGN
RITPSYVAFT PEGERLIGDA AKNQLTSNPE NTVFDAKRLI GRTWNDPSVQ QDIKFLPFKV
VEKKTKPYIQ VDIGGGQTKT FAPEEISAMV LTKMKETAEA YLGKKVTHAV VTVPAYFNDA
QRQATKDAGT IAGLNVMRII NEPTAAAIAY GLDKREGEKN ILVFDLGGGT FDVSLLTIDN
GVFEVVATNG DTHLGGEDFD QRVMEHFIKL YKKKTGKDVR KDNRAVQKLR REVEKAKRAL
SSQHQARIEI ESFFEGEDFS ETLTRAKFEE LNMDLFRSTM KPVQKVLEDS DLKKSDIDEI
VLVGGSTRIP KIQQLVKEFF NGKEPSRGIN PDEAVAYGAA VQAGVLSGDQ DTGDLVLLDV
CPLTLGIETV GGVMTKLIPR NTVVPTKKSQ IFSTASDNQP TVTIKVYEGE RPLTKDNHLL
GTFDLTGIPP APRGVPQIEV TFEIDVNGIL RVTAEDKGTG NKNKITITND QNRLTPEEIE
RMVNDAEKFA EEDKKLKERI DTRNELESYA YSLKNQIGDK EKLGGKLSSE DKETMEKAVE
EKIEWLESHQ DADIEDFKAK KKELEEIVQP IISKLYGSGG PPPTGEEDTS EKDEL


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