ENPL_MESAU
ID ENPL_MESAU Reviewed; 400 AA.
AC P08712;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Endoplasmin;
DE AltName: Full=94 kDa glucose-regulated protein;
DE Short=GRP-94;
DE AltName: Full=Heat shock protein 90 kDa beta member 1;
DE Flags: Fragment;
GN Name=HSP90B1; Synonyms=GRP94;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3612810; DOI=10.1016/0022-2836(87)90380-9;
RA Sorger P.K., Pelham H.R.B.;
RT "The glucose-regulated protein grp94 is related to heat shock protein
RT hsp90.";
RL J. Mol. Biol. 194:341-344(1987).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
CC -!- FUNCTION: Molecular chaperone that functions in the processing and
CC transport of secreted proteins. When associated with CNPY3, required
CC for proper folding of Toll-like receptors. Functions in endoplasmic
CC reticulum associated degradation (ERAD). Has ATPase activity. May
CC participate in the unfolding of cytosolic leaderless cargos (lacking
CC the secretion signal sequence) such as the interleukin 1/IL-1 to
CC facilitate their translocation into the ERGIC (endoplasmic reticulum-
CC Golgi intermediate compartment) and secretion; the translocation
CC process is mediated by the cargo receptor TMED10 (By similarity).
CC {ECO:0000250|UniProtKB:P08113, ECO:0000250|UniProtKB:P14625}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Component of an EIF2 complex at
CC least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1
CC and HSPA5 (By similarity). Part of a large chaperone multiprotein
CC complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6,
CC PPIB, SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at
CC very low levels, CALR nor CANX. Interacts with AIMP1; regulates its
CC retention in the endoplasmic reticulum. Interacts with OS9 (By
CC similarity). Interacts with CNPY3; this interaction is disrupted in the
CC presence of ATP. Interacts with several TLRs, including TLR4 and TLR9,
CC but not with TLR3 (By similarity). Interacts with MZB1 in a calcium-
CC dependent manner (By similarity). Interacts with METTL23 (By
CC similarity). Interacts with IL1B; the interaction facilitates cargo
CC translocation into the ERGIC (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P14625}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q66HD0}. Sarcoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P41148}. Melanosome
CC {ECO:0000250|UniProtKB:P14625}.
CC -!- TISSUE SPECIFICITY: Detected in the acrosome of the caput epididymal
CC spermatazoa, not detected in the cauda epididymal spermatazoa (at
CC protein level). {ECO:0000269|PubMed:20400973}.
CC -!- INDUCTION: The synthesis of this protein is stimulated when fibroblasts
CC are deprived of glucose.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; X04850; CAA28541.1; -; mRNA.
DR PIR; A26258; A26258.
DR AlphaFoldDB; P08712; -.
DR SMR; P08712; -.
DR STRING; 10036.XP_005068020.1; -.
DR eggNOG; KOG0020; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR Gene3D; 1.20.120.790; -; 1.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF00183; HSP90; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Calcium; Chaperone; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Sarcoplasmic reticulum.
FT CHAIN <1..400
FT /note="Endoplasmin"
FT /id="PRO_0000062926"
FT REGION 346..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 397..400
FT /note="Prevents secretion from ER"
FT COMPBIAS 350..389
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 45
FT /note="Important for ATP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT MOD_RES 1
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT MOD_RES 76
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 230
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ SEQUENCE 400 AA; 46794 MW; 3419AD98410EEB80 CRC64;
KKSDYIKLYV RRVFITDDFH DMMPKYLNFV KGVVDSDDLP LNVSRETLQQ HKLLKVIRKK
LVRKTLDMIK KIADEKYNDT FWKEFGTNIK LGVIEDHSNR TRLAKLLRFQ SSHHSTDITS
LDQYVERMKE KQDKIYFMAG SSRKEAESSP FVERLLKKGY EVIYLTEPVD EYCIQALPEF
DGKRFQNVAK EGVKFDESEK TKENREATEK EFEPLLNWMK DKALKDKIEK AVVSQRLTES
PCALVASQYG WSGNMERIMK AQAYQTGKDI STNYYASQKK TFEINPRHPL IRDMLRRVKE
DEDDKTVLDL AVVLFETATL RSGYLLPDTK AYADRIERML RLSLNIDPEA QVEEEPEEEP
EDTTEDTEQD EEEEVDAGTE EEEEEEQETA KESTAEKDEL
