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   24-JAN-2024, entry version 131.
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.ENSMAUP00000021968; -.
DR   GlyCosmos; P08712; 3 sites, No reported glycans.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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
//