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Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1) (Fragment)

 ENPL_RABIT              Reviewed;         716 AA.
O18750;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 121.
RecName: Full=Endoplasmin;
AltName: Full=94 kDa glucose-regulated protein;
Short=GRP-94;
AltName: Full=Heat shock protein 90 kDa beta member 1;
Flags: Fragment;
Name=HSP90B1; Synonyms=GRP94;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=New Zealand white;
PubMed=9601063; DOI=10.1042/bj3320351;
Vitadello M., Colpo P., Gorza L.;
"Rabbit cardiac and skeletal myocytes differ in constitutive and
inducible expression of the glucose-regulated protein GRP94.";
Biochem. J. 332:351-359(1998).
-!- FUNCTION: Molecular chaperone that functions in the processing and
transport of secreted proteins. When associated with CNPY3,
required for proper folding of Toll-like receptors. Functions in
endoplasmic reticulum associated degradation (ERAD). Has ATPase
activity (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer; disulfide-linked. Component of an EIF2 complex
at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2,
HSP90B1 and HSPA5 (By similarity). 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. Interacts
with AIMP1; regulates its retention in the endoplasmic reticulum.
Interacts with OS9 (By similarity). Interacts with CNPY3; this
interaction is disrupted in the presence of ATP. Interacts with
several TLRs, including TLR4 and TLR9, but not with TLR3 (By
similarity). Interacts with MZB1 in a calcium-dependent manner (By
similarity). Interacts with METTL23 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome
{ECO:0000250}.
-!- PTM: Phosphorylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
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EMBL; AF001631; AAC48853.1; -; mRNA.
UniGene; Ocu.4906; -.
ProteinModelPortal; O18750; -.
SMR; O18750; -.
PRIDE; O18750; -.
HOVERGEN; HBG007374; -.
InParanoid; O18750; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
CDD; cd00075; HATPase_c; 1.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR019805; Heat_shock_protein_90_CS.
InterPro; IPR037196; HSP90_C.
InterPro; IPR001404; Hsp90_fam.
InterPro; IPR020575; Hsp90_N.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR11528; PTHR11528; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00183; HSP90; 1.
PIRSF; PIRSF002583; Hsp90; 1.
PRINTS; PR00775; HEATSHOCK90.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF110942; SSF110942; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 2.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00298; HSP90; 1.
2: Evidence at transcript level;
Acetylation; ATP-binding; Calcium; Chaperone; Complete proteome;
Disulfide bond; Endoplasmic reticulum; Glycoprotein;
Nucleotide-binding; Phosphoprotein; Reference proteome.
CHAIN <1 716 Endoplasmin.
/FTId=PRO_0000062927.
MOTIF 713 716 Prevents secretion from ER.
{ECO:0000255}.
BINDING 28 28 ATP. {ECO:0000250}.
BINDING 70 70 ATP. {ECO:0000250}.
BINDING 83 83 ATP. {ECO:0000250}.
BINDING 89 89 ATP. {ECO:0000250}.
BINDING 120 120 ATP; via amide nitrogen. {ECO:0000250}.
BINDING 368 368 ATP. {ECO:0000250}.
MOD_RES 93 93 Phosphoserine.
{ECO:0000250|UniProtKB:Q66HD0}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000250|UniProtKB:Q66HD0}.
MOD_RES 324 324 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08113}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000250|UniProtKB:P14625}.
MOD_RES 399 399 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08113}.
MOD_RES 552 552 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08113}.
MOD_RES 696 696 Phosphothreonine.
{ECO:0000250|UniProtKB:P14625}.
CARBOHYD 28 28 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 421 421 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 59 59 Interchain. {ECO:0000250}.
NON_TER 1 1
SEQUENCE 716 AA; 82608 MW; 7098C6442F0EC84B CRC64;
AEVNRMMKLI INSLYKNKEI FLRELISNAS DALDKIRLIS LTDEQALSGN EELTVKIKCD
KEKNLLHVTD TGVGMTREEL VKNLGTIAKS GTSEFLNKMT EAQEDGQSTS ELIGQFGVGF
YSAFLVADKV IVTSKHNNDT QHIWESDSNE FSVIADPRGN TLGRGTTITL VLKEEASDYL
ELDTIKNLVK KYSQFINFPI YVWSSKTETV EEPAGEEEAA KEEKEEAVDE AAVEEEEEEK
KPKTKKVEKQ VWDWELMNDI KPIWQRPSKE VEEDEYKAFY KSFSKESDDP MAYIHFTAEE
STFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD DFHDMMPKYL NFVKGVVDSD
DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADEKY NDDTFWKGTN IKLGVIEDHS
NRTRLAKLLR FQSSHHPTDI TSLDQYVERM KEKQDKIYFM AGASRKEAES SPFVERLLKK
GYEVIYLTEP VDEYCIQALP EFDGKRFQNV AKEGVKFDES EKTKESREAT EKEFEPLLNW
MKDKALKDKI EKAVVSQRLT ESPCALVASQ YGWSANMERI MKAQAYQTGK DSTKYYASQK
TFEINPRHPL IRDMLRIKED DKTVMDLAVV LFETAILRSG YLLPDTKAYG DRIERIVRLS
LNIDPDAKVE EEPEEEPEDT TEDTEQDEEE EMDAGTDEQE QEQEPEKKST AEKDEL


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