ENPL_PONAB
ID ENPL_PONAB Reviewed; 804 AA.
AC Q5R6F7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Endoplasmin;
DE AltName: Full=Heat shock protein 90 kDa beta member 1;
DE Flags: Precursor;
GN Name=HSP90B1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; CR860533; CAH92659.1; -; mRNA.
DR RefSeq; NP_001127573.1; NM_001134101.1.
DR AlphaFoldDB; Q5R6F7; -.
DR SMR; Q5R6F7; -.
DR STRING; 9601.ENSPPYP00000001345; -.
DR GeneID; 100174651; -.
DR KEGG; pon:100174651; -.
DR CTD; 7184; -.
DR eggNOG; KOG0020; Eukaryota.
DR InParanoid; Q5R6F7; -.
DR OrthoDB; 924636at2759; -.
DR Proteomes; UP000001595; 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:0019899; F:enzyme binding; IEA:UniProt.
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 Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Calcium; Chaperone; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Hydroxylation; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Sarcoplasmic reticulum; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..804
FT /note="Endoplasmin"
FT /id="PRO_0000233905"
FT REGION 288..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 801..804
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT COMPBIAS 290..314
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..790
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT SITE 448
FT /note="Important for ATP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT MOD_RES 168
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HD0"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HD0"
FT MOD_RES 404
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT MOD_RES 479
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 633
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 786
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 138
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 804 AA; 92581 MW; A186DD33F6DAD947 CRC64;
MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ REEEAIQLDG
LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF LRELISNASD ALDKIRLISL
TDENALSGNE ELTVKIKCDK EKNLLHVTDT GVGMTREELV KNLGTIAKSG TSEFLNKMTE
AQEDGQSTSE LIGQFGVGFC SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT
LGRGTTITLV LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK
EEKEESDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV EEDEYKAFYK
SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD
DFHDMMPKYL NFVKGVVDSD DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADDKY
NDTFWKEFGT NIKLGVIEDH SNRTRLAKLL RFQSSHHPTD ITSLDQYVER MKEKQDKIYF
MAGSSRKEAE SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
SEKTKESREA IEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS QYGWSGNMER
IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR IKEDEDDKTV LDLAVVLFET
ATLRSGYLLP DTKAYGDRIE RMLRLSLNID PDAKVEEEPE EEPEETTEDT TEDTEQDEDE
EMDVGTDEEE QETAKESTAE KDEL
