ID ENPL_CATRO Reviewed; 817 AA. AC P35016; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 24-JAN-2024, entry version 120. DE RecName: Full=Endoplasmin homolog; DE AltName: Full=Glucose-regulated protein 94 homolog; DE Short=GRP-94 homolog; DE Flags: Precursor; GN Name=HSP90; OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae; OC Catharanthinae; Catharanthus. OX NCBI_TaxID=4058; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. CP3A; RX PubMed=8106014; DOI=10.1007/bf00019305; RA Schroeder G., Beck M., Eichel J., Vetter H.P., Schroeder J.; RT "HSP90 homologue from Madagascar periwinkle (Catharanthus roseus): cDNA RT sequence, regulation of protein expression and location in the endoplasmic RT reticulum."; RL Plant Mol. Biol. 23:583-594(1993). CC -!- FUNCTION: May have a molecular chaperone role in the processing of CC secreted materials. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. CC -!- TISSUE SPECIFICITY: Not detected in extracts from young plants unless CC they are exposed to heat shock for several hours. Found to be CC constitutively expressed in cell cultures. CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L14594; AAA16785.1; -; mRNA. DR PIR; S39558; S39558. DR AlphaFoldDB; P35016; -. DR SMR; P35016; -. DR GlyCosmos; P35016; 5 sites, No reported glycans. DR GO; GO:0005788; C:endoplasmic 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 CDD; cd16927; HATPase_Hsp90-like; 1. 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 Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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_Su5_D2-typ_SF. DR PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1. DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1. DR Pfam; PF13589; HATPase_c_3; 1. DR Pfam; PF00183; HSP90; 1. DR PIRSF; PIRSF002583; Hsp90; 1. DR PRINTS; PR00775; HEATSHOCK90. DR SMART; SM00387; HATPase_c; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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. DR PROSITE; PS00298; HSP90; 1. PE 2: Evidence at transcript level; KW ATP-binding; Calcium; Chaperone; Endoplasmic reticulum; Glycoprotein; KW Nucleotide-binding; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..817 FT /note="Endoplasmin homolog" FT /id="PRO_0000013602" FT REGION 31..58 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 293..333 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 777..817 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 814..817 FT /note="Prevents secretion from ER" FT COMPBIAS 293..323 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 111 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P41148" FT BINDING 155 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P41148" FT BINDING 168 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P41148" FT BINDING 200 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P41148" FT SITE 459 FT /note="Important for ATP hydrolysis" FT /evidence="ECO:0000250|UniProtKB:P41148" FT CARBOHYD 111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 306 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 416 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 456 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 624 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 817 AA; 93492 MW; 26C06CDC5E0D19FA CRC64; MRKWTVPSVL FLLCPSLSSS CQGRKIHANA EADSDAPVDP PKVEDKIGAV PNGLSTDSDV AKREAESMSM RNLRSDAEKF EFQAEVSRLM DIIINSLYSN KDIFLRELIS NASDALDKIR FLALTDKEIL GEGDTAKLEI QIKLDKEKKI LSIRDRGIGM TKEDLIKNLG TIAKSGTSAF VEKMQTSGDL NLIGQFGVGF YSVYLVPDYV EVISKHNDDK QYIWESKADG AFAISEDVWN EPLGRGTEIR LHLRDEAQEY LDEFKLKELV KRYSEFINFP IYLWASKEVE VEVPAEEDDS SDDEDNKSES SSSEEGEEEE TEKEEDEKKP KTKKVKETTY EWELLNDMKA IWLRNPKDVT DDEYTKFYHS LAKDFSEEKP LAWSHFTAEG DVEFKAFTLL PPKAPQDLYE SYYNSNKSNL KLYVRRVFIS DEFDELLPKY LNFLKGLVDS DTLPLNVSRE MLQQHSSLKT IKKKLIRKAL DMIRKIADED PDEANDKDKK EVEESTDNDE KKGQYAKFWN EFGKSIKLGI IEDAANRNRL AKLLRFESTK SEGKLTSLDQ YISRMKSGQK DIFYITGTSK EQLEKSPFLE RLTKKNYEVI LFTDPVDEYL MQYLMDYEDK KFQNVSKEGL KIGKDSKDKE LKESFKELTK WWKGALASEN VDDVKISNRL ANTPCVVVTS KYGWSSNMER IMQSQTLSDA SKQAYMRGKR VLEINPRHPI IKELRERVVK DAEDESVKQT ARLMYQTALM ESGFMLNDPK EFASSIYDSV KSSLKISPDA TVEEEDDTEE AEAESGTTES SAAEDAGAET LDLKDEL //