ENPL_CATRO
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 03-AUG-2022, entry version 115.
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}.
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DR EMBL; L14594; AAA16785.1; -; mRNA.
DR PIR; S39558; S39558.
DR AlphaFoldDB; P35016; -.
DR SMR; P35016; -.
DR PRIDE; P35016; -.
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:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
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 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
