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Endoplasmin homolog (Glucose-regulated protein 94 homolog) (GRP-94 homolog)

 ENPL_CATRO              Reviewed;         817 AA.
P35016;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
25-OCT-2017, entry version 102.
RecName: Full=Endoplasmin homolog;
AltName: Full=Glucose-regulated protein 94 homolog;
Short=GRP-94 homolog;
Flags: Precursor;
Name=HSP90;
Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; lamiids; Gentianales; Apocynaceae;
Rauvolfioideae; Vinceae; Catharanthinae; Catharanthus.
NCBI_TaxID=4058;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. CP3A;
PubMed=8106014; DOI=10.1007/BF00019305;
Schroeder G., Beck M., Eichel J., Vetter H.P., Schroeder J.;
"HSP90 homologue from Madagascar periwinkle (Catharanthus roseus):
cDNA sequence, regulation of protein expression and location in the
endoplasmic reticulum.";
Plant Mol. Biol. 23:583-594(1993).
-!- FUNCTION: May have a molecular chaperone role in the processing of
secreted materials.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
-!- TISSUE SPECIFICITY: Not detected in extracts from young plants
unless they are exposed to heat shock for several hours. Found to
be constitutively expressed in cell cultures.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
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EMBL; L14594; AAA16785.1; -; mRNA.
PIR; S39558; S39558.
ProteinModelPortal; P35016; -.
SMR; P35016; -.
PRIDE; P35016; -.
GO; GO:0005788; C:endoplasmic reticulum lumen; 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:0006950; P:response to stress; IEA:InterPro.
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; 1.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00298; HSP90; 1.
2: Evidence at transcript level;
ATP-binding; Calcium; Chaperone; Endoplasmic reticulum; Glycoprotein;
Nucleotide-binding; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 817 Endoplasmin homolog.
/FTId=PRO_0000013602.
MOTIF 814 817 Prevents secretion from ER.
BINDING 111 111 ATP. {ECO:0000250}.
BINDING 155 155 ATP. {ECO:0000250}.
BINDING 168 168 ATP. {ECO:0000250}.
BINDING 174 174 ATP. {ECO:0000250}.
BINDING 200 200 ATP; via amide nitrogen. {ECO:0000250}.
BINDING 459 459 ATP. {ECO:0000250}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 416 416 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 456 456 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 624 624 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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