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Endoplasmin homolog (92 kDa phosphoprotein) (Glucose-regulated protein 94 homolog) (GRP-94 homolog)

 ENPL_DICDI              Reviewed;         768 AA.
Q9NKX1; Q54VP2;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
29-APR-2008, sequence version 2.
31-JAN-2018, entry version 101.
RecName: Full=Endoplasmin homolog;
AltName: Full=92 kDa phosphoprotein;
AltName: Full=Glucose-regulated protein 94 homolog;
Short=GRP-94 homolog;
Flags: Precursor;
Name=grp94; ORFNames=DDB_G0280057;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliaceae;
Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=10913338; DOI=10.1006/bbrc.2000.3096;
Morita T., Saitoh K., Takagi T., Maeda Y.;
"Involvement of the glucose-regulated protein 94 (Dd-GRP94) in
starvation response of Dictyostelium discoideum cells.";
Biochem. Biophys. Res. Commun. 274:323-331(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[3]
SUBCELLULAR LOCATION.
PubMed=15652353; DOI=10.1016/j.yexcr.2004.10.005;
Yamaguchi H., Morita T., Amagai A., Maeda Y.;
"Changes in spatial and temporal localization of Dictyostelium
homologues of TRAP1 and GRP94 revealed by immunoelectron microscopy.";
Exp. Cell Res. 303:415-424(2005).
-!- FUNCTION: May play a role in late differentiation as well as in
starvation response. When overexpressed, suppresses the ability to
form normal fruiting bodies and impairs prespore differentiation
as well as maturation into spores.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Golgi apparatus.
Note=In prespore cells, preferentially localizes in Golgi vesicles
and cisternae. Colocalizes with trap1 in the prespore-specific
vacuole.
-!- INDUCTION: Expression is greatly reduced following starvation.
-!- PTM: Phosphorylated. {ECO:0000305}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB040814; BAA94290.2; -; mRNA.
EMBL; AAFI02000035; EAL67255.1; -; Genomic_DNA.
PIR; JC7352; JC7352.
RefSeq; XP_641313.1; XM_636221.1.
ProteinModelPortal; Q9NKX1; -.
SMR; Q9NKX1; -.
STRING; 44689.DDB0215015; -.
PaxDb; Q9NKX1; -.
PRIDE; Q9NKX1; -.
EnsemblProtists; EAL67255; EAL67255; DDB_G0280057.
GeneID; 8622445; -.
KEGG; ddi:DDB_G0280057; -.
dictyBase; DDB_G0280057; grp94.
eggNOG; KOG0020; Eukaryota.
eggNOG; COG0326; LUCA.
InParanoid; Q9NKX1; -.
KO; K09487; -.
PhylomeDB; Q9NKX1; -.
PRO; PR:Q9NKX1; -.
Proteomes; UP000002195; Chromosome 3.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005798; C:Golgi-associated vesicle; IDA:dictyBase.
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; 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.
2: Evidence at transcript level;
ATP-binding; Calcium; Chaperone; Complete proteome;
Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
Nucleotide-binding; Phosphoprotein; Reference proteome; Signal.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 768 Endoplasmin homolog.
/FTId=PRO_0000327690.
MOTIF 765 768 Prevents secretion from ER.
{ECO:0000255}.
COMPBIAS 260 315 Glu-rich.
COMPBIAS 283 287 Poly-Thr.
BINDING 83 83 ATP. {ECO:0000250}.
BINDING 127 127 ATP. {ECO:0000250}.
BINDING 140 140 ATP. {ECO:0000250}.
BINDING 173 173 ATP; via amide nitrogen. {ECO:0000250}.
BINDING 426 426 ATP. {ECO:0000250}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 309 309 T -> I (in Ref. 1; BAA94290).
{ECO:0000305}.
CONFLICT 444 445 LV -> G (in Ref. 2; EAL67255).
{ECO:0000305}.
SEQUENCE 768 AA; 87269 MW; 7EB40FDDC56059E0 CRC64;
MKSITKIFLI LGLFAFLLVA FAPSSSVATV NLESDGYTEA EAKLIEEKGE KFTFQTEVNK
LMNIIINSLY SKKEIFLREL ISNASDALDK IRFLALTNAD LLGEGEQSNL DIHIKIDKAN
NVLHITDRGV GMTKDELVRN LGTIAQSGTK EFIKKVSDSA ESSNLIGQFG VGFYSLFLVA
DSVVVTSKSN DDDQYVWTSD SQSSYTIAKD PKGNTLGRGT RISLHIKDDS KEFLDQEVIK
QLVKKYSQFI NFPIYLYVSE EVEIPKEEQE DSKPITDDQV EETTTTTEEG EEETTTEEEG
QTEEKKTKTV YKWEELNDSK PLWMKAAKDV TKEEYTEFFR SLSKTQDTPI TYSHFKTEGD
TEFRSILYIP ENPPSNMFDL EAAGSGLKLF VRRVFITDNL KELVPNWLRF LVGVIDSDDL
PLNVSREMLQ QNKILDAIKK KVILVKFISM IKELSEDEDK TKYNEFFKKF GSSMKLGAIE
DQANKKRLTK YLLFPSSKEE LTTFAGYVER MKEGQDQIYF ITGKSKDSVE ASPLIEQAIK
KGYEVLFLVD PIDEYLVPQL DKFDDKYKFT NLARSGVKFN EDKEEEDQRK QTAEEFKPLL
SYLKKTLSDK LEKVVISKVL ADSPSILVSN SWGVTANQER IMKAQAHQAN AQPQFNSKKI
MEINPSHPLI KKLLNRLNEF GEEDETTKVS AHVLYETSAL TAGYSIDNPT NFADFIYKLM
MINGDSLAQT NFETTKNENS GPSVSFGDDD ENQQQDFQQP PQSTHDEL


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