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Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1)

 ENPL_CANLF              Reviewed;         804 AA.
P41148;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
18-JUL-2018, entry version 155.
RecName: Full=Endoplasmin;
AltName: Full=94 kDa glucose-regulated protein;
Short=GRP-94;
AltName: Full=Heat shock protein 90 kDa beta member 1;
Flags: Precursor;
Name=HSP90B1; Synonyms=GRP94, TRA1;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
PHOSPHORYLATION.
TISSUE=Heart;
PubMed=8119936;
Cala S.E., Jones L.R.;
"GRP94 resides within cardiac sarcoplasmic reticulum vesicles and is
phosphorylated by casein kinase II.";
J. Biol. Chem. 269:5926-5931(1994).
[2]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 69-337 IN COMPLEX WITH
ADENOSINE ANALOG.
PubMed=12970348; DOI=10.1074/jbc.M308661200;
Soldano K.L., Jivan A., Nicchitta C.V., Gewirth D.T.;
"Structure of the N-terminal domain of GRP94. Basis for ligand
specificity and regulation.";
J. Biol. Chem. 278:48330-48338(2003).
[3]
X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 69-337 IN COMPLEXES WITH
ATP; ADP AND AMP, AND SUBUNIT.
PubMed=15292259; DOI=10.1074/jbc.M405253200;
Immormino R.M., Dollins D.E., Shaffer P.L., Soldano K.L., Walker M.A.,
Gewirth D.T.;
"Ligand-induced conformational shift in the N-terminal domain of
GRP94, an Hsp90 chaperone.";
J. Biol. Chem. 279:46162-46171(2004).
[4]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 69-337 OF APOPROTEIN AND IN
COMPLEXES WITH ADP AND NECA.
PubMed=15951571; DOI=10.1074/jbc.M503761200;
Dollins D.E., Immormino R.M., Gewirth D.T.;
"Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis
for nucleotide-induced conformational change.";
J. Biol. Chem. 280:30438-30447(2005).
[5]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 73-754 IN COMPLEXES WITH
AMPPNP AND ADP, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
GLU-103 AND ARG-448, AND CATALYTIC ACTIVITY.
PubMed=17936703; DOI=10.1016/j.molcel.2007.08.024;
Dollins D.E., Warren J.J., Immormino R.M., Gewirth D.T.;
"Structures of GRP94-nucleotide complexes reveal mechanistic
differences between the hsp90 chaperones.";
Mol. Cell 28:41-56(2007).
-!- FUNCTION: Molecular chaperone that functions in the processing and
transport of secreted proteins. When associated with CNPY3,
required for proper folding of Toll-like receptors. Functions in
endoplasmic reticulum associated degradation (ERAD). Has ATPase
activity (By similarity). {ECO:0000250}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=10 uM for ATP {ECO:0000269|PubMed:17936703};
-!- SUBUNIT: Homodimer; disulfide-linked. Component of an EIF2 complex
at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2,
HSP90B1 and HSPA5 (By similarity). Part of a large chaperone
multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU,
PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts
of ERP29, but not, or at very low levels, CALR nor CANX. Interacts
with AIMP1; regulates its retention in the endoplasmic reticulum.
Interacts with OS9 (By similarity). Interacts with CNPY3; this
interaction is disrupted in the presence of ATP. Interacts with
several TLRs, including TLR4 and TLR9, but not with TLR3 (By
similarity). Interacts with MZB1 in a calcium-dependent manner (By
similarity). Interacts with METTL23 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Sarcoplasmic
reticulum. Melanosome {ECO:0000250}.
-!- PTM: Phosphorylated by CK2. {ECO:0000269|PubMed:8119936}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
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EMBL; U01153; AAA17708.1; -; mRNA.
PIR; A53211; A53211.
RefSeq; NP_001003327.1; NM_001003327.2.
UniGene; Cfa.3896; -.
PDB; 1QY8; X-ray; 1.85 A; A=69-337.
PDB; 1QYE; X-ray; 2.10 A; A=69-337.
PDB; 1TBW; X-ray; 2.15 A; A/B=69-286, A/B=328-337.
PDB; 1TC0; X-ray; 2.20 A; A/B=69-286, A/B=328-337.
PDB; 1TC6; X-ray; 1.87 A; A/B=69-286, A/B=328-337.
PDB; 1U0Z; X-ray; 1.90 A; A/B=69-286, A/B=328-337.
PDB; 1U2O; X-ray; 2.10 A; A/B=69-286, A/B=328-337.
PDB; 1YSZ; X-ray; 2.65 A; A=69-286, A=328-337.
PDB; 1YT0; X-ray; 2.40 A; A=69-286, A=328-337.
PDB; 1YT1; X-ray; 2.20 A; A/B=69-286, A/B=328-337.
PDB; 1YT2; X-ray; 3.25 A; A=69-337.
PDB; 2ESA; X-ray; 1.90 A; A=69-286, A=328-337.
PDB; 2EXL; X-ray; 2.35 A; A/B=69-286, A/B=328-337.
PDB; 2FYP; X-ray; 1.95 A; A/B=69-286, A/B=328-337.
PDB; 2GFD; X-ray; 2.30 A; A/B=69-286, A/B=328-337.
PDB; 2GQP; X-ray; 1.50 A; A/B=69-286, A/B=328-337.
PDB; 2H8M; X-ray; 1.80 A; A/B=69-286, A/B=328-337.
PDB; 2HCH; X-ray; 2.30 A; A/B=69-286, A/B=328-337.
PDB; 2HG1; X-ray; 2.30 A; A/B=69-286.
PDB; 2O1T; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J=336-765.
PDB; 2O1U; X-ray; 2.40 A; A/B=73-286, A/B=328-754.
PDB; 2O1V; X-ray; 2.45 A; A/B=73-286, A/B=328-754.
PDB; 2O1W; X-ray; 3.40 A; A/B/C/D/E=73-286, A/B/C/D/E=328-594.
PDB; 3O2F; X-ray; 2.00 A; A/B=69-286, A/B=328-337.
PDB; 5IN9; X-ray; 2.60 A; A/B=69-286, A/B=328-337.
PDB; 5TTZ; X-ray; 2.71 A; A/B=69-286.
PDB; 5ULS; X-ray; 2.62 A; A/B=48-286, A/B=328-754.
PDB; 5WMT; X-ray; 2.75 A; A/B/C/D=69-286.
PDB; 6AOL; X-ray; 2.76 A; A=69-286.
PDB; 6AOM; X-ray; 2.87 A; A/B=69-286.
PDB; 6ASP; X-ray; 2.70 A; A/B=69-286.
PDB; 6ASQ; X-ray; 2.35 A; A/B=69-286.
PDB; 6BAW; X-ray; 2.70 A; A/B/C/D=69-286.
PDB; 6C91; X-ray; 2.90 A; B/C=69-286.
PDB; 6D1X; X-ray; 2.30 A; A=69-337.
PDB; 6D28; X-ray; 1.75 A; A=69-337.
PDBsum; 1QY8; -.
PDBsum; 1QYE; -.
PDBsum; 1TBW; -.
PDBsum; 1TC0; -.
PDBsum; 1TC6; -.
PDBsum; 1U0Z; -.
PDBsum; 1U2O; -.
PDBsum; 1YSZ; -.
PDBsum; 1YT0; -.
PDBsum; 1YT1; -.
PDBsum; 1YT2; -.
PDBsum; 2ESA; -.
PDBsum; 2EXL; -.
PDBsum; 2FYP; -.
PDBsum; 2GFD; -.
PDBsum; 2GQP; -.
PDBsum; 2H8M; -.
PDBsum; 2HCH; -.
PDBsum; 2HG1; -.
PDBsum; 2O1T; -.
PDBsum; 2O1U; -.
PDBsum; 2O1V; -.
PDBsum; 2O1W; -.
PDBsum; 3O2F; -.
PDBsum; 5IN9; -.
PDBsum; 5TTZ; -.
PDBsum; 5ULS; -.
PDBsum; 5WMT; -.
PDBsum; 6AOL; -.
PDBsum; 6AOM; -.
PDBsum; 6ASP; -.
PDBsum; 6ASQ; -.
PDBsum; 6BAW; -.
PDBsum; 6C91; -.
PDBsum; 6D1X; -.
PDBsum; 6D28; -.
ProteinModelPortal; P41148; -.
SMR; P41148; -.
STRING; 9615.ENSCAFP00000011044; -.
BindingDB; P41148; -.
ChEMBL; CHEMBL4748; -.
PaxDb; P41148; -.
PRIDE; P41148; -.
GeneID; 404019; -.
KEGG; cfa:404019; -.
CTD; 7184; -.
eggNOG; KOG0020; Eukaryota.
eggNOG; COG0326; LUCA.
HOGENOM; HOG000031988; -.
HOVERGEN; HBG007374; -.
InParanoid; P41148; -.
KO; K09487; -.
EvolutionaryTrace; P41148; -.
PRO; PR:P41148; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016529; C:sarcoplasmic reticulum; 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:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
CDD; cd00075; HATPase_c; 1.
Gene3D; 1.20.120.790; -; 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; 2.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00298; HSP90; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Calcium; Chaperone;
Complete proteome; Direct protein sequencing; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Nucleotide-binding;
Phosphoprotein; Reference proteome; Sarcoplasmic reticulum; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 804 Endoplasmin.
/FTId=PRO_0000013597.
MOTIF 801 804 Prevents secretion from ER.
{ECO:0000255}.
BINDING 107 107 ATP.
BINDING 149 149 ATP.
BINDING 162 162 ATP.
BINDING 168 168 ATP. {ECO:0000250}.
BINDING 199 199 ATP; via amide nitrogen.
BINDING 448 448 ATP. {ECO:0000250}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000250|UniProtKB:P14625}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000250|UniProtKB:Q66HD0}.
MOD_RES 288 288 Phosphothreonine; by CK2. {ECO:0000255}.
MOD_RES 306 306 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P14625,
ECO:0000255}.
MOD_RES 403 403 Phosphoserine.
{ECO:0000250|UniProtKB:Q66HD0}.
MOD_RES 404 404 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08113}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000250|UniProtKB:P14625}.
MOD_RES 479 479 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08113}.
MOD_RES 633 633 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08113}.
MOD_RES 766 766 Phosphothreonine; by CK2. {ECO:0000255}.
MOD_RES 770 770 Phosphothreonine; by CK2. {ECO:0000255}.
MOD_RES 774 774 Phosphothreonine; by CK2. {ECO:0000255}.
MOD_RES 786 786 Phosphothreonine; by CK2.
{ECO:0000250|UniProtKB:P14625,
ECO:0000255}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 217 217 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 445 445 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 481 481 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 502 502 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 138 138 Interchain. {ECO:0000250}.
MUTAGEN 103 103 E->A: Loss of ATPase activity.
{ECO:0000269|PubMed:17936703}.
MUTAGEN 448 448 R->A: Reduces ATPase activity by 85%.
{ECO:0000269|PubMed:17936703}.
TURN 72 74 {ECO:0000244|PDB:2GQP}.
STRAND 75 77 {ECO:0000244|PDB:5ULS}.
HELIX 80 92 {ECO:0000244|PDB:2GQP}.
TURN 93 95 {ECO:0000244|PDB:2GQP}.
HELIX 99 121 {ECO:0000244|PDB:2GQP}.
TURN 123 128 {ECO:0000244|PDB:2GQP}.
STRAND 134 139 {ECO:0000244|PDB:2GQP}.
TURN 140 143 {ECO:0000244|PDB:2GQP}.
STRAND 144 149 {ECO:0000244|PDB:2GQP}.
HELIX 156 164 {ECO:0000244|PDB:2GQP}.
HELIX 169 184 {ECO:0000244|PDB:6D28}.
HELIX 189 194 {ECO:0000244|PDB:2GQP}.
HELIX 198 204 {ECO:0000244|PDB:2GQP}.
STRAND 206 214 {ECO:0000244|PDB:2GQP}.
STRAND 216 218 {ECO:0000244|PDB:2O1V}.
STRAND 221 228 {ECO:0000244|PDB:2GQP}.
STRAND 230 234 {ECO:0000244|PDB:2GQP}.
STRAND 241 251 {ECO:0000244|PDB:2GQP}.
HELIX 253 259 {ECO:0000244|PDB:2GQP}.
HELIX 261 272 {ECO:0000244|PDB:2GQP}.
STRAND 273 277 {ECO:0000244|PDB:5ULS}.
STRAND 279 284 {ECO:0000244|PDB:2GQP}.
STRAND 331 337 {ECO:0000244|PDB:6D28}.
TURN 342 344 {ECO:0000244|PDB:2O1U}.
TURN 347 349 {ECO:0000244|PDB:2O1U}.
HELIX 352 361 {ECO:0000244|PDB:2O1U}.
STRAND 370 377 {ECO:0000244|PDB:2O1U}.
STRAND 379 381 {ECO:0000244|PDB:2O1U}.
STRAND 383 389 {ECO:0000244|PDB:2O1U}.
TURN 395 403 {ECO:0000244|PDB:5ULS}.
STRAND 409 413 {ECO:0000244|PDB:2O1U}.
STRAND 416 420 {ECO:0000244|PDB:2O1U}.
TURN 423 425 {ECO:0000244|PDB:5ULS}.
HELIX 428 430 {ECO:0000244|PDB:2O1U}.
STRAND 434 442 {ECO:0000244|PDB:2O1U}.
STRAND 444 446 {ECO:0000244|PDB:2O1U}.
HELIX 448 452 {ECO:0000244|PDB:2O1U}.
HELIX 455 474 {ECO:0000244|PDB:2O1U}.
HELIX 477 482 {ECO:0000244|PDB:2O1U}.
HELIX 484 498 {ECO:0000244|PDB:2O1U}.
HELIX 500 502 {ECO:0000244|PDB:2O1U}.
HELIX 503 507 {ECO:0000244|PDB:2O1U}.
STRAND 512 514 {ECO:0000244|PDB:2O1U}.
STRAND 517 519 {ECO:0000244|PDB:2O1U}.
STRAND 521 523 {ECO:0000244|PDB:5ULS}.
HELIX 524 530 {ECO:0000244|PDB:2O1U}.
STRAND 537 542 {ECO:0000244|PDB:2O1U}.
HELIX 546 550 {ECO:0000244|PDB:2O1U}.
HELIX 553 555 {ECO:0000244|PDB:2O1U}.
HELIX 556 560 {ECO:0000244|PDB:2O1U}.
STRAND 566 568 {ECO:0000244|PDB:2O1U}.
HELIX 572 578 {ECO:0000244|PDB:2O1U}.
STRAND 586 590 {ECO:0000244|PDB:2O1U}.
HELIX 602 614 {ECO:0000244|PDB:2O1U}.
HELIX 616 624 {ECO:0000244|PDB:2O1U}.
TURN 625 630 {ECO:0000244|PDB:2O1U}.
STRAND 631 636 {ECO:0000244|PDB:2O1U}.
STRAND 644 649 {ECO:0000244|PDB:2O1U}.
HELIX 656 668 {ECO:0000244|PDB:2O1U}.
HELIX 670 673 {ECO:0000244|PDB:5ULS}.
STRAND 677 680 {ECO:0000244|PDB:2O1U}.
STRAND 683 687 {ECO:0000244|PDB:2O1U}.
STRAND 689 691 {ECO:0000244|PDB:5ULS}.
HELIX 692 703 {ECO:0000244|PDB:2O1U}.
HELIX 708 725 {ECO:0000244|PDB:2O1U}.
HELIX 732 744 {ECO:0000244|PDB:2O1U}.
TURN 751 757 {ECO:0000244|PDB:2O1T}.
HELIX 758 760 {ECO:0000244|PDB:2O1T}.
HELIX 762 764 {ECO:0000244|PDB:2O1T}.
SEQUENCE 804 AA; 92514 MW; 36AA126EDCFFC2D5 CRC64;
MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ REEEAIQLDG
LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF LRELISNASD ALDKIRLISL
TDENALAGNE ELTVKIKCDK EKNLLHVTDT GVGMTREELV KNLGTIAKSG TSEFLNKMTE
AQEDGQSTSE LIGQFGVGFY SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT
LGRGTTITLV LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK
EEKEDSDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV EDDEYKAFYK
SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD
DFHDMMPKYL NFVKGVVDSD DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADEKY
NDTFWKEFGT NIKLGVIEDH SNRTRLAKLL RFQSSHHPSD ITSLDQYVER MKEKQDKIYF
MAGSSRKEAE SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
SEKTKESREA IEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS QYGWSGNMER
IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIKDMLRR VKEDEDDKTV SDLAVVLFET
ATLRSGYLLP DTKAYGDRIE RMLRLSLNID PDAKVEEEPE EEPEETTEDT TEDTEQDDEE
EMDAGTDDEE QETVKKSTAE KDEL


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E0823c ELISA Chicken,Endoplasmin,Gallus gallus,Heat shock 108 kDa protein,Heat shock protein 90 kDa beta member 1,HSP 108,HSP108,HSP90B1,TRA1,Transferrin-binding protein 96T
E0823c ELISA kit Chicken,Endoplasmin,Gallus gallus,Heat shock 108 kDa protein,Heat shock protein 90 kDa beta member 1,HSP 108,HSP108,HSP90B1,TRA1,Transferrin-binding protein 96T
U0823c CLIA Chicken,Endoplasmin,Gallus gallus,Heat shock 108 kDa protein,Heat shock protein 90 kDa beta member 1,HSP 108,HSP108,HSP90B1,TRA1,Transferrin-binding protein 96T


 

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