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Endoplasmin (Heat shock 108 kDa protein) (HSP 108) (HSP108) (Heat shock protein 90 kDa beta member 1) (Transferrin-binding protein)

 ENPL_CHICK              Reviewed;         795 AA.
P08110; Q90869; Q90870;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
28-MAR-2018, entry version 139.
RecName: Full=Endoplasmin;
AltName: Full=Heat shock 108 kDa protein;
Short=HSP 108;
Short=HSP108;
AltName: Full=Heat shock protein 90 kDa beta member 1;
AltName: Full=Transferrin-binding protein;
Flags: Precursor;
Name=HSP90B1; Synonyms=TRA1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3024703; DOI=10.1021/bi00368a061;
Kulomaa M.S., Weigel N.L., Kleinsek D.A., Beattie W.G., Conneely O.M.,
March C., Zarucki-Schulz T., Schrader W.T., O'Malley B.W.;
"Amino acid sequence of a chicken heat shock protein derived from the
complementary DNA nucleotide sequence.";
Biochemistry 25:6244-6251(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Oviduct;
PubMed=3027654; DOI=10.1093/nar/14.24.10053;
Kleinsek D.A., Beattie W.G., Tsai M.J., O'Malley B.W.;
"Molecular cloning of a steroid-regulated 108K heat shock protein gene
from hen oviduct.";
Nucleic Acids Res. 14:10053-10069(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Oviduct;
Forsgren M.;
Submitted (SEP-1987) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
GLYCOSYLATION AT ASN-216.
PubMed=8166742; DOI=10.1006/bbrc.1994.1414;
Hayes G.R., Himpler B.S., Weiner K.X.B., Lucas J.J.;
"A chicken transferrin binding protein is heat shock protein 108.";
Biochem. Biophys. Res. Commun. 200:65-70(1994).
-!- FUNCTION: Molecular chaperone that functions in the processing and
transport of secreted proteins. Has ATPase activity (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer; disulfide-linked.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
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EMBL; M14772; AAA48826.1; -; mRNA.
EMBL; M31321; AAA48827.1; -; Genomic_DNA.
EMBL; X04961; CAA28629.1; -; Genomic_DNA.
PIR; A24461; HHCH08.
PIR; I50255; I50255.
RefSeq; NP_989620.1; NM_204289.1.
UniGene; Gga.4724; -.
ProteinModelPortal; P08110; -.
SMR; P08110; -.
BioGrid; 675192; 1.
IntAct; P08110; 1.
STRING; 9031.ENSGALP00000020744; -.
iPTMnet; P08110; -.
PaxDb; P08110; -.
PRIDE; P08110; -.
GeneID; 374163; -.
KEGG; gga:374163; -.
CTD; 7184; -.
eggNOG; KOG0020; Eukaryota.
eggNOG; COG0326; LUCA.
HOGENOM; HOG000031988; -.
HOVERGEN; HBG007374; -.
InParanoid; P08110; -.
KO; K09487; -.
PhylomeDB; P08110; -.
PRO; PR:P08110; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005783; C:endoplasmic reticulum; ISS:AgBase.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0006880; P:intracellular sequestering of iron ion; TAS:AgBase.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0006950; P:response to stress; IEA:InterPro.
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;
ATP-binding; Calcium; Chaperone; Complete proteome;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Nucleotide-binding; Reference proteome; Signal;
Stress response.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 795 Endoplasmin.
/FTId=PRO_0000013601.
MOTIF 792 795 Prevents secretion from ER.
BINDING 106 106 ATP. {ECO:0000250}.
BINDING 148 148 ATP. {ECO:0000250}.
BINDING 161 161 ATP. {ECO:0000250}.
BINDING 167 167 ATP. {ECO:0000250}.
BINDING 198 198 ATP; via amide nitrogen. {ECO:0000250}.
BINDING 447 447 ATP. {ECO:0000250}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 216 216 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8166742}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 480 480 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 501 501 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 137 137 Interchain. {ECO:0000250}.
CONFLICT 206 206 D -> E (in Ref. 2; AAA48827 and 3;
CAA28629). {ECO:0000305}.
CONFLICT 267 267 V -> L (in Ref. 2; AAA48827).
{ECO:0000305}.
CONFLICT 303 303 E -> Q (in Ref. 2; AAA48827).
{ECO:0000305}.
CONFLICT 307 307 N -> D (in Ref. 2; AAA48827 and 3;
CAA28629). {ECO:0000305}.
CONFLICT 317 317 E -> H (in Ref. 2; AAA48827).
{ECO:0000305}.
CONFLICT 378 378 G -> A (in Ref. 2; AAA48827).
{ECO:0000305}.
CONFLICT 593 594 EG -> DR (in Ref. 2; AAA48827).
{ECO:0000305}.
CONFLICT 653 653 W -> C (in Ref. 2; AAA48827).
{ECO:0000305}.
CONFLICT 669 675 GKDISTN -> VFSS (in Ref. 3; CAA28629).
{ECO:0000305}.
SEQUENCE 795 AA; 91555 MW; BE1B29E1DBEC5A9A CRC64;
MKSAWALALA CTLLLAASVT AEEVDVDATV EEDLGKSREG SRTDDEVVQR EEEAIQLDGL
NASQIKEIRE KSEKFAFQAE VNRMMKLIIN SLYKNKEIFL RELISNASDA LDKIRLISLT
DENALAGNEE LTVKIKCDKE KNMLHVTDTG IGMTKEELIK NLGTIAKSGT SEFLNKMTEM
QDDSQSTSEL IGQFGVGFYS AFLVADRVIV TSKHNNDTQH IWESDSNEFS VIDDPRGNTL
GRGTTITLVL KEEASDYLEL DTVKNLVKKY SQFINFPIYV WSSKTETVEE PVEEEEAKEE
KEETDDNEAA VEEEEEEKKP KTKKVEKTVW DWELMNDIKP IWQRPSKEVE EDEYKAFYKT
FSKEHDDPMA YIHFTAEGEV TFKSILFVPN SAPRGLFDEY GSKKSDFIKL YVRRVFITDD
FHDMMPKYLN FVKGVVDSDD LPLNVSRETL QQHKLLKVIR KKLVRKTLDM IKKIAEEKYN
DTFWKEFGTN VKLGVIEDHS NRTRLAKLLR FQSSHHESNL TSLDQYVERM KEKQDKIYFM
AGASRKEAES SPFVERLLKK GYEVIYLTEP VDEYCIQALP EFDGKRFQNV AKEGVKFEES
EKSKESREAL EKEFEPLLNW MKDKALKDKI EKAVLSQRLT QSPCALVASQ YGWSGNMERI
MKAQAYQTGK DISTNYYASQ KKTFEINPRH PLIKDMLRRV KENEDDKTVS DLAVVLFETA
TLRSGYMLPD TKEYGDRIER MLRLSLNIDL DAKVEEEPEE PEDAAEEAEQ DEEEVDADAE
DSETQKESTD VKDEL


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