ENPL_CHICK
ID ENPL_CHICK Reviewed; 795 AA.
AC P08110; Q90869; Q90870;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Endoplasmin;
DE AltName: Full=Heat shock 108 kDa protein;
DE Short=HSP 108;
DE Short=HSP108;
DE AltName: Full=Heat shock protein 90 kDa beta member 1;
DE AltName: Full=Transferrin-binding protein;
DE Flags: Precursor;
GN Name=HSP90B1; Synonyms=TRA1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3024703; DOI=10.1021/bi00368a061;
RA Kulomaa M.S., Weigel N.L., Kleinsek D.A., Beattie W.G., Conneely O.M.,
RA March C., Zarucki-Schulz T., Schrader W.T., O'Malley B.W.;
RT "Amino acid sequence of a chicken heat shock protein derived from the
RT complementary DNA nucleotide sequence.";
RL Biochemistry 25:6244-6251(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Oviduct;
RX PubMed=3027654; DOI=10.1093/nar/14.24.10053;
RA Kleinsek D.A., Beattie W.G., Tsai M.J., O'Malley B.W.;
RT "Molecular cloning of a steroid-regulated 108K heat shock protein gene from
RT hen oviduct.";
RL Nucleic Acids Res. 14:10053-10069(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Oviduct;
RA Forsgren M.;
RL Submitted (SEP-1987) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT
RP ASN-216.
RX PubMed=8166742; DOI=10.1006/bbrc.1994.1414;
RA Hayes G.R., Himpler B.S., Weiner K.X.B., Lucas J.J.;
RT "A chicken transferrin binding protein is heat shock protein 108.";
RL Biochem. Biophys. Res. Commun. 200:65-70(1994).
CC -!- FUNCTION: Molecular chaperone that functions in the processing and
CC transport of secreted proteins (By similarity). Has ATPase activity (By
CC similarity). {ECO:0000250|UniProtKB:P08113}.
CC -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q66HD0}. Sarcoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P41148}. Melanosome
CC {ECO:0000250|UniProtKB:P14625}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; M14772; AAA48826.1; -; mRNA.
DR EMBL; M31321; AAA48827.1; -; Genomic_DNA.
DR EMBL; X04961; CAA28629.1; -; Genomic_DNA.
DR PIR; A24461; HHCH08.
DR PIR; I50255; I50255.
DR RefSeq; NP_989620.1; NM_204289.1.
DR AlphaFoldDB; P08110; -.
DR SMR; P08110; -.
DR BioGRID; 675192; 2.
DR IntAct; P08110; 1.
DR STRING; 9031.ENSGALP00000020744; -.
DR iPTMnet; P08110; -.
DR PaxDb; P08110; -.
DR GeneID; 374163; -.
DR KEGG; gga:374163; -.
DR CTD; 7184; -.
DR VEuPathDB; HostDB:geneid_374163; -.
DR eggNOG; KOG0020; Eukaryota.
DR InParanoid; P08110; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; P08110; -.
DR PRO; PR:P08110; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:AgBase.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR GO; GO:0033018; C:sarcoplasmic 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; IBA:GO_Central.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; TAS:AgBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Calcium; Chaperone; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Nucleotide-binding;
KW Reference proteome; Sarcoplasmic reticulum; Signal; Stress response.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..795
FT /note="Endoplasmin"
FT /id="PRO_0000013601"
FT REGION 289..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 792..795
FT /note="Prevents secretion from ER"
FT COMPBIAS 289..313
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..781
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT SITE 447
FT /note="Important for ATP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8166742"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 137
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 206
FT /note="D -> E (in Ref. 2; AAA48827 and 3; CAA28629)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="V -> L (in Ref. 2; AAA48827)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="E -> Q (in Ref. 2; AAA48827)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="N -> D (in Ref. 2; AAA48827 and 3; CAA28629)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="E -> H (in Ref. 2; AAA48827)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="G -> A (in Ref. 2; AAA48827)"
FT /evidence="ECO:0000305"
FT CONFLICT 593..594
FT /note="EG -> DR (in Ref. 2; AAA48827)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="W -> C (in Ref. 2; AAA48827)"
FT /evidence="ECO:0000305"
FT CONFLICT 669..675
FT /note="GKDISTN -> VFSS (in Ref. 3; CAA28629)"
FT /evidence="ECO:0000305"
SQ 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
