ID M1AWJ2_SOLTU Unreviewed; 667 AA.
AC M1AWJ2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Luminal-binding protein {ECO:0000313|EnsemblPlants:PGSC0003DMT400031937};
GN Name=102598457 {ECO:0000313|EnsemblPlants:PGSC0003DMT400031937};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400031937, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400031937}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400031937};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Probably plays a role in facilitating the assembly of
CC multimeric protein complexes inside the ER.
CC {ECO:0000256|ARBA:ARBA00003955}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_006343810.1; XM_006343748.2.
DR AlphaFoldDB; M1AWJ2; -.
DR SMR; M1AWJ2; -.
DR STRING; 4113.M1AWJ2; -.
DR PaxDb; 4113-PGSC0003DMT400031937; -.
DR EnsemblPlants; PGSC0003DMT400031937; PGSC0003DMT400031937; PGSC0003DMG400012254.
DR GeneID; 102598457; -.
DR Gramene; PGSC0003DMT400031937; PGSC0003DMT400031937; PGSC0003DMG400012254.
DR KEGG; sot:102598457; -.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_7_2_1; -.
DR InParanoid; M1AWJ2; -.
DR OMA; AWNRRTS; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1AWJ2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR CDD; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042050; BIP_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR45639:SF4; HSC70CB, ISOFORM G; 1.
DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..667
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004011715"
FT REGION 643..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 285..312
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 547..623
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 667 AA; 73463 MW; B5A85E22814381DB CRC64;
MAGCLRRGNS LVVLTIVLLG CLSALSTAKE EATKLGTVIG IDLGTTYSCV GVYKNGHVEI
IANDQGNRIT PSWVAFTDNE RLIGEAAKNL AAVNPERTIF DVKRLIGRKF EDKEVQRDMK
LVPYKIISKD GKPYIQVKIK DGEVKVFSPE EISAMILTKM KETAEAFLGK TIKDAVVTVP
AYFNDAQRQA TKDAGVIAGL NVARIINEPT AAAIAYGLDK KDGEKNILVF DLGGGTFDVS
ILTIDNGVFE VLATNGDTHL GGEDFDQRIM EYFIKLIKKK HGKDISKDNR ALSKLRREAE
RAKRSLSSQH QVRVEIESLF DGTDFSEPLT RARFEELNND LFRKTMGPVK KAMDDAGLQK
NQIDEIVLVG GSTRIPKVQQ LLKDYFDGKE PSKGVNPDEA VAYGAAVQGG ILSGEGGDET
KDILLLDVAP LTLGIETVGG VMTKLIPRNT VIPTKKSQVF TTYQDQQTTV SIQVFEGERS
LTKDCRNLGK FDLTGIPPAP RGTPQIEVTF EVDANGILNV KAEDKGTGKA EKITITNDKG
RLSQEEIERM VREAEEFAEE DKKVKEKIDA RNALETYVYN MKNQINDKDK LADKLESDEK
EKIETATKEA LEWLDDNQSA EKEDYDEKLK EVEAVCNPII TAVYQRSGGS PGGGASEEED
DDSHDEL
//
