ID A0A384B529_BALAS Unreviewed; 655 AA.
AC A0A384B529;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=78 kDa glucose-regulated protein {ECO:0000256|ARBA:ARBA00029695};
DE AltName: Full=Binding-immunoglobulin protein {ECO:0000256|ARBA:ARBA00031291};
DE AltName: Full=Heat shock protein 70 family protein 5 {ECO:0000256|ARBA:ARBA00031035};
DE AltName: Full=Heat shock protein family A member 5 {ECO:0000256|ARBA:ARBA00030223};
DE AltName: Full=Immunoglobulin heavy chain-binding protein {ECO:0000256|ARBA:ARBA00033037};
GN Name=HSPA5 {ECO:0000313|RefSeq:XP_007194740.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007194740.1};
RN [1] {ECO:0000313|RefSeq:XP_007194740.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007194740.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR RefSeq; XP_007194739.1; XM_007194677.1.
DR RefSeq; XP_007194740.1; XM_007194678.1.
DR AlphaFoldDB; A0A384B529; -.
DR STRING; 310752.A0A384B529; -.
DR GeneID; 103018736; -.
DR KEGG; bacu:103018736; -.
DR CTD; 3309; -.
DR InParanoid; A0A384B529; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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; PTHR19375:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..655
FT /note="78 kDa glucose-regulated protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030070526"
FT REGION 633..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 279..306
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 655 AA; 72396 MW; 62913B2F8DC95186 CRC64;
MKLSLVAAVL LLMLGAARPE EEDKKEDVGT VVGIDLGTTY SCVGVFKNGR VEIIANDQGN
RITPSYVAFT PEGERLIGDA AKNQLTSNPE NTVFDAKRLI GRTWNDPSVQ QDIKFLPFKV
VEKKTKPYIQ VDVGGGQTKT FAPEEISAMV LTKMKETAEA YLGKKVTHAV VTVPAYFNDA
QRQATKDAGT IAGLNVMRII NEPTAAAIAY GLDKREGEKN ILVFDLGGGT FDVSLLTIDN
GVFEVVATNG DTHLGGEDFD QRVMEHFIKL YKKKTGKDVR KDNRAVQKLR REVEKAKRAL
SSQHQARIEI ESFYEGEDFS ETLTRAKFEE LNMDLFRSTM KPVQKVLEDS DLKKSDIDEI
VLVGGSTRIP KIQQLVKEFF NGKEPSRGIN PDEAVAYGAA VQAGVLSGDQ DTGDLVLLDV
CPLTLGIETV GGVMTKLIPR NTVVPTKKSQ IFSTASDNQP TVTIKVYEGE RPLTKDNHLL
GTFDLTGIPP APRGVPQIEV TFEIDVNGIL RVTAEDKGTG NKNKITITND QNRLTPEEIE
RMVNDAEKFA EEDKKLKERI DTRNELESYA YSLKNQIGDK EKLGGKLSSE DKETMEKAVE
EKIEWLESHQ DADIEDFKAK KKELEEIVQP IISKLYGSAG PPPTGDEEPA DKDEL
//
