ID G3T5V4_LOXAF Unreviewed; 840 AA.
AC G3T5V4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 08-NOV-2023, entry version 65.
DE RecName: Full=Heat shock 70 kDa protein 4 {ECO:0000256|ARBA:ARBA00018348};
GN Name=HSPA4 {ECO:0000313|Ensembl:ENSLAFP00000008844.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000008844.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000008844.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000008844.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000008844.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000008844.3};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBUNIT: Interacts with TJP1/ZO-1. {ECO:0000256|ARBA:ARBA00011800}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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DR RefSeq; XP_003405063.1; XM_003405015.2.
DR AlphaFoldDB; G3T5V4; -.
DR STRING; 9785.ENSLAFP00000008844; -.
DR Ensembl; ENSLAFT00000010562.3; ENSLAFP00000008844.3; ENSLAFG00000010561.3.
DR GeneID; 100661115; -.
DR KEGG; lav:100661115; -.
DR CTD; 3308; -.
DR eggNOG; KOG0103; Eukaryota.
DR GeneTree; ENSGT00940000156067; -.
DR HOGENOM; CLU_005965_5_1_1; -.
DR InParanoid; G3T5V4; -.
DR OMA; PSCIAFG; -.
DR OrthoDB; 276440at2759; -.
DR TreeFam; TF105043; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:Ensembl.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IEA:Ensembl.
DR CDD; cd11737; HSPA4_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 2.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_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 InterPro; IPR042052; HSPA4_NBD.
DR PANTHER; PTHR45639:SF6; HEAT SHOCK 70 KDA PROTEIN 4; 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; 2.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT REGION 501..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 94442 MW; 8C50F43F064C1912 CRC64;
MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACIS FGPKNRSIGA AAKSQVISNA
KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD IVQLPTGLTG IKVRYMEEER NFTTEQVTAM
LLSKLKETAE NVLKKPVVDC VISVPCFYTD AERRSVMDAT QIAGLNCLRL MNETTAVALA
YGIYKQDLPA LEEKPRNVVF VDMGHSAYQV SVCAFNRGKL KVLATAFNTT LGGRKFDEVL
VNHFCEEFGK KYKLDIKSKI RALLRLSQEC EKLKKLMSAN ASDLPLNIEC FMNDVDVSGT
MNRGKFLEMC DDLLARVEPP LRSVLEQAKL KKEDIYAVEI VGGATRIPAV KEKISKFFGK
ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY PISLRWNSPA EEGSSDCEVF
PKNHAAPFSR VLTFYRKEPF TLEAYYSSPQ DLPYPDPAIA QFSVQKVTPQ SDGSSSKVKV
KARVNIHGIF SVSSASLVEV HKSEENEEPM ETDQNAKEEE KMQVDQEEPH VEEQQQQTPA
ENKAESEEME TSQAGSKDKK MDQPPQAKKA KVKTSTVDLP IENQLLWQID REMLNLYIEN
EGKMIMQDKL EKERNDAKNA VEEYVYEMRD KLNGEYEKFV SEDDRNSFSL KLEDTENWLY
EDGEDQPKQV YVDKLAELKN LGQPIKMRFQ ESEERPKLFE ELGKQIQQYM KVVSSFKNKE
DQYDHLDAAD VVKVEKSMNE AMEWMNNKLN LQNKQSLTMD PVIKAKEIEA KIKELINTCS
PIVSKPKPKV EPPKEEQKNA EQNGPVNGQG DSPGPQAAEQ GTDTAVPSDS DKKLPEMDID
//