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Database: UniProt
Entry: G3T5V4_LOXAF
LinkDB: G3T5V4_LOXAF
Original site: G3T5V4_LOXAF 
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
//
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