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Database: UniProt
Entry: G3R755_GORGO
LinkDB: G3R755_GORGO
Original site: G3R755_GORGO 
ID   G3R755_GORGO            Unreviewed;       390 AA.
AC   G3R755;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=DnaJ heat shock protein family (Hsp40) member A4 {ECO:0000313|Ensembl:ENSGGOP00000011183.3};
GN   Name=DNAJA4 {ECO:0000313|Ensembl:ENSGGOP00000011183.3};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000011183.3, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000011183.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000011183.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000011183.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC       anchor {ECO:0000256|ARBA:ARBA00004635}.
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DR   EMBL; CABD030097328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030097329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G3R755; -.
DR   STRING; 9593.ENSGGOP00000011183; -.
DR   Ensembl; ENSGGOT00000011511.3; ENSGGOP00000011183.3; ENSGGOG00000011469.3.
DR   eggNOG; KOG0712; Eukaryota.
DR   GeneTree; ENSGT00940000155707; -.
DR   InParanoid; G3R755; -.
DR   OMA; FPDVINP; -.
DR   TreeFam; TF105141; -.
DR   Proteomes; UP000001519; Chromosome 15.
DR   Bgee; ENSGGOG00000011469; Expressed in testis and 5 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
DR   GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0090084; P:negative regulation of inclusion body assembly; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10747; DnaJ_C; 1.
DR   CDD; cd10719; DnaJ_zf; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR   Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR044713; DNJA1/2-like.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR43888:SF9; DNAJ HOMOLOG SUBFAMILY A MEMBER 4; 1.
DR   PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-RELATED; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR   SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00546}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00546};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00546}.
FT   DOMAIN          1..61
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          115..199
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         115..199
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
SQ   SEQUENCE   390 AA;  43927 MW;  7AA440B5298EDF3B CRC64;
     YDILGVKPSA SPEEIKKAYR KLALKYHPDK NPDEGEKFKL ISQAYEVLSD PKKRDVYDQG
     GEQAIKEGGS GSPSFSSPMD IFDMFFGGGG RMARERRGKN VVHQLSVTLE DLYNGVTKKL
     ALQKNVICEK CEGVGGKKGS VEKCPLCKGR GMQIHIQQIG PGMVQQIQTV CIECKGQGER
     INPKDRCESC SGAKVIREKK IIEVHVEKGM KDGQKILFHG EGDQEPELEP GDVIIVLDQK
     DHSVFQRRGH DLIMKMKIQL SEALCGFKKT IKTLDNRILV ITSKAGEVIK HGDLRCVHDE
     GMPIYKAPLE KGILIIQFLV IFPEKHWLSL EKLPQLEALL PPRQKVRITD DMDQVELKEF
     CPNEQNWRQH REAYEEDEDG PRAGVQCQTA
//
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