ID A0A2U9CDC6_SCOMX Unreviewed; 360 AA.
AC A0A2U9CDC6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DnaJ homolog subfamily B member 11 {ECO:0000256|ARBA:ARBA00039611};
DE AltName: Full=ER-associated DNAJ {ECO:0000256|ARBA:ARBA00041948};
DE AltName: Full=ER-associated Hsp40 co-chaperone {ECO:0000256|ARBA:ARBA00042329};
DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 3 {ECO:0000256|ARBA:ARBA00041532};
GN Name=dnajb11 {ECO:0000313|Ensembl:ENSSMAP00000026092.1};
GN ORFNames=SMAX5B_010762 {ECO:0000313|EMBL:AWP13699.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP13699.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP13699.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSMAP00000026092.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
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DR EMBL; CP026256; AWP13699.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000026092; -.
DR Ensembl; ENSSMAT00000026408.2; ENSSMAP00000026092.1; ENSSMAG00000015925.2.
DR GeneTree; ENSGT00940000155792; -.
DR OMA; FAGRDFY; -.
DR OrthoDB; 2785358at2759; -.
DR Proteomes; UP000246464; Chromosome 14.
DR Proteomes; UP000694558; Chromosome 14.
DR Bgee; ENSSMAG00000015925; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10747; DnaJ_C; 1.
DR Gene3D; 1.10.287.110; DnaJ 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; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR44298; DNAJ HOMOLOG SUBFAMILY B MEMBER 11; 1.
DR PANTHER; PTHR44298:SF1; DNAJ HOMOLOG SUBFAMILY B MEMBER 11; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..360
FT /note="DnaJ homolog subfamily B member 11"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040585464"
FT DOMAIN 27..92
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 360 AA; 40729 MW; ECD36AAA6AB271C6 CRC64;
MATGGMNLCR VCCLLLGVVS AVLAGRDFYQ ILGVSKSASV RDVKKAYRKL ALQLHPDRNQ
DDPKAQDKFA DLGAAYEVLS DEEKRKQYDA YGEDGLKEGH HSSHNDIFSS FFGDFGFMFG
GNRQQQDRNI PRGNDIILDL EVTLEEVYSG NFVEVVRNKP IAKEAPGKRK CNCRQEMRTT
QLGPGRFQMT QEMVCDECPN VKLVNEERTL EVEIEQGVRD EMEYPFIGEG EPHIDGEPGD
LRFRIKVLKH PVFERRGDDL YTNVTISLVE ALVGFEMDIV HLDGHKVHIV RDKITKPGAR
MWKKGEGLPN FDNINIRGSL IISFDVEFPQ TQLDEQQKDG IRSLLKQGSA QKVYNGLQGY
//
