ID   DJB11_CANLF             Reviewed;         358 AA.
AC   P81999;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=DnaJ homolog subfamily B member 11;
DE   AltName: Full=ER-associated DNAJ;
DE   AltName: Full=ER-associated Hsp40 co-chaperone;
DE   AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 3;
DE            Short=ER-resident protein ERdj3;
DE            Short=ERdj3;
DE            Short=ERj3p;
DE   Flags: Precursor;
GN   Name=DNAJB11;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer;
RX   PubMed=16341006; DOI=10.1038/nature04338;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA   Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA   Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA   Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA   Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA   Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA   Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA   Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA   Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA   Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA   Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA   Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA   Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA   Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA   Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA   Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA   Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA   Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA   Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA   LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA   Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA   Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA   Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA   Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA   Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA   Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA   Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA   Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA   Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA   Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA   Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA   Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA   Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 23-45; 220-233 AND 275-285.
RC   TISSUE=Pancreas;
RX   PubMed=10595580; DOI=10.1515/bc.1999.149;
RA   Bies C., Guth S., Janoschek K., Nastainczyk W., Volkmer J., Zimmermann R.;
RT   "A Scj1p homolog and folding catalysts present in dog pancreas
RT   microsomes.";
RL   Biol. Chem. 380:1175-1182(1999).
RN   [3]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH HSPA5 AND SDF2L1.
RX   PubMed=15195998; DOI=10.1515/bc.2004.043;
RA   Bies C., Blum R., Dudek J., Nastainczyk W., Oberhauser S., Jung M.,
RA   Zimmermann R.;
RT   "Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like protein
RT   Scj1p.";
RL   Biol. Chem. 385:389-395(2004).
CC   -!- FUNCTION: As a co-chaperone for HSPA5 it is required for proper
CC       folding, trafficking or degradation of proteins. Binds directly to both
CC       unfolded proteins that are substrates for ERAD and nascent unfolded
CC       peptide chains, but dissociates from the HSPA5-unfolded protein complex
CC       before folding is completed. May help recruiting HSPA5 and other
CC       chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is
CC       necessary for maturation and correct trafficking of PKD1.
CC       {ECO:0000250|UniProtKB:Q9UBS4}.
CC   -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC       DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1
CC       and very small amounts of ERP29, but not, or at very low levels, CALR
CC       nor CANX. Binds to denatured substrates in an ATP-independent manner.
CC       Interacts via the J domain with HSPA5 in an ATP-dependent manner (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000269|PubMed:15195998}.
CC   -!- TISSUE SPECIFICITY: Pancreas.
CC   -!- PTM: Contains high-mannose Endo H-sensitive carbohydrates.
CC       {ECO:0000250}.
CC   -!- PTM: Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular
CC       disulfide bonds. The preferential partner for each Cys is not known (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; AAEX02021638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAEX02021639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P81999; -.
DR   SMR; P81999; -.
DR   STRING; 9612.ENSCAFP00000019966; -.
DR   PaxDb; P81999; -.
DR   Ensembl; ENSCAFT00000021500; ENSCAFP00000019966; ENSCAFG00000013546.
DR   Ensembl; ENSCAFT00030038402; ENSCAFP00030033502; ENSCAFG00030020904.
DR   Ensembl; ENSCAFT00040030616; ENSCAFP00040026611; ENSCAFG00040016457.
DR   Ensembl; ENSCAFT00845036198; ENSCAFP00845028323; ENSCAFG00845020542.
DR   VEuPathDB; HostDB:ENSCAFG00845020542; -.
DR   VGNC; VGNC:53459; DNAJB11.
DR   eggNOG; KOG0713; Eukaryota.
DR   GeneTree; ENSGT00940000155792; -.
DR   InParanoid; P81999; -.
DR   Proteomes; UP000002254; Chromosome 34.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
DR   GO; GO:0016556; P:mRNA modification; IEA:Ensembl.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0051604; P:protein maturation; ISS:UniProtKB.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
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   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   SUPFAM; SSF49493; SSF49493; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Direct protein sequencing; Disulfide bond;
KW   Endoplasmic reticulum; Glycoprotein; Phosphoprotein; Reference proteome;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:10595580"
FT   CHAIN           23..358
FT                   /note="DnaJ homolog subfamily B member 11"
FT                   /id="PRO_0000071036"
FT   DOMAIN          25..90
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   MOD_RES         188
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBS4"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   358 AA;  40422 MW;  D827E1F0E3BCE37B CRC64;
     MAPQNLGTLC LLLLYLLGAA IAGRDFYKIL GVPRSASIKD IKKAYRKLAL QLHPDRNPDD
     PRAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS SHGDIFSHFF GDFGFMFGGT
     PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL
     GPGRFQMTQE VVCDECPNVK LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR
     FRIKVVKHPI FERRGDDLYT NVTISLVESL VGFDMDITHL DGHKVHISRD KITRPGAKLW
     KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAREGIK QLLNQGSVQK VYNGLQGY