DJB14_MOUSE
ID DJB14_MOUSE Reviewed; 379 AA.
AC Q149L6; Q3TU54; Q3UTE5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=DnaJ homolog subfamily B member 14 {ECO:0000312|MGI:MGI:1917854};
GN Name=Dnajb14 {ECO:0000312|MGI:MGI:1917854};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-235 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Egg;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Acts as a co-chaperone with HSPA8/Hsc70; required to promote
CC protein folding and trafficking, prevent aggregation of client
CC proteins, and promote unfolded proteins to endoplasmic reticulum-
CC associated degradation (ERAD) pathway. Acts by determining
CC HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act
CC independently of HSPA8/Hsc70: together with DNAJB12, acts as a
CC chaperone that promotes maturation of potassium channels KCND2 and
CC KCNH2 by stabilizing nascent channel subunits and assembling them into
CC tetramers. While stabilization of nascent channel proteins is dependent
CC on HSPA8/Hsc70, the process of oligomerization of channel subunits is
CC independent of HSPA8/Hsc70. When overexpressed, forms membranous
CC structures together with DNAJB12 and HSPA8/Hsc70 within the nucleus;
CC the role of these structures, named DJANGOs, is still unclear.
CC {ECO:0000250|UniProtKB:Q8TBM8}.
CC -!- SUBUNIT: Interacts (via J domain) with HSPA8/Hsc70. Forms a
CC multiprotein complex, at least composed of DNAJB12, DNAJB14,
CC HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and HSPA8/Hsc70 is
CC direct. {ECO:0000250|UniProtKB:Q8TBM8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8TBM8}; Single-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q8TBM8}; Single-
CC pass membrane protein {ECO:0000255}. Note=Localizes to the endoplasmic
CC reticulum membrane. When overexpressed, forms membranous structures in
CC the nucleus. {ECO:0000250|UniProtKB:Q8TBM8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q149L6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q149L6-2; Sequence=VSP_024008;
CC Name=3;
CC IsoId=Q149L6-3; Sequence=VSP_024009, VSP_024010;
CC -!- SIMILARITY: Belongs to the DnaJ family. DNAJB12/DNAJB14 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK139489; BAE24035.1; -; mRNA.
DR EMBL; AK160961; BAE36117.1; -; mRNA.
DR EMBL; BC117717; AAI17718.1; -; mRNA.
DR EMBL; BC117718; AAI17719.1; -; mRNA.
DR CCDS; CCDS51077.1; -. [Q149L6-1]
DR RefSeq; NP_001028327.1; NM_001033155.1. [Q149L6-1]
DR RefSeq; XP_006502118.1; XM_006502055.2. [Q149L6-2]
DR AlphaFoldDB; Q149L6; -.
DR SMR; Q149L6; -.
DR BioGRID; 214160; 1.
DR STRING; 10090.ENSMUSP00000087641; -.
DR iPTMnet; Q149L6; -.
DR PhosphoSitePlus; Q149L6; -.
DR MaxQB; Q149L6; -.
DR PaxDb; Q149L6; -.
DR PeptideAtlas; Q149L6; -.
DR PRIDE; Q149L6; -.
DR ProteomicsDB; 279666; -. [Q149L6-1]
DR ProteomicsDB; 279667; -. [Q149L6-2]
DR ProteomicsDB; 279668; -. [Q149L6-3]
DR Antibodypedia; 45017; 101 antibodies from 22 providers.
DR Ensembl; ENSMUST00000090178; ENSMUSP00000087641; ENSMUSG00000074212. [Q149L6-1]
DR GeneID; 70604; -.
DR KEGG; mmu:70604; -.
DR UCSC; uc008rmq.2; mouse. [Q149L6-3]
DR UCSC; uc008rmr.2; mouse. [Q149L6-1]
DR CTD; 79982; -.
DR MGI; MGI:1917854; Dnajb14.
DR VEuPathDB; HostDB:ENSMUSG00000074212; -.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000157887; -.
DR HOGENOM; CLU_043579_3_0_1; -.
DR InParanoid; Q149L6; -.
DR OMA; AYCRKPA; -.
DR OrthoDB; 1173544at2759; -.
DR PhylomeDB; Q149L6; -.
DR TreeFam; TF105145; -.
DR BioGRID-ORCS; 70604; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Dnajb14; mouse.
DR PRO; PR:Q149L6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q149L6; protein.
DR Bgee; ENSMUSG00000074212; Expressed in spermatid and 224 other tissues.
DR ExpressionAtlas; Q149L6; baseline and differential.
DR Genevisible; Q149L6; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0071218; P:cellular response to misfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR015399; DUF1977_DnaJ-like.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF09320; DUF1977; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chaperone; Endoplasmic reticulum; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..379
FT /note="DnaJ homolog subfamily B member 14"
FT /id="PRO_0000281479"
FT TOPO_DOM 1..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..379
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 108..172
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 56..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024008"
FT VAR_SEQ 151..158
FT /note="KIGNAYAV -> SKVTYDTS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024009"
FT VAR_SEQ 159..379
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024010"
SQ SEQUENCE 379 AA; 42326 MW; 83C79C1C51A18D82 CRC64;
MEGNRDEAEK CVQIAREALS AGNRDKAQRF LQKAEKLYPL PAARALLEII MKNGSTAGSS
THCRKPPGSS DQSKPSCGKD GTSGAGEGGK VYTKDQVEGV LSINKCKNYY EVLGVTKDAG
DEDLKKAYRK LALKFHPDKN HAPGATDAFK KIGNAYAVLS NPEKRKQYDL TGSEEQACNH
QNNGRFNFHR GCEADITPED LFNIFFGGGF PSGSVHSFSN GRAAYSHQHQ HRHSGHEREE
ERADGGFSVF IQLMPIIVLI LVSLLSQLMV SNPPYSLYPR SGSGQTIKMQ TENLGVVYYV
SKDFKSEYKG TLLQKVEKSV EEDYVTNIRN NCWKERQQKT DMQYAAKVYR DEQLRRKADA
LSMENCKELE RLTSLYKGG
