DNJ21_ARATH
ID DNJ21_ARATH Reviewed; 687 AA.
AC Q0WT48; Q9CA96; Q9SSD9;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=DnaJ protein ERDJ2A;
DE AltName: Full=Chaperone protein dnaJ 21;
DE Short=AtDjC21;
DE Short=AtJ21;
DE AltName: Full=Endoplasmic reticulum dnaJ domain-containing protein 2A;
DE Short=AtERdj2A;
DE AltName: Full=Translocation protein SEC63 homolog ERDJ2A;
GN Name=ERDJ2A; Synonyms=C21; OrderedLocusNames=At1g79940;
GN ORFNames=F18B13.2, F19K16.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11599562; DOI=10.1379/1466-1268(2001)006<0209:tjdpoa>2.0.co;2;
RA Miernyk J.A.;
RT "The J-domain proteins of Arabidopsis thaliana: an unexpectedly large and
RT diverse family of chaperones.";
RL Cell Stress Chaperones 6:209-218(2001).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY TUNICAMYCIN, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18718935; DOI=10.1093/pcp/pcn119;
RA Yamamoto M., Maruyama D., Endo T., Nishikawa S.;
RT "Arabidopsis thaliana has a set of J proteins in the endoplasmic reticulum
RT that are conserved from yeast to animals and plants.";
RL Plant Cell Physiol. 49:1547-1562(2008).
RN [6]
RP INTERACTION WITH OEP61/TPR7.
RX PubMed=22899711; DOI=10.1242/jcs.111054;
RA Schweiger R., Muller N.C., Schmitt M.J., Soll J., Schwenkert S.;
RT "AtTPR7 is a chaperone-docking protein of the Sec translocon in
RT Arabidopsis.";
RL J. Cell Sci. 125:5196-5207(2012).
CC -!- FUNCTION: Required for integral membrane and secreted preprotein
CC translocation across the endoplasmic reticulum membrane. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with OEP61/TPR7. {ECO:0000269|PubMed:22899711}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:18718935}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:18718935}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q0WT48-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flower buds and flowers.
CC {ECO:0000269|PubMed:18718935}.
CC -!- INDUCTION: By tunicamycin. {ECO:0000269|PubMed:18718935}.
CC -!- DISRUPTION PHENOTYPE: Male gametophytic lethal due to defect in pollen
CC germination and pollen tube growth. {ECO:0000269|PubMed:18718935}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55462.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG52236.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009322; AAD55462.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011717; AAG52236.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36329.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36330.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36331.1; -; Genomic_DNA.
DR EMBL; AK227714; BAE99700.1; -; mRNA.
DR PIR; F96830; F96830.
DR RefSeq; NP_001031306.2; NM_001036229.3. [Q0WT48-1]
DR RefSeq; NP_001117623.1; NM_001124151.1. [Q0WT48-1]
DR RefSeq; NP_178112.2; NM_106643.5. [Q0WT48-1]
DR AlphaFoldDB; Q0WT48; -.
DR BioGRID; 29552; 21.
DR IntAct; Q0WT48; 16.
DR STRING; 3702.AT1G79940.3; -.
DR iPTMnet; Q0WT48; -.
DR SwissPalm; Q0WT48; -.
DR PaxDb; Q0WT48; -.
DR PRIDE; Q0WT48; -.
DR ProteomicsDB; 222084; -. [Q0WT48-1]
DR EnsemblPlants; AT1G79940.1; AT1G79940.1; AT1G79940. [Q0WT48-1]
DR EnsemblPlants; AT1G79940.2; AT1G79940.2; AT1G79940. [Q0WT48-1]
DR EnsemblPlants; AT1G79940.3; AT1G79940.3; AT1G79940. [Q0WT48-1]
DR GeneID; 844334; -.
DR Gramene; AT1G79940.1; AT1G79940.1; AT1G79940. [Q0WT48-1]
DR Gramene; AT1G79940.2; AT1G79940.2; AT1G79940. [Q0WT48-1]
DR Gramene; AT1G79940.3; AT1G79940.3; AT1G79940. [Q0WT48-1]
DR KEGG; ath:AT1G79940; -.
DR Araport; AT1G79940; -.
DR TAIR; locus:2016354; AT1G79940.
DR eggNOG; KOG0721; Eukaryota.
DR eggNOG; KOG0951; Eukaryota.
DR InParanoid; Q0WT48; -.
DR OMA; RAILHAH; -.
DR PhylomeDB; Q0WT48; -.
DR PRO; PR:Q0WT48; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WT48; baseline and differential.
DR Genevisible; Q0WT48; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0031207; C:Sec62/Sec63 complex; IBA:GO_Central.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR004179; Sec63-dom.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF02889; Sec63; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..687
FT /note="DnaJ protein ERDJ2A"
FT /id="PRO_0000430364"
FT TOPO_DOM 1..8
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..190
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..687
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 99..164
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 205..603
FT /note="SEC63"
FT REGION 619..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..654
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 687 AA; 76904 MW; 7F9989FDECD529F7 CRC64;
MAASEENSAL FPIFILTIMA IPLVPYTMVK LSGALSKKQR TIHCQCLECD RSGKYKRSLF
KKISNFSTWS NLTLVLLWVV MIFLIYYTKN MSREAQVFDP FSILGLEPGV TDSEIKKAYR
RLSIQYHPDK NPDPEANKYF VEFISKAYQA LTDSVSRENF EKYGHPDGRQ GFQMGIALPQ
FLLDIDGASG GILLLWIVGV CILLPLVIAV IYLSRSSKYT GNYVMHQTLS AYYYLMKPSL
APSKVMEVFT KAAEYMEIPV RRTDDEPLQK LFMSVRSELN LDLKNMKQEQ AKFWKQHPAI
VKTELLIQAQ LTRESGVLSP ALQGDFRRVL ELAPRLLEEL LKMAVIPRTA QGHGWLRPAV
GVVELSQCIV QAVPLSARKS SGVSSEGISP FLQLPHFSDA VVKKIARKKV KSFQDLQEMR
LEDRSELLTQ VAGLSATDVE DIEKVLEMMP SITVDITCET EGEEGIQEGD IVTLQAWVTL
KRPNGLVGAL PHAPYFPFHK EENYWVLLAD SVSNNVWFSQ KVSFLDEGGA ITAASKAISE
SMEGSGAGVK ETNDAVREAI EKVKGGSRLV MGKLQAPAEG TYNLTCFCLC DTWIGCDKKQ
ALKVKVLKRT RAGTRGLVSD EGAIAEEGME EEDEIEEEDY DDDYESEYSE DEDEKKDMDE
KRGSKKANGS VKQKKESSSE ESGSEEE
