DNJ29_ARATH
ID DNJ29_ARATH Reviewed; 661 AA.
AC F4JIN3; O49559; Q949Z5;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=DnaJ protein ERDJ2B;
DE AltName: Full=Chaperone protein dnaJ 29;
DE Short=AtDjC29;
DE Short=AtJ29;
DE AltName: Full=Endoplasmic reticulum dnaJ domain-containing protein 2B;
DE Short=AtERdj2B;
DE AltName: Full=Translocation protein SEC63 homolog ERDJ2B;
GN Name=ERDJ2B; Synonyms=C29; OrderedLocusNames=At4g21180; ORFNames=F7J7.120;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] OF 365-661.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 -!- 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: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:18718935}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA17537.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79118.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021960; CAA17537.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161554; CAB79118.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84416.1; -; Genomic_DNA.
DR EMBL; AY050792; AAK92727.2; -; mRNA.
DR PIR; T04949; T04949.
DR RefSeq; NP_567621.1; NM_118237.4.
DR AlphaFoldDB; F4JIN3; -.
DR STRING; 3702.AT4G21180.1; -.
DR PaxDb; F4JIN3; -.
DR PRIDE; F4JIN3; -.
DR ProteomicsDB; 222085; -.
DR EnsemblPlants; AT4G21180.1; AT4G21180.1; AT4G21180.
DR GeneID; 827866; -.
DR Gramene; AT4G21180.1; AT4G21180.1; AT4G21180.
DR KEGG; ath:AT4G21180; -.
DR Araport; AT4G21180; -.
DR TAIR; locus:2127373; AT4G21180.
DR eggNOG; KOG0721; Eukaryota.
DR eggNOG; KOG0951; Eukaryota.
DR HOGENOM; CLU_014210_2_0_1; -.
DR InParanoid; F4JIN3; -.
DR OMA; IAISETM; -.
DR OrthoDB; 686427at2759; -.
DR PRO; PR:F4JIN3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JIN3; baseline and differential.
DR Genevisible; F4JIN3; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA: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 Chaperone; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..661
FT /note="DnaJ protein ERDJ2B"
FT /id="PRO_0000430365"
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..661
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 99..164
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 206..597
FT /note="SEC63"
FT REGION 608..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..633
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..654
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 661 AA; 74825 MW; 733E03956D2D0471 CRC64;
MAESEENSVL FPIFILTMMA IPLVPYTFVK LSRAFSKKQR SIHCQCLECD RSGKYKRSIS
QSISSFTSCS NLTVVLLWIV MIFLIYHTKN MSRESQLFEP FGILGLEPGA SDSEIKKAYR
RLSIQYHPDK NPDPEANKYF VESIAKAYQA LTDPLSRENF EKYGHPDGRQ GYTMGIALPQ
FILNMNGESG GILLLCTVGL CILLPLVIAS IYLWRSSKYT GNHVKLQTRQ AYFELLQPSL
TPSKVMDIFI RAAEYAEISV RKSDDESLQK LFMSVKSELN LDPKKLKQEE AKFWKKHPAT
IKTELLIQKQ LTRESSVLSP TLQRDFRHVL EFAPRLLEDL IKMAVIPRNE QGRGWLRPAL
GVMELSQCIV QAVPLSARKS SSEDIAPFLQ LPHFNESIAK SIALQVKSFQ KFQELSLAER
SKLLREVVSL SETDVQDIEK VLEMIPSLKI NVTCKTEGEE GIQEGDIMTV QAWITLKRPN
GLIGAIPHSP YFPFHKEENF WVLLADSNHV WFFQKVKFMD EAGAIAAASN TITETMEPLG
ASVKETNDAV KEAVEKVKSG SRLVMGRLLA PGEGTYNLTC FCLSDTWIGC DQKTSLKVEV
LKRTRDVEGE NAEEGLEEED DEIEEEDYES EYSEDEEDKK RGSKKKVNKE SSSEESGSDE
E
