SCJ1_YEAST
ID SCJ1_YEAST Reviewed; 377 AA.
AC P25303; D6W039;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=DnaJ-related protein SCJ1;
DE Short=J protein SCJ1;
DE Flags: Precursor;
GN Name=SCJ1; OrderedLocusNames=YMR214W; ORFNames=YM8261.08;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2000136; DOI=10.1038/349627a0;
RA Blumberg H., Silver P.A.;
RT "A homologue of the bacterial heat-shock gene DnaJ that alters protein
RT sorting in yeast.";
RL Nature 349:627-630(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=7744969; DOI=10.1083/jcb.129.4.979;
RA Schlenstedt G., Harris S., Risse B., Lill R., Silver P.A.;
RT "A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum
RT with BiP/Kar2p via a conserved domain that specifies interactions with
RT Hsp70s.";
RL J. Cell Biol. 129:979-988(1995).
RN [5]
RP FUNCTION.
RX PubMed=9817751; DOI=10.1083/jcb.143.4.921;
RA Silberstein S., Schlenstedt G., Silver P.A., Gilmore R.;
RT "A role for the DnaJ homologue Scj1p in protein folding in the yeast
RT endoplasmic reticulum.";
RL J. Cell Biol. 143:921-933(1998).
RN [6]
RP FUNCTION.
RX PubMed=11381090; DOI=10.1083/jcb.153.5.1061;
RA Nishikawa S.I., Fewell S.W., Kato Y., Brodsky J.L., Endo T.;
RT "Molecular chaperones in the yeast endoplasmic reticulum maintain the
RT solubility of proteins for retrotranslocation and degradation.";
RL J. Cell Biol. 153:1061-1070(2001).
RN [7]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Regulates protein folding in the endoplasmic reticulum lumen.
CC Probably acts as a J-protein for the Hsp70-type chaperone KAR2 by
CC stimulating its ATP-dependent reaction cycle and initiating folding
CC reactions. Also involved in the endoplasmic reticulum-associated
CC degradation (ERAD) process. Cooperates with KAR2 and another J-protein
CC JEM1 to facilitate the export of ERAD substrates to the cytoplasm by
CC maintaining them in a translocation-competent state and preventing
CC their aggregation in the endoplasmic reticulum lumen.
CC {ECO:0000269|PubMed:11381090, ECO:0000269|PubMed:9817751}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:7744969}.
CC -!- MISCELLANEOUS: Present with 8260 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA41529.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA89929.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X58679; CAA41529.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z49809; CAA89929.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006946; DAA10113.1; -; Genomic_DNA.
DR PIR; S13648; S13648.
DR RefSeq; NP_013941.2; NM_001182721.1.
DR AlphaFoldDB; P25303; -.
DR SMR; P25303; -.
DR BioGRID; 35392; 170.
DR DIP; DIP-2395N; -.
DR IntAct; P25303; 36.
DR MINT; P25303; -.
DR STRING; 4932.YMR214W; -.
DR MaxQB; P25303; -.
DR PaxDb; P25303; -.
DR PRIDE; P25303; -.
DR EnsemblFungi; YMR214W_mRNA; YMR214W; YMR214W.
DR GeneID; 855254; -.
DR KEGG; sce:YMR214W; -.
DR SGD; S000004827; SCJ1.
DR VEuPathDB; FungiDB:YMR214W; -.
DR eggNOG; KOG0712; Eukaryota.
DR HOGENOM; CLU_017633_0_2_1; -.
DR InParanoid; P25303; -.
DR OMA; DHCRGSG; -.
DR BioCyc; YEAST:G3O-32897-MON; -.
DR PRO; PR:P25303; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P25303; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IMP:SGD.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006986; P:response to unfolded protein; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10719; DnaJ_zf; 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; IPR044713; DNJA1/2-like.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR43888; PTHR43888; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR SUPFAM; SSF57938; SSF57938; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 1: Evidence at protein level;
KW Chaperone; Endoplasmic reticulum; Metal-binding; Protein transport;
KW Reference proteome; Repeat; Signal; Transport; Zinc; Zinc-finger.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..377
FT /note="DnaJ-related protein SCJ1"
FT /id="PRO_0000071091"
FT DOMAIN 23..88
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REPEAT 169..176
FT /note="CXXCXGXG motif"
FT REPEAT 185..192
FT /note="CXXCXGXG motif"
FT REPEAT 211..218
FT /note="CXXCXGXG motif"
FT REPEAT 225..232
FT /note="CXXCXGXG motif"
FT ZN_FING 156..237
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT MOTIF 288..290
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 374..377
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
SQ SEQUENCE 377 AA; 41543 MW; FD0226902F33E2B8 CRC64;
MIPKLYIHLI LSLLLLPLIL AQDYYAILEI DKDATEKEIK SAYRQLSKKY HPDKNAGSEE
AHQKFIEVGE AYDVLSDPEK KKIYDQFGAD AVKNGGGGGG PGGPGAGGFH DPFDIFERMF
QGGHGGPGGG FGQRQRQRGP MIKVQEKLSL KQFYSGSSIE FTLNLNDECD ACHGSGSADG
KLAQCPDCQG RGVIIQVLRM GIMTQQIQQM CGRCGGTGQI IKNECKTCHG KKVTKKNKFF
HVDVPPGAPR NYMDTRVGEA EKGPDFDAGD LVIEFKEKDT ENMGYRRRGD NLYRTEVLSA
AEALYGGWQR TIEFLDENKP VKLSRPAHVV VSNGEVEVVK GFGMPKGSKG YGDLYIDYVV
VMPKTFKSGQ NMLKDEL
