P25303 (SCJ1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DnaJ-related protein SCJ1
Short name=J protein SCJ1

Gene names

Name:	SCJ1
Ordered Locus Names:	YMR214W
ORF Names:	YM8261.08

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulates protein folding in the endoplasmic reticulum lumen. Probably acts as a J-protein for the Hsp70-type chaperone KAR2 by stimulating its ATP-dependent reaction cycle and initiating folding reactions. Also involved in the endoplasmic reticulum-associated degradation (ERAD) process. Cooperates with KAR2 and another J-protein JEM1 to facilitate the export of ERAD substrates to the cytoplasm by maintaining them in a translocation-competent state and preventing their aggregation in the endoplasmic reticulum lumen. Ref.5 Ref.6
Subcellular location	Endoplasmic reticulum lumen Ref.4.
Miscellaneous	Present with 8260 molecules/cell in log phase SD medium.
Sequence similarities	Contains 1 CR-type zinc finger. Contains 1 J domain.
Sequence caution	The sequence CAA41529.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA89929.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Endoplasmic reticulum
Domain	Repeat Signal Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chaperone
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from mutant phenotype Ref.6. Source: SGD protein folding in endoplasmic reticulum Inferred from mutant phenotype Ref.5. Source: SGD protein transport Inferred from electronic annotation. Source: UniProtKB-KW response to unfolded protein Inferred from mutant phenotype Ref.5. Source: SGD
Cellular_component	endoplasmic reticulum lumen Inferred from direct assay Ref.4. Source: SGD
Molecular_function	chaperone binding Inferred from mutant phenotype Ref.5. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 377	356	DnaJ-related protein SCJ1		PRO_0000071091
Regions
	Domain	23 – 88	66	J
	Repeat	169 – 176	8	CXXCXGXG motif
	Repeat	185 – 192	8	CXXCXGXG motif
	Repeat	211 – 218	8	CXXCXGXG motif
	Repeat	225 – 232	8	CXXCXGXG motif
	Zinc finger	156 – 237	82	CR-type
	Motif	288 – 290	3	Cell attachment site Potential
	Motif	374 – 377	4	Prevents secretion from ER Potential
	Compositional bias	95 – 132	38	Gly-rich

Sequences

	Sequence		Length	Mass (Da)
	P25303 [UniParc]. Last modified September 5, 2006. Version 2. Checksum: FD0226902F33E2B8	FASTA	377	41,543
	10 20 30 40 50 60 MIPKLYIHLI LSLLLLPLIL AQDYYAILEI DKDATEKEIK SAYRQLSKKY HPDKNAGSEE 70 80 90 100 110 120 AHQKFIEVGE AYDVLSDPEK KKIYDQFGAD AVKNGGGGGG PGGPGAGGFH DPFDIFERMF 130 140 150 160 170 180 QGGHGGPGGG FGQRQRQRGP MIKVQEKLSL KQFYSGSSIE FTLNLNDECD ACHGSGSADG 190 200 210 220 230 240 KLAQCPDCQG RGVIIQVLRM GIMTQQIQQM CGRCGGTGQI IKNECKTCHG KKVTKKNKFF 250 260 270 280 290 300 HVDVPPGAPR NYMDTRVGEA EKGPDFDAGD LVIEFKEKDT ENMGYRRRGD NLYRTEVLSA 310 320 330 340 350 360 AEALYGGWQR TIEFLDENKP VKLSRPAHVV VSNGEVEVVK GFGMPKGSKG YGDLYIDYVV 370 VMPKTFKSGQ NMLKDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A homologue of the bacterial heat-shock gene DnaJ that alters protein sorting in yeast." Blumberg H., Silver P.A. Nature 349:627-630(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s." Schlenstedt G., Harris S., Risse B., Lill R., Silver P.A. J. Cell Biol. 129:979-988(1995) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION OF PROBABLE INITIATION SITE.
[5]	"A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum." Silberstein S., Schlenstedt G., Silver P.A., Gilmore R. J. Cell Biol. 143:921-933(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation." Nishikawa S.I., Fewell S.W., Kato Y., Brodsky J.L., Endo T. J. Cell Biol. 153:1061-1070(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Sequencing and comparison of yeast species to identify genes and regulatory elements." Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S. Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X58679 Genomic DNA. Translation: CAA41529.1. Different initiation. Z49809 Genomic DNA. Translation: CAA89929.1. Different initiation. BK006946 Genomic DNA. Translation: DAA10113.1.
PIR	S13648.
RefSeq	NP_013941.2. NM_001182721.1.
3D structure databases
ProteinModelPortal	P25303.
SMR	P25303. Positions 22-91, 137-364.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2395N.
IntAct	P25303. 10 interactions.
MINT	MINT-639819.
STRING	4932.YMR214W.
Proteomic databases
PaxDb	P25303.
PeptideAtlas	P25303.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR214W; YMR214W; YMR214W.
GeneID	855254.
KEGG	sce:YMR214W.
Organism-specific databases
CYGD	YMR214w.
SGD	S000004827. SCJ1.
Phylogenomic databases
eggNOG	COG0484.
GeneTree	ENSGT00700000104542.
HOGENOM	HOG000226718.
KO	K14002.
OMA	APDMNDI.
OrthoDB	EOG4HQHT6.
Gene expression databases
Genevestigator	P25303.
GermOnline	YMR214W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.10.287.110. 1 hit. 2.10.230.10. 1 hit.
InterPro	IPR002939. DnaJ_C. IPR001623. DnaJ_domain. IPR018253. DnaJ_domain_CS. IPR008971. HSP40/DnaJ_pept-bd. IPR001305. HSP_DnaJ_Cys-rich_dom. [Graphical view]
Pfam	PF00226. DnaJ. 1 hit. PF01556. DnaJ_C. 1 hit. PF00684. DnaJ_CXXCXGXG. 1 hit. [Graphical view]
PRINTS	PR00625. JDOMAIN.
SMART	SM00271. DnaJ. 1 hit. [Graphical view]
SUPFAM	SSF46565. DnaJ_N. 1 hit. SSF49493. HSP40_DnaJ_pep. 2 hits. SSF57938. HSP_DnaJ_cys-rich. 1 hit.
PROSITE	PS00636. DNAJ_1. 1 hit. PS50076. DNAJ_2. 1 hit. PS00014. ER_TARGET. 1 hit. PS51188. ZF_CR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	978834.

Entry information

Entry name

SCJ1_YEAST

Accession

Primary (citable) accession number: P25303
Secondary accession number(s): D6W039

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program