SEC63/YOR254C Summary

Standard Name	SEC63 1
Systematic Name	YOR254C
Alias	PTL1 2
Feature Type	ORF, Verified
Description	Essential subunit of Sec63 complex (Sec63p, Sec62p, Sec66p and Sec72p); with Sec61 complex, Kar2p/BiP and Lhs1p forms a channel competent for SRP-dependent and post-translational SRP-independent protein targeting and import into the ER (3, 4, 5 and see Summary Paragraph)
Name Description	SECretory 6

Chromosomal Location	ChrXV:807023 to 805032 \| ORF Map \| GBrowse
	Note: this feature is encoded on the Crick strand.

Gene Ontology Annotations All SEC63 GO evidence and references

	View Computational GO annotations for SEC63
Molecular Function
Manually curated	protein transporter activity (IMP)
Biological Process
Manually curated	cytosol to ER transport (IMP) posttranslational protein targeting to membrane (IMP) posttranslational protein targeting to membrane, translocation (IDA) SRP-dependent cotranslational protein targeting to membrane (IMP)
Cellular Component
Manually curated	endoplasmic reticulum membrane (TAS) Sec62/Sec63 complex (IPI)
High-throughput	integral to membrane (ISM) mitochondrion (IDA)

Mutant phenotypes All SEC63 Phenotype evidence and references

Classical genetics
conditional	KAR2 mRNA accumulation: increased RPL3 mRNA accumulation: decreased endocytosis: decreased heat sensitivity: increased K28 killer toxin secretion: decreased prepro-carboxypeptidase (ppCPY) accumulation: increased prepro-alpha factor accumulation: increased CPY* accumulation: increased SV40-NLS-cytochrome c1 distribution: abnormal SV40-NLS-invertase distribution: abnormal 35-kD nucleolar protein distribution: abnormal alpha-amylase distribution: abnormal
null	inviable
reduction of function	mating efficiency: decreased nuclear fusion during mating: absent
Large-scale survey
null	haploproficient inviable
overexpression	vegetative growth: decreased rate
reduction of function	competitive fitness: decreased telomere length: increased
repressible	mitochondrial morphology: abnormal
Resources	PROPHECY \| PhenoM \| SCMD \| ScreenTroll \| Yeast Fitness Database

interactions All SEC63 Interaction evidence and references

	416 total interaction(s) for 261 unique genes/features.
Physical Interactions	Affinity Capture-MS: 32 Affinity Capture-RNA: 1 Affinity Capture-Western: 15 Biochemical Activity: 5 Co-localization: 3 Co-purification: 14 PCA: 22 Reconstituted Complex: 3 Two-hybrid: 4
Genetic Interactions	Dosage Lethality: 1 Dosage Rescue: 4 Negative Genetic: 270 Phenotypic Enhancement: 2 Positive Genetic: 32 Synthetic Growth Defect: 2 Synthetic Lethality: 2 Synthetic Rescue: 4
Resources	BioGRID \| BOND \| BioPIXIE \| CYC2008 (complexes) \| Complexome \| DIP \| DRYGIN \| GeneMANIA \| InterologFinder

Expression Summary


Resources	Expression Summary \| Cell cycle and metabolic oscillation \| Cell cycle transcript profile \| Cyclebase \| Genevestigator \| GermOnline \| SPELL \| YMGV \| YeastFunc

Protein Information All SEC63 Protein evidence and references

Localization	YeastRC \| YPL+ \| YeastGFP
Phosphorylation	PhosphoGRID \| PhosphoPep Database
Structure	GPMDB \| SCOP \| YeastRC
Homologs	Ashbya (AGD) \| CGD Homologs \| CandidaDB Homologs \| Fungal Orthogroups Repository \| P-POD \| PDB Homologs \| PhylomeDB \| YGOB \| YOGY

sequence information

ChrXV:807023 to 805032 | |

Note: this feature is encoded on the Crick strand.

Last Update

Coordinates: 2011-02-03 | Sequence: 1996-07-31

Subfeature details

	Relative Coordinates	Chromosomal Coordinates	Most Recent Updates
	Relative Coordinates	Chromosomal Coordinates	Coordinates	Sequence
CDS	1..1992	807023..805032	2011-02-03	1996-07-31

Retrieve sequences

Analyze Sequence

S288C only	BLASTP \| ATCC/WashU Clones \| BLASTN \| Design Primers \| Restriction Fragment Map \| Restriction Fragment Sizes \| Six-Frame Translation
S288C vs. other species	Fungal Alignment \| BLASTN vs. fungi \| BLASTP at NCBI \| BLASTP vs. fungi \| Synteny Viewer
S288C vs. other strains	Strain Alignment

Resources

External Links	All Associated Seq \| Entrez Gene \| Entrez RefSeq Protein \| MIPS \| Search all NCBI (Entrez) \| UniProtKB

Primary SGDID	S000005780

SUMMARY PARAGRAPH for SEC63

Hsp40/DnaJ is a family of proteins, established by bacterial DnaJ, that regulates Hsp70 chaperone activity. Hsp40s stimulate the intrinsically weak ATPase activity of Hsp70 proteins and facilitate Hsp70 interaction with polypeptide substrates. Hsp70 family members often have multiple Hsp40 partners, and these specific pairings govern Hsp70 chaperone involvement in particular processes (reviewed in 7, 8, and 9). All Hsp40s contain a highly conserved 75-amino acid J domain, which interacts with the ATPase domain of Hsp70 to stimulate ATP hydrolysis. However, there are also other conserved structural domains, and based on the presence or absence of these regions, the Hsp40 family can be divided into three subtypes: type I, type II and type III (a comprehensive overview of the structural features of the different HSP40 subtypes can be found in 9). Sequence analysis of the S. cerevisiae genome has revealed 22 proteins in the Hsp40/DnaJ family: YDJ1, XDJ1, APJ1, SIS1, DJP1, ZUO1, SWA2, JJJ1, JJJ2, JJJ3, CAJ1, CWC23, MDJ1, MDJ2, PAM18, JAC1, JID1, SCJ1, HLJ1, JEM1, SEC63, and ERJ5 (9).

Last updated: 2006-12-19

References cited on this page View Complete Literature Guide for SEC63

1)	Rothblatt JA, et al. (1989) Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. J Cell Biol 109(6 Pt 1):2641-52
2)	Toyn J, et al. (1988) In vivo and in vitro analysis of ptl1, a yeast ts mutant with a membrane-associated defect in protein translocation. EMBO J 7(13):4347-53
3)	Young BP, et al. (2001) Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo. EMBO J 20(1-2):262-71
4)	Willer M, et al. (2003) Identification of novel protein-protein interactions at the cytosolic surface of the Sec63 complex in the yeast ER membrane. Yeast 20(2):133-48
5)	Misselwitz B, et al. (1999) Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex. J Biol Chem 274(29):20110-5
6)	Novick P, et al. (1980) Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21(1):205-15
7)	Qiu XB, et al. (2006) The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cell Mol Life Sci 63(22):2560-2570
8)	Cyr DM, et al. (1994) DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem Sci 19(4):176-81
9)	Walsh P, et al. (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep 5(6):567-71