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Protein

Protein translocation protein SEC63

Gene

SEC63

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC63 may affect SEC1-polypeptide interactions by increasing the affinity of targeting pathways for SEC61 and/or by modifying SEC61 to allow more efficient polypeptide interaction. May also be involved in SRP-dependent cotranslational translocation. Is essential for cell growth and for germination.1 Publication

GO - Molecular functioni

  • protein transporter activity Source: SGD

GO - Biological processi

  • cytosol to ER transport Source: SGD
  • posttranslational protein targeting to membrane Source: SGD
  • posttranslational protein targeting to membrane, translocation Source: SGD
  • SRP-dependent cotranslational protein targeting to membrane Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33745-MONOMER.
ReactomeiR-SCE-381038. XBP1(S) activates chaperone genes.

Protein family/group databases

TCDBi3.A.5.8.1. the general secretory pathway (sec) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocation protein SEC63
Alternative name(s):
Protein NPL1
Sec62/63 complex 73 kDa subunit
Gene namesi
Name:SEC63
Synonyms:NPL1, PTL1
Ordered Locus Names:YOR254C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR254C.
SGDiS000005780. SEC63.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313LumenalSequence analysisAdd
BLAST
Transmembranei14 – 4128HelicalSequence analysisAdd
BLAST
Topological domaini42 – 9251CytoplasmicSequence analysisAdd
BLAST
Transmembranei93 – 10816HelicalSequence analysisAdd
BLAST
Topological domaini109 – 220112LumenalSequence analysisAdd
BLAST
Transmembranei221 – 23919HelicalSequence analysisAdd
BLAST
Topological domaini240 – 663424CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • nuclear inner membrane Source: UniProtKB-SubCell
  • Sec62/Sec63 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi179 – 1791A → T: Temperature-sensitive. 1 Publication
Mutagenesisi426 – 4261P → L: Temperature-sensitive. 1 Publication
Mutagenesisi431 – 4311I → N: Temperature-sensitive. 1 Publication
Mutagenesisi503 – 5031P → A: Temperature-sensitive. 1 Publication
Mutagenesisi511 – 5111G → R: Temperature-sensitive. 1 Publication
Mutagenesisi652 – 6521T → A: Abolishes interaction with SEC62; defect in protein translocation. 1 Publication
Mutagenesisi654 – 6541T → A: Abolishes interaction with SEC62; defect in protein translocation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 663663Protein translocation protein SEC63PRO_0000071095Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei512 – 5121PhosphoserineCombined sources

Post-translational modificationi

Phosphotylated by casein kinase II.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP14906.
PeptideAtlasiP14906.

PTM databases

iPTMnetiP14906.

Interactioni

Subunit structurei

Component of the heterotetrameric Sec62/63complex composed of SEC62, SEC63, SEC66 and SEC72. The Sec62/63 complex associates with the Sec61 complex to form the Sec complex. SEC63 interacts in its phosphorylated form with SEC62. May physically associate with KAR2 in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis. Part of a complex consisting of KAR2, SEC63, SEC66 and SEC72.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SEC62P218258EBI-16636,EBI-16632
SEC66P337545EBI-16636,EBI-16647
SEC72P397424EBI-16636,EBI-16651

Protein-protein interaction databases

BioGridi34644. 261 interactions.
DIPiDIP-2396N.
IntActiP14906. 18 interactions.
MINTiMINT-666868.

Structurei

3D structure databases

ProteinModelPortaliP14906.
SMRiP14906. Positions 124-203.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini123 – 19876JPROSITE-ProRule annotationAdd
BLAST
Domaini228 – 532305SEC63Add
BLAST
Repeati461 – 471111Add
BLAST
Repeati493 – 503112Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni461 – 503432 X 11 AA repeatsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi612 – 66352Asp/Glu-rich (highly acidic)Add
BLAST

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation
Contains 1 SEC63 domain.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000001965.
HOGENOMiHOG000248842.
InParanoidiP14906.
KOiK09540.
OMAiCDSYIGF.
OrthoDBiEOG72VHFN.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR014756. Ig_E-set.
IPR004179. Sec63-dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF02889. Sec63. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
SM00973. Sec63. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF81296. SSF81296. 3 hits.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14906-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTNYEYDEA SETWPSFILT GLLMVVGPMT LLQIYQIFFG ANAEDGNSGK
60 70 80 90 100
SKEFNEEVFK NLNEEYTSDE IKQFRRKFDK NSNKKSKIWS RRNIIIIVGW
110 120 130 140 150
ILVAILLQRI NSNDAIKDAA TKLFDPYEIL GISTSASDRD IKSAYRKLSV
160 170 180 190 200
KFHPDKLAKG LTPDEKSVME ETYVQITKAY ESLTDELVRQ NYLKYGHPDG
210 220 230 240 250
PQSTSHGIAL PRFLVDGSAS PLLVVCYVAL LGLILPYFVS RWWARTQSYT
260 270 280 290 300
KKGIHNVTAS NFVSNLVNYK PSEIVTTDLI LHWLSFAHEF KQFFPDLQPT
310 320 330 340 350
DFEKLLQDHI NRRDSGKLNN AKFRIVAKCH SLLHGLLDIA CGFRNLDIAL
360 370 380 390 400
GAINTFKCIV QAVPLTPNCQ ILQLPNVDKE HFITKTGDIH TLGKLFTLED
410 420 430 440 450
AKIGEVLGIK DQAKLNETLR VASHIPNLKI IKADFLVPGE NQVTPSSTPY
460 470 480 490 500
ISLKVLVRSA KQPLIPTSLI PEENLTEPQD FESQRDPFAM MSKQPLVPYS
510 520 530 540 550
FAPFFPTKRR GSWCCLVSSQ KDGKILQTPI IIEKLSYKNL NDDKDFFDKR
560 570 580 590 600
IKMDLTKHEK FDINDWEIGT IKIPLGQPAP ETVGDFFFRV IVKSTDYFTT
610 620 630 640 650
DLDITMNMKV RDSPAVEQVE VYSEEDDEYS TDDDETESDD ESDASDYTDI
660
DTDTEAEDDE SPE
Length:663
Mass (Da):75,345
Last modified:November 1, 1997 - v2
Checksum:i7D6757144C8A301F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti263 – 2631V → I in CAA34424 (PubMed:2556404).Curated
Sequence conflicti293 – 2931F → L in CAA34424 (PubMed:2556404).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16388 Genomic DNA. Translation: CAA34424.1.
Z75162 Genomic DNA. Translation: CAA99476.1.
BK006948 Genomic DNA. Translation: DAA11021.1.
PIRiA33618.
RefSeqiNP_014897.1. NM_001183673.1.

Genome annotation databases

EnsemblFungiiYOR254C; YOR254C; YOR254C.
GeneIDi854428.
KEGGisce:YOR254C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16388 Genomic DNA. Translation: CAA34424.1.
Z75162 Genomic DNA. Translation: CAA99476.1.
BK006948 Genomic DNA. Translation: DAA11021.1.
PIRiA33618.
RefSeqiNP_014897.1. NM_001183673.1.

3D structure databases

ProteinModelPortaliP14906.
SMRiP14906. Positions 124-203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34644. 261 interactions.
DIPiDIP-2396N.
IntActiP14906. 18 interactions.
MINTiMINT-666868.

Protein family/group databases

TCDBi3.A.5.8.1. the general secretory pathway (sec) family.

PTM databases

iPTMnetiP14906.

Proteomic databases

MaxQBiP14906.
PeptideAtlasiP14906.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR254C; YOR254C; YOR254C.
GeneIDi854428.
KEGGisce:YOR254C.

Organism-specific databases

EuPathDBiFungiDB:YOR254C.
SGDiS000005780. SEC63.

Phylogenomic databases

GeneTreeiENSGT00390000001965.
HOGENOMiHOG000248842.
InParanoidiP14906.
KOiK09540.
OMAiCDSYIGF.
OrthoDBiEOG72VHFN.

Enzyme and pathway databases

BioCyciYEAST:G3O-33745-MONOMER.
ReactomeiR-SCE-381038. XBP1(S) activates chaperone genes.

Miscellaneous databases

NextBioi976649.
PROiP14906.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR014756. Ig_E-set.
IPR004179. Sec63-dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF02889. Sec63. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
SM00973. Sec63. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF81296. SSF81296. 3 hits.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein."
    Sadler I., Chiang A., Kurihara T., Rothblatt J.A., Way J., Silver P.A.
    J. Cell Biol. 109:2665-2675(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1 and VPH1."
    Poirey R., Jauniaux J.-C.
    Yeast 13:483-487(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex."
    Deshaies R.J., Sanders S.L., Feldheim D.A., Schekman R.
    Nature 349:806-808(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SEC62/63 COMPLEX.
  6. "Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation."
    Feldheim D., Rothblatt J., Schekman R.
    Mol. Cell. Biol. 12:3288-3296(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SEC62/63 COMPLEX.
  7. "Extragenic suppressors of mutations in the cytoplasmic C-terminus of SEC63 define five genes in Saccharomyces cerevisiae."
    Nelson M.K., Kurihara T., Silver P.A.
    Genetics 134:159-173(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  8. "A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome."
    Brodsky J.L., Schekman R.
    J. Cell Biol. 123:1355-1363(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH KAR2; SEC66 AND SEC72.
  9. "Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p."
    Panzner S., Dreier L., Hartmann E., Kostka S., Rapoport T.A.
    Cell 81:561-570(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF THE SEC62/63 COMPLEX WITH THE SEC61 COMPLEX.
  10. "Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo."
    Young B.P., Craven R.A., Reid P.J., Willer M., Stirling C.J.
    EMBO J. 20:262-271(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "Identification of novel protein-protein interactions at the cytosolic surface of the Sec63 complex in the yeast ER membrane."
    Willer M., Jermy A.J., Young B.P., Stirling C.J.
    Yeast 20:133-148(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SEC63.
  13. "Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of the endoplasmic reticulum protein translocation apparatus."
    Wang X., Johnsson N.
    J. Cell Sci. 118:723-732(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CASEIN KINASE II, INTERACTION WITH SEC63, MUTAGENESIS OF THR-652 AND THR-654.
  14. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  15. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  16. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSEC63_YEAST
AccessioniPrimary (citable) accession number: P14906
Secondary accession number(s): D6W2V5, Q08690
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 17700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.