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Protein translocation protein SEC63 (Protein NPL1) (Sec62/63 complex 73 kDa subunit)

 SEC63_YEAST             Reviewed;         663 AA.
P14906; D6W2V5; Q08690;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
25-OCT-2017, entry version 176.
RecName: Full=Protein translocation protein SEC63;
AltName: Full=Protein NPL1;
AltName: Full=Sec62/63 complex 73 kDa subunit;
Name=SEC63; Synonyms=NPL1, PTL1; OrderedLocusNames=YOR254C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2556404; DOI=10.1083/jcb.109.6.2665;
Sadler I., Chiang A., Kurihara T., Rothblatt J.A., Way J.,
Silver P.A.;
"A yeast gene important for protein assembly into the endoplasmic
reticulum and the nucleus has homology to DnaJ, an Escherichia coli
heat shock protein.";
J. Cell Biol. 109:2665-2675(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9153759;
DOI=10.1002/(SICI)1097-0061(199704)13:5<483::AID-YEA105>3.0.CO;2-U;
Poirey R., Jauniaux J.-C.;
"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.";
Yeast 13:483-487(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
IDENTIFICATION IN THE SEC62/63 COMPLEX.
PubMed=2000150; DOI=10.1038/349806a0;
Deshaies R.J., Sanders S.L., Feldheim D.A., Schekman R.;
"Assembly of yeast Sec proteins involved in translocation into the
endoplasmic reticulum into a membrane-bound multisubunit complex.";
Nature 349:806-808(1991).
[6]
IDENTIFICATION IN THE SEC62/63 COMPLEX.
PubMed=1620130; DOI=10.1128/MCB.12.7.3288;
Feldheim D., Rothblatt J., Schekman R.;
"Topology and functional domains of Sec63p, an endoplasmic reticulum
membrane protein required for secretory protein translocation.";
Mol. Cell. Biol. 12:3288-3296(1992).
[7]
MUTAGENESIS.
PubMed=8514125;
Nelson M.K., Kurihara T., Silver P.A.;
"Extragenic suppressors of mutations in the cytoplasmic C-terminus of
SEC63 define five genes in Saccharomyces cerevisiae.";
Genetics 134:159-173(1993).
[8]
IDENTIFICATION IN A COMPLEX WITH KAR2; SEC66 AND SEC72.
PubMed=8253836; DOI=10.1083/jcb.123.6.1355;
Brodsky J.L., Schekman R.;
"A Sec63p-BiP complex from yeast is required for protein translocation
in a reconstituted proteoliposome.";
J. Cell Biol. 123:1355-1363(1993).
[9]
ASSOCIATION OF THE SEC62/63 COMPLEX WITH THE SEC61 COMPLEX.
PubMed=7758110; DOI=10.1016/0092-8674(95)90077-2;
Panzner S., Dreier L., Hartmann E., Kostka S., Rapoport T.A.;
"Posttranslational protein transport in yeast reconstituted with a
purified complex of Sec proteins and Kar2p.";
Cell 81:561-570(1995).
[10]
FUNCTION.
PubMed=11226176; DOI=10.1093/emboj/20.1.262;
Young B.P., Craven R.A., Reid P.J., Willer M., Stirling C.J.;
"Sec63p and Kar2p are required for the translocation of SRP-dependent
precursors into the yeast endoplasmic reticulum in vivo.";
EMBO J. 20:262-271(2001).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
INTERACTION WITH SEC63.
PubMed=12518317; DOI=10.1002/yea.954;
Willer M., Jermy A.J., Young B.P., Stirling C.J.;
"Identification of novel protein-protein interactions at the cytosolic
surface of the Sec63 complex in the yeast ER membrane.";
Yeast 20:133-148(2003).
[13]
PHOSPHORYLATION BY CASEIN KINASE II, INTERACTION WITH SEC63, AND
MUTAGENESIS OF THR-652 AND THR-654.
PubMed=15671059; DOI=10.1242/jcs.01671;
Wang X., Johnsson N.;
"Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of
the endoplasmic reticulum protein translocation apparatus.";
J. Cell Sci. 118:723-732(2005).
[14]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
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.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: 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. {ECO:0000269|PubMed:11226176}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:12518317, ECO:0000269|PubMed:15671059,
ECO:0000269|PubMed:1620130, ECO:0000269|PubMed:2000150,
ECO:0000269|PubMed:8253836}.
-!- INTERACTION:
P21825:SEC62; NbExp=7; IntAct=EBI-16636, EBI-16632;
P33754:SEC66; NbExp=4; IntAct=EBI-16636, EBI-16647;
P39742:SEC72; NbExp=4; IntAct=EBI-16636, EBI-16651;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein. Nucleus membrane; Multi-pass membrane protein.
Nucleus inner membrane; Multi-pass membrane protein.
-!- PTM: Phosphotylated by casein kinase II.
-!- MISCELLANEOUS: Present with 17700 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; X16388; CAA34424.1; -; Genomic_DNA.
EMBL; Z75162; CAA99476.1; -; Genomic_DNA.
EMBL; BK006948; DAA11021.1; -; Genomic_DNA.
PIR; A33618; A33618.
RefSeq; NP_014897.1; NM_001183673.1.
ProteinModelPortal; P14906; -.
SMR; P14906; -.
BioGrid; 34644; 605.
DIP; DIP-2396N; -.
IntAct; P14906; 18.
MINT; MINT-666868; -.
STRING; 4932.YOR254C; -.
TCDB; 3.A.5.8.1; the general secretory pathway (sec) family.
iPTMnet; P14906; -.
MaxQB; P14906; -.
PRIDE; P14906; -.
EnsemblFungi; YOR254C; YOR254C; YOR254C.
GeneID; 854428; -.
KEGG; sce:YOR254C; -.
EuPathDB; FungiDB:YOR254C; -.
SGD; S000005780; SEC63.
GeneTree; ENSGT00390000001965; -.
HOGENOM; HOG000248842; -.
InParanoid; P14906; -.
KO; K09540; -.
OMA; RIVAKCH; -.
OrthoDB; EOG092C20BT; -.
BioCyc; YEAST:G3O-33745-MONOMER; -.
Reactome; R-SCE-381038; XBP1(S) activates chaperone genes.
PRO; PR:P14906; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0031207; C:Sec62/Sec63 complex; IPI:SGD.
GO; GO:0008565; F:protein transporter activity; IDA:SGD.
GO; GO:0046967; P:cytosol to ER transport; IMP:SGD.
GO; GO:0006620; P:posttranslational protein targeting to endoplasmic reticulum membrane; IMP:SGD.
GO; GO:0031204; P:posttranslational protein targeting to membrane, translocation; IDA:SGD.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IMP:SGD.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR036869; DnaJ_dom_sf.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR027137; Sec63.
InterPro; IPR004179; Sec63-dom.
PANTHER; PTHR24075:SF0; PTHR24075:SF0; 1.
Pfam; PF00226; DnaJ; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SMART; SM00973; Sec63; 1.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF81296; SSF81296; 3.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
1: Evidence at protein level;
Chaperone; Complete proteome; Endoplasmic reticulum; Membrane;
Nucleus; Phosphoprotein; Protein transport; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 663 Protein translocation protein SEC63.
/FTId=PRO_0000071095.
TOPO_DOM 1 13 Lumenal. {ECO:0000255}.
TRANSMEM 14 41 Helical. {ECO:0000255}.
TOPO_DOM 42 92 Cytoplasmic. {ECO:0000255}.
TRANSMEM 93 108 Helical. {ECO:0000255}.
TOPO_DOM 109 220 Lumenal. {ECO:0000255}.
TRANSMEM 221 239 Helical. {ECO:0000255}.
TOPO_DOM 240 663 Cytoplasmic. {ECO:0000255}.
DOMAIN 123 198 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
DOMAIN 228 532 SEC63.
REPEAT 461 471 1.
REPEAT 493 503 2.
REGION 461 503 2 X 11 AA repeats.
COMPBIAS 612 663 Asp/Glu-rich (highly acidic).
MOD_RES 512 512 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MUTAGEN 179 179 A->T: Temperature-sensitive.
{ECO:0000269|PubMed:8514125}.
MUTAGEN 426 426 P->L: Temperature-sensitive.
{ECO:0000269|PubMed:8514125}.
MUTAGEN 431 431 I->N: Temperature-sensitive.
{ECO:0000269|PubMed:8514125}.
MUTAGEN 503 503 P->A: Temperature-sensitive.
{ECO:0000269|PubMed:8514125}.
MUTAGEN 511 511 G->R: Temperature-sensitive.
{ECO:0000269|PubMed:8514125}.
MUTAGEN 652 652 T->A: Abolishes interaction with SEC62;
defect in protein translocation.
{ECO:0000269|PubMed:15671059}.
MUTAGEN 654 654 T->A: Abolishes interaction with SEC62;
defect in protein translocation.
{ECO:0000269|PubMed:15671059}.
CONFLICT 263 263 V -> I (in Ref. 1; CAA34424).
{ECO:0000305}.
CONFLICT 293 293 F -> L (in Ref. 1; CAA34424).
{ECO:0000305}.
SEQUENCE 663 AA; 75345 MW; 7D6757144C8A301F CRC64;
MPTNYEYDEA SETWPSFILT GLLMVVGPMT LLQIYQIFFG ANAEDGNSGK SKEFNEEVFK
NLNEEYTSDE IKQFRRKFDK NSNKKSKIWS RRNIIIIVGW ILVAILLQRI NSNDAIKDAA
TKLFDPYEIL GISTSASDRD IKSAYRKLSV KFHPDKLAKG LTPDEKSVME ETYVQITKAY
ESLTDELVRQ NYLKYGHPDG PQSTSHGIAL PRFLVDGSAS PLLVVCYVAL LGLILPYFVS
RWWARTQSYT KKGIHNVTAS NFVSNLVNYK PSEIVTTDLI LHWLSFAHEF KQFFPDLQPT
DFEKLLQDHI NRRDSGKLNN AKFRIVAKCH SLLHGLLDIA CGFRNLDIAL GAINTFKCIV
QAVPLTPNCQ ILQLPNVDKE HFITKTGDIH TLGKLFTLED AKIGEVLGIK DQAKLNETLR
VASHIPNLKI IKADFLVPGE NQVTPSSTPY ISLKVLVRSA KQPLIPTSLI PEENLTEPQD
FESQRDPFAM MSKQPLVPYS FAPFFPTKRR GSWCCLVSSQ KDGKILQTPI IIEKLSYKNL
NDDKDFFDKR IKMDLTKHEK FDINDWEIGT IKIPLGQPAP ETVGDFFFRV IVKSTDYFTT
DLDITMNMKV RDSPAVEQVE VYSEEDDEYS TDDDETESDD ESDASDYTDI DTDTEAEDDE
SPE


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