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 SEC63_YEAST             Reviewed;         663 AA.
 P14906; D6W2V5; Q08690;
 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
 01-NOV-1997, sequence version 2.
 18-JUL-2018, entry version 182.
 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]
 IDENTIFICATION BY MASS SPECTROMETRY.
 PubMed=14690591; DOI=10.1016/S1097-2765(03)00476-3;
 Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B.,
 Riffle M., Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H.,
 Snydsman B.E., Bradley P., Muller E.G.D., Fields S., Baker D.,
 Yates J.R. III, Davis T.N.;
 "Assigning function to yeast proteins by integration of
 technologies.";
 Mol. Cell 12:1353-1365(2003).
 [12]
 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).
 [13]
 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).
 [14]
 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).
 [15]
 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).
 [16]
 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).
 [17]
 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).
 [18]
 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).
 [19]
 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=8; IntAct=EBI-16636, EBI-16632;
     P33754:SEC66; NbExp=6; IntAct=EBI-16636, EBI-16647;
     P39742:SEC72; NbExp=6; IntAct=EBI-16636, EBI-16651;
     P40217:TIF34; NbExp=2; IntAct=EBI-16636, EBI-8951;
 -!- 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; 606.
 ComplexPortal; CPX-3055; Translocon complex.
 ComplexPortal; CPX-3056; SEC62-SEC63 complex.
 DIP; DIP-2396N; -.
 IntAct; P14906; 156.
 MINT; P14906; -.
 STRING; 4932.YOR254C; -.
 TCDB; 3.A.5.8.1; the general secretory pathway (sec) family.
 iPTMnet; P14906; -.
 MaxQB; P14906; -.
 PaxDb; 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:0030176; C:integral component of endoplasmic reticulum membrane; IEA:InterPro.
 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.
 InterPro; IPR001623; DnaJ_domain.
 InterPro; IPR018253; DnaJ_domain_CS.
 InterPro; IPR014756; Ig_E-set.
 InterPro; IPR036869; J_dom_sf.
 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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