SEC62_YEAST
ID SEC62_YEAST Reviewed; 274 AA.
AC P21825; D6W3S3;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Translocation protein SEC62;
DE AltName: Full=Sec62/63 complex 30 kDa subunit;
GN Name=SEC62; OrderedLocusNames=YPL094C; ORFNames=LPG14C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2687286; DOI=10.1083/jcb.109.6.2653;
RA Deshaies R.J., Schekman R.;
RT "SEC62 encodes a putative membrane protein required for protein
RT translocation into the yeast endoplasmic reticulum.";
RL J. Cell Biol. 109:2653-2664(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION IN THE SEC62/63 COMPLEX.
RX PubMed=2000150; DOI=10.1038/349806a0;
RA Deshaies R.J., Sanders S.L., Feldheim D.A., Schekman R.;
RT "Assembly of yeast Sec proteins involved in translocation into the
RT endoplasmic reticulum into a membrane-bound multisubunit complex.";
RL Nature 349:806-808(1991).
RN [5]
RP ASSOCIATION OF THE SEC62/63 COMPLEX WITH THE SEC61 COMPLEX.
RX PubMed=7758110; DOI=10.1016/0092-8674(95)90077-2;
RA Panzner S., Dreier L., Hartmann E., Kostka S., Rapoport T.A.;
RT "Posttranslational protein transport in yeast reconstituted with a purified
RT complex of Sec proteins and Kar2p.";
RL Cell 81:561-570(1995).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP ASSOCIATION WITH THE SIGNAL SEQUENCE.
RX PubMed=14617809; DOI=10.1091/mbc.e03-06-0390;
RA Plath K., Wilkinson B.M., Stirling C.J., Rapoport T.A.;
RT "Interactions between Sec complex and prepro-alpha-factor during
RT posttranslational protein transport into the endoplasmic reticulum.";
RL Mol. Biol. Cell 15:1-10(2004).
RN [8]
RP IDENTIFICATION OF N-TERMINUS, AND INTERACTION WITH SEC63.
RX PubMed=12518317; DOI=10.1002/yea.954;
RA Willer M., Jermy A.J., Young B.P., Stirling C.J.;
RT "Identification of novel protein-protein interactions at the cytosolic
RT surface of the Sec63 complex in the yeast ER membrane.";
RL Yeast 20:133-148(2003).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Acts as component of the Sec62/63 complex which is involved
CC in SRP-independent post-translational translocation across the
CC endoplasmic reticulum (ER) and functions together with the Sec61
CC complex and KAR2 in a channel-forming translocon complex. In an initial
CC step, the signal sequence seems to bind simultaneously to SEC61 and
CC SEC62. SEC62 and SEC63 are required for interactions between SEC61 and
CC translocating polypeptides. SEC62 may affect SEC1-polypeptide
CC interactions by increasing the affinity of targeting pathways for SEC61
CC and/or by modifying SEC61 to allow more efficient polypeptide
CC interaction. A cycle of assembly and disassembly of Sec62/63 complex
CC from SEC61 may govern the activity of the translocon. SEC62 is
CC essential for cell growth.
CC -!- SUBUNIT: Component of the heterotetrameric Sec62/63complex composed of
CC SEC62, SEC63, SEC71 and SEC72. The Sec62/63 complex associates with the
CC Sec61 complex to form the Sec complex. {ECO:0000269|PubMed:2000150}.
CC -!- INTERACTION:
CC P21825; P32915: SEC61; NbExp=12; IntAct=EBI-16632, EBI-16400;
CC P21825; P14906: SEC63; NbExp=7; IntAct=EBI-16632, EBI-16636;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- MISCELLANEOUS: Present with 16500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SEC62 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB68205.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB56541.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X51666; CAB56541.1; ALT_INIT; Genomic_DNA.
DR EMBL; U43281; AAB68205.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006949; DAA11339.1; -; Genomic_DNA.
DR PIR; A33617; A33617.
DR RefSeq; NP_015231.2; NM_001183908.1.
DR PDB; 6ZZZ; X-ray; 2.54 A; A/B=18-145.
DR PDB; 7AFT; EM; 4.40 A; G=1-274.
DR PDBsum; 6ZZZ; -.
DR PDBsum; 7AFT; -.
DR AlphaFoldDB; P21825; -.
DR SMR; P21825; -.
DR BioGRID; 36087; 477.
DR ComplexPortal; CPX-3055; Translocon complex.
DR ComplexPortal; CPX-3056; SEC62-SEC63 complex.
DR DIP; DIP-3827N; -.
DR IntAct; P21825; 43.
DR MINT; P21825; -.
DR STRING; 4932.YPL094C; -.
DR TCDB; 1.A.15.1.1; the non-selective cation channel-2 (nscc2) family.
DR iPTMnet; P21825; -.
DR MaxQB; P21825; -.
DR PaxDb; P21825; -.
DR PRIDE; P21825; -.
DR DNASU; 856011; -.
DR EnsemblFungi; YPL094C_mRNA; YPL094C; YPL094C.
DR GeneID; 856011; -.
DR KEGG; sce:YPL094C; -.
DR SGD; S000006015; SEC62.
DR VEuPathDB; FungiDB:YPL094C; -.
DR eggNOG; KOG2927; Eukaryota.
DR GeneTree; ENSGT00390000002757; -.
DR HOGENOM; CLU_040936_1_0_1; -.
DR InParanoid; P21825; -.
DR OMA; GLWLYPN; -.
DR BioCyc; YEAST:G3O-33998-MON; -.
DR PRO; PR:P21825; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P21825; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0031207; C:Sec62/Sec63 complex; IPI:SGD.
DR GO; GO:0071256; C:translocon complex; IPI:ComplexPortal.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IDA:SGD.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IDA:SGD.
DR InterPro; IPR004728; Sec62.
DR InterPro; IPR011553; Sec62_asco.
DR PANTHER; PTHR12443; PTHR12443; 1.
DR Pfam; PF03839; Sec62; 1.
DR TIGRFAMs; TIGR00869; sec62; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Endoplasmic reticulum; Membrane;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..274
FT /note="Translocation protein SEC62"
FT /id="PRO_0000206627"
FT TOPO_DOM 2..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..183
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 251..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:6ZZZ"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:6ZZZ"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:6ZZZ"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6ZZZ"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:6ZZZ"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:6ZZZ"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:6ZZZ"
FT HELIX 79..95
FT /evidence="ECO:0007829|PDB:6ZZZ"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:6ZZZ"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:6ZZZ"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:6ZZZ"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6ZZZ"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:6ZZZ"
SQ SEQUENCE 274 AA; 31347 MW; 2B2BA0DAAF3ACCA1 CRC64;
MSAVGPGSNA GASVNGGSAT AIATLLRNHK ELKQRQGLFQ AKQTDFFRYK RFVRALHSEE
YANKSARQPE IYPTIPSNKI EDQLKSREIF IQLIKAQMVI PVKKLHSQEC KEHGLKPSKD
FPHLIVSNKA QLEADEYFVW NYNPRTYMDY LIVIGVVSII LALVCYPLWP RSMRRGSYYV
SLGAFGILAG FFAVAILRLI LYVLSLIVYK DVGGFWIFPN LFEDCGVLES FKPLYGFGEK
DTYSYKKKLK RMKKKQAKRE SNKKKAINEK AEQN
