SEC66_YEAST
ID SEC66_YEAST Reviewed; 206 AA.
AC P33754; D6VQG7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Translocation protein SEC66;
DE AltName: Full=Protein HSS1;
DE AltName: Full=Sec62/63 complex 31.5 kDa subunit;
GN Name=SEC66; Synonyms=HSS1, SEC71; OrderedLocusNames=YBR171W;
GN ORFNames=YBR1232;
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], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION IN THE SEC62/63 COMPLEX.
RX PubMed=8257795; DOI=10.1091/mbc.4.9.931;
RA Feldheim D., Yoshimura K., Admon A., Schekman R.;
RT "Structural and functional characterization of Sec66p, a new subunit of the
RT polypeptide translocation apparatus in the yeast endoplasmic reticulum.";
RL Mol. Biol. Cell 4:931-939(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8257794; DOI=10.1091/mbc.4.9.919;
RA Kurihara T., Silver P.A.;
RT "Suppression of a sec63 mutation identifies a novel component of the yeast
RT endoplasmic reticulum translocation apparatus.";
RL Mol. Biol. Cell 4:919-930(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8212898; DOI=10.1002/yea.320090811;
RA Schaaff-Gerstenschlaeger I., Bauer A., Boles E., Zimmermann F.K.;
RT "Sequence and function analysis of a 4.3 kb fragment of Saccharomyces
RT cerevisiae chromosome II including three open reading frames.";
RL Yeast 9:915-921(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
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 [8]
RP IDENTIFICATION IN A COMPLEX WITH KAR2; SEC63 AND SEC72.
RX PubMed=8253836; DOI=10.1083/jcb.123.6.1355;
RA Brodsky J.L., Schekman R.;
RT "A Sec63p-BiP complex from yeast is required for protein translocation in a
RT reconstituted proteoliposome.";
RL J. Cell Biol. 123:1355-1363(1993).
RN [9]
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 [10]
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).
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. A cycle of
CC assembly and disassembly of Sec62/63 complex from SEC61 may govern the
CC activity of the translocon. SEC66 is required to attach or retain SEC72
CC in the SEC63 complex. It is essential for growth at elevated
CC temperatures.
CC -!- SUBUNIT: Component of the heterotetrameric Sec62/63complex composed of
CC SEC62, SEC63, SEC66 and SEC72. The Sec62/63 complex associates with the
CC Sec61 complex to form the Sec complex. Part of a complex consisting of
CC KAR2, SEC63, SEC66 and SEC72. {ECO:0000269|PubMed:2000150,
CC ECO:0000269|PubMed:8253836, ECO:0000269|PubMed:8257795}.
CC -!- INTERACTION:
CC P33754; P32915: SEC61; NbExp=11; IntAct=EBI-16647, EBI-16400;
CC P33754; P14906: SEC63; NbExp=4; IntAct=EBI-16647, EBI-16636;
CC P33754; P39742: SEC72; NbExp=5; IntAct=EBI-16647, EBI-16651;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8257795}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:8257795}.
CC -!- MISCELLANEOUS: Present with 7820 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: To S.pombe SpBC409.21. {ECO:0000305}.
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DR EMBL; U00797; AAA18910.1; -; Unassigned_DNA.
DR EMBL; X72224; CAA51025.1; -; Genomic_DNA.
DR EMBL; X74437; CAA52451.1; -; Genomic_DNA.
DR EMBL; Z36040; CAA85132.1; -; Genomic_DNA.
DR EMBL; AY558125; AAS56451.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07287.1; -; Genomic_DNA.
DR PIR; A47735; A47735.
DR RefSeq; NP_009730.3; NM_001178519.3.
DR PDB; 6N3Q; EM; 3.68 A; E=1-206.
DR PDB; 6ND1; EM; 4.10 A; E=1-206.
DR PDB; 7AFT; EM; 4.40 A; E=1-206.
DR PDB; 7KAH; EM; 3.10 A; E=1-206.
DR PDB; 7KAI; EM; 3.20 A; E=1-206.
DR PDB; 7KAJ; EM; 3.10 A; E=1-206.
DR PDB; 7KAO; EM; 4.00 A; E=1-206.
DR PDB; 7KAP; EM; 4.10 A; E=1-206.
DR PDB; 7KAQ; EM; 4.00 A; E=1-206.
DR PDB; 7KAR; EM; 4.00 A; E=1-206.
DR PDB; 7KAS; EM; 3.90 A; E=1-206.
DR PDB; 7KAT; EM; 4.40 A; E=1-206.
DR PDB; 7KAU; EM; 4.00 A; E=1-206.
DR PDB; 7KB5; EM; 3.80 A; E=1-206.
DR PDBsum; 6N3Q; -.
DR PDBsum; 6ND1; -.
DR PDBsum; 7AFT; -.
DR PDBsum; 7KAH; -.
DR PDBsum; 7KAI; -.
DR PDBsum; 7KAJ; -.
DR PDBsum; 7KAO; -.
DR PDBsum; 7KAP; -.
DR PDBsum; 7KAQ; -.
DR PDBsum; 7KAR; -.
DR PDBsum; 7KAS; -.
DR PDBsum; 7KAT; -.
DR PDBsum; 7KAU; -.
DR PDBsum; 7KB5; -.
DR AlphaFoldDB; P33754; -.
DR SMR; P33754; -.
DR BioGRID; 32871; 588.
DR ComplexPortal; CPX-3055; Translocon complex.
DR ComplexPortal; CPX-3056; SEC62-SEC63 complex.
DR DIP; DIP-1694N; -.
DR IntAct; P33754; 13.
DR MINT; P33754; -.
DR STRING; 4932.YBR171W; -.
DR TCDB; 3.A.5.8.1; the general secretory pathway (sec) family.
DR iPTMnet; P33754; -.
DR MaxQB; P33754; -.
DR PaxDb; P33754; -.
DR PRIDE; P33754; -.
DR EnsemblFungi; YBR171W_mRNA; YBR171W; YBR171W.
DR GeneID; 852469; -.
DR KEGG; sce:YBR171W; -.
DR SGD; S000000375; SEC66.
DR VEuPathDB; FungiDB:YBR171W; -.
DR eggNOG; KOG4699; Eukaryota.
DR HOGENOM; CLU_066294_1_1_1; -.
DR InParanoid; P33754; -.
DR OMA; WQRYQNE; -.
DR BioCyc; YEAST:G3O-29119-MON; -.
DR PRO; PR:P33754; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P33754; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0030447; P:filamentous growth; IMP:SGD.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IDA:SGD.
DR InterPro; IPR018624; Sec66.
DR PANTHER; PTHR28229; PTHR28229; 1.
DR Pfam; PF09802; Sec66; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Protein transport; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..206
FT /note="Translocation protein SEC66"
FT /id="PRO_0000097663"
FT TOPO_DOM 1..27
FT /note="Lumenal"
FT TRANSMEM 28..48
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 49..206
FT /note="Cytoplasmic"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 90..123
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 129..155
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 161..181
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:7KAH"
SQ SEQUENCE 206 AA; 24231 MW; E2A8BB4994A227D4 CRC64;
MSEFNETKFS NNGTFFETEE PIVETKSISV YTPLIYVFIL VVSLVMFASS YRKKQAKKIS
EQPSIFDEND AHDLYFQIKE MSENEKIHEK VLKAALLNRG AESVRRSLKL KELAPQINLL
YKNGSIGEDY WKRFETEVKL IELEFKDTLQ EAERLQPGWV QLFVMVCKEI CFNQALSRRY
QSILKRKEVC IKEWELKINN DGRLVN
