SC61G_YEAST
ID SC61G_YEAST Reviewed; 80 AA.
AC P35179; D6VS73;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Protein transport protein SSS1;
DE AltName: Full=Sec61 complex subunit SSS1;
DE AltName: Full=Sec61 complex subunit gamma;
DE AltName: Full=Ssh1 complex subunit SSS1;
DE AltName: Full=Ssh1 complex subunit gamma;
GN Name=SSS1; OrderedLocusNames=YDR086C; ORFNames=D4475;
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=8223425; DOI=10.1002/j.1460-2075.1993.tb06092.x;
RA Esnault Y., Blondel M.-O., Deshaies R.J., Schekman R., Kepes F.;
RT "The yeast SSS1 gene is essential for secretory protein translocation and
RT encodes a conserved protein of the endoplasmic reticulum.";
RL EMBO J. 12:4083-4093(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [5]
RP ELECTRON MICROSCOPY OF THE SEC61 COMPLEX.
RX PubMed=8929540; DOI=10.1016/s0092-8674(00)81391-4;
RA Hanein D., Matlack K.E., Jungnickel B., Plath K., Kalies K.-U.,
RA Miller K.R., Rapoport T.A., Akey C.W.;
RT "Oligomeric rings of the Sec61p complex induced by ligands required for
RT protein translocation.";
RL Cell 87:721-732(1996).
RN [6]
RP TRANSLOCON COMPLEX PORE.
RX PubMed=9160745; DOI=10.1016/s0092-8674(00)80235-4;
RA Hamman B.D., Chen J.C., Johnson E.E., Johnson A.E.;
RT "The aqueous pore through the translocon has a diameter of 40-60 A during
RT cotranslational protein translocation at the ER membrane.";
RL Cell 89:535-544(1997).
RN [7]
RP REVIEW ON THE TRANSLOCON COMPLEX.
RX PubMed=10611978; DOI=10.1146/annurev.cellbio.15.1.799;
RA Johnson A.E., van Waes M.A.;
RT "The translocon: a dynamic gateway at the ER membrane.";
RL Annu. Rev. Cell Dev. Biol. 15:799-842(1999).
RN [8]
RP ASSOCIATION OF THE SEC61 COMPLEX WITH RIBOSOMES.
RX PubMed=10775273; DOI=10.1093/emboj/19.8.1900;
RA Prinz A., Behrens C., Rapoport T.A., Hartmann E., Kalies K.-U.;
RT "Evolutionarily conserved binding of ribosomes to the translocation channel
RT via the large ribosomal RNA.";
RL EMBO J. 19:1900-1906(2000).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP INTERACTION WITH OST1; OST4; SWP1 AND WBP1.
RX PubMed=15831493; DOI=10.1074/jbc.m502858200;
RA Chavan M., Yan A., Lennarz W.J.;
RT "Subunits of the translocon interact with components of the oligosaccharyl
RT transferase complex.";
RL J. Biol. Chem. 280:22917-22924(2005).
CC -!- FUNCTION: Part of the Sec61 complex, which is the major component of
CC channel-forming translocon complex that mediates protein translocation
CC across the endoplasmic reticulum (ER). The functional states of the
CC translocon complex include co- and post-translational ER import,
CC cotranslational membrane protein integration and retrograde transport
CC of misfolded proteins out of the ER. In the cotranslational pathway,
CC ribosomes synthesizing presecretory proteins are targeted to the
CC translocon by the cytosolic signal recognition particle (SRP) and its
CC ER-localized receptor. The association of the Sec61 complex with the
CC ribosome is mediated by the 28S rRNA of the large ribosomal subunit.
CC SRP-independent post-translational translocation requires the
CC association of additional factors, such as the Sec62/63 complex and
CC KAR2. Also part of the Ssh1 complex, which probably is the major
CC component of a channel-forming translocon complex that may function
CC exclusively in the cotranslational pathway of protein ER import.
CC -!- SUBUNIT: Component of the heterotrimeric Sec61 complex, which is
CC composed of SSH1, SBH1 and SSS1. Presumably three to four Sec61
CC heterotrimers assemble into an oligomeric ring with a central aqueous
CC pore. In cotranslational ER import, the pore diameter varies from 9-15
CC A in a ribosome-free resting state to 40-60 A in a functional state
CC when associated with the ribosome. The Sec61 complex is part of a
CC channel-forming translocon complex whose composition seem to change
CC dependent upon different functional states. During post-translational
CC ER import the Sec61 complex associates with the Sec62/63 complex to
CC form the Sec complex. SSH1 is a component of the heterotrimeric Ssh1
CC complex, which is composed of SSH1, SBH2 and SSS1. SSS1 interacts with
CC OST1, OST4, SWP1 and WBP1, components of the OT complex.
CC {ECO:0000269|PubMed:15831493}.
CC -!- INTERACTION:
CC P35179; P41543: OST1; NbExp=2; IntAct=EBI-16406, EBI-12651;
CC P35179; Q99380: OST4; NbExp=2; IntAct=EBI-16406, EBI-12689;
CC P35179; P32915: SEC61; NbExp=17; IntAct=EBI-16406, EBI-16400;
CC P35179; P38353: SSH1; NbExp=8; IntAct=EBI-16406, EBI-18175;
CC P35179; Q02795: SWP1; NbExp=2; IntAct=EBI-16406, EBI-12666;
CC P35179; P33767: WBP1; NbExp=2; IntAct=EBI-16406, EBI-12658;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Single-pass membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000305}.
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DR EMBL; Z46796; CAA86808.1; -; Genomic_DNA.
DR EMBL; X74499; CAA52608.1; -; Genomic_DNA.
DR EMBL; X82086; CAA57615.1; -; Genomic_DNA.
DR EMBL; Z74382; CAA98906.1; -; Genomic_DNA.
DR EMBL; AY557659; AAS55985.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11933.1; -; Genomic_DNA.
DR PIR; S48775; S48775.
DR RefSeq; NP_010371.1; NM_001180394.1.
DR PDB; 2WW9; EM; 8.60 A; B=1-80.
DR PDB; 2WWA; EM; 8.90 A; B=1-80.
DR PDB; 6N3Q; EM; 3.68 A; C=1-80.
DR PDB; 6ND1; EM; 4.10 A; C=1-80.
DR PDB; 7AFT; EM; 4.40 A; C=1-80.
DR PDB; 7KAH; EM; 3.10 A; C=1-80.
DR PDB; 7KAI; EM; 3.20 A; C=1-80.
DR PDB; 7KAJ; EM; 3.10 A; C=1-80.
DR PDB; 7KAO; EM; 4.00 A; C=1-80.
DR PDB; 7KAP; EM; 4.10 A; C=1-80.
DR PDB; 7KAQ; EM; 4.00 A; C=1-80.
DR PDB; 7KAR; EM; 4.00 A; C=1-80.
DR PDB; 7KAS; EM; 3.90 A; C=1-80.
DR PDB; 7KAT; EM; 4.40 A; C=1-80.
DR PDB; 7KAU; EM; 4.00 A; C=1-80.
DR PDB; 7KB5; EM; 3.80 A; C=1-80.
DR PDBsum; 2WW9; -.
DR PDBsum; 2WWA; -.
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; P35179; -.
DR SMR; P35179; -.
DR BioGRID; 32142; 302.
DR ComplexPortal; CPX-1833; SEC61 translocon complex.
DR ComplexPortal; CPX-1834; SSH1 translocon complex.
DR ComplexPortal; CPX-3055; Translocon complex.
DR DIP; DIP-2432N; -.
DR IntAct; P35179; 16.
DR MINT; P35179; -.
DR STRING; 4932.YDR086C; -.
DR TCDB; 3.A.5.8.1; the general secretory pathway (sec) family.
DR iPTMnet; P35179; -.
DR MaxQB; P35179; -.
DR PaxDb; P35179; -.
DR PRIDE; P35179; -.
DR TopDownProteomics; P35179; -.
DR EnsemblFungi; YDR086C_mRNA; YDR086C; YDR086C.
DR GeneID; 851659; -.
DR KEGG; sce:YDR086C; -.
DR SGD; S000002493; SSS1.
DR VEuPathDB; FungiDB:YDR086C; -.
DR eggNOG; KOG3498; Eukaryota.
DR GeneTree; ENSGT00390000001319; -.
DR HOGENOM; CLU_167752_2_0_1; -.
DR InParanoid; P35179; -.
DR OMA; RDGNQFL; -.
DR BioCyc; YEAST:G3O-29691-MON; -.
DR Reactome; R-SCE-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR EvolutionaryTrace; P35179; -.
DR PRO; PR:P35179; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P35179; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:SGD.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0005784; C:Sec61 translocon complex; IDA:SGD.
DR GO; GO:0071261; C:Ssh1 translocon complex; IDA:SGD.
DR GO; GO:0071256; C:translocon complex; IPI:ComplexPortal.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IDA:SGD.
DR GO; GO:0005198; F:structural molecule activity; IMP:SGD.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IDA:SGD.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IC:ComplexPortal.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IMP:SGD.
DR Gene3D; 1.20.5.820; -; 1.
DR HAMAP; MF_00422; SecE; 1.
DR InterPro; IPR023391; Prot_translocase_SecE_dom_sf.
DR InterPro; IPR008158; Translocase_Sec61-g.
DR InterPro; IPR001901; Translocase_SecE/Sec61-g.
DR Pfam; PF00584; SecE; 1.
DR SUPFAM; SSF103456; SSF103456; 1.
DR TIGRFAMs; TIGR00327; secE_euk_arch; 1.
DR PROSITE; PS01067; SECE_SEC61G; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..80
FT /note="Protein transport protein SSS1"
FT /id="PRO_0000104211"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..80
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CONFLICT 58
FT /note="F -> L (in Ref. 1; CAA52608)"
FT /evidence="ECO:0000305"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 44..79
FT /evidence="ECO:0007829|PDB:7KAH"
SQ SEQUENCE 80 AA; 8944 MW; 340F2EA913850D85 CRC64;
MARASEKGEE KKQSNNQVEK LVEAPVEFVR EGTQFLAKCK KPDLKEYTKI VKAVGIGFIA
VGIIGYAIKL IHIPIRYVIV
