SC61A_YEAST
ID SC61A_YEAST Reviewed; 480 AA.
AC P32915; D6VZ14;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Protein transport protein SEC61;
DE AltName: Full=Sec61 complex subunit SEC61;
DE AltName: Full=Sec61 complex subunit alpha;
GN Name=SEC61; OrderedLocusNames=YLR378C; ORFNames=L3502.5;
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=1550957; DOI=10.1091/mbc.3.2.129;
RA Stirling C.J., Rothblatt J., Hosobuchi M., Deshaies R., Schekman R.;
RT "Protein translocation mutants defective in the insertion of integral
RT membrane proteins into the endoplasmic reticulum.";
RL Mol. Biol. Cell 3:129-142(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 TOPOLOGY.
RX PubMed=8810333; DOI=10.1074/jbc.271.41.25590;
RA Wilkinson B.M., Critchley A.J., Stirling J.;
RT "Determination of the transmembrane topology of yeast Sec61p, an essential
RT component of the endoplasmic reticulum translocation complex.";
RL J. Biol. Chem. 271:25590-25597(1996).
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 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 [10]
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 [11]
RP INTERACTION WITH STT3; OST1; OST2; 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).
RN [12]
RP ASSOCIATION WITH THE RIBOSOME, AND MUTAGENESIS OF LYS-273; ARG-275;
RP GLY-276; LYS-405 AND ARG-406.
RX PubMed=15631991; DOI=10.1083/jcb.200408188;
RA Cheng Z., Jiang Y., Mandon E.C., Gilmore R.;
RT "Identification of cytoplasmic residues of Sec61p involved in ribosome
RT binding and cotranslational translocation.";
RL J. Cell Biol. 168:67-77(2005).
RN [13]
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).
CC -!- FUNCTION: Part of the Sec61 complex, which is the major component of a
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. In an initial step, the signal sequence seems to bind
CC simultaneously to SEC61 and SEC62. A cycle of assembly and disassembly
CC of Sec62/63 complex from SEC61 may govern the activity of the
CC translocon. SEC61 mediates the association with the ribosome.
CC -!- SUBUNIT: Component of the heterotrimeric Sec61 complex, which is
CC composed of SEC61, 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. SEC61 interacts with STT3, OST1, OST2, OST4, SWP1
CC AND WBP1 components of the OT complex. {ECO:0000269|PubMed:15831493}.
CC -!- INTERACTION:
CC P32915; Q05787: HRD3; NbExp=2; IntAct=EBI-16400, EBI-31647;
CC P32915; P46964: OST2; NbExp=2; IntAct=EBI-16400, EBI-12673;
CC P32915; Q99380: OST4; NbExp=2; IntAct=EBI-16400, EBI-12689;
CC P32915; P00729: PRC1; NbExp=4; IntAct=EBI-16400, EBI-4153;
CC P32915; P21825: SEC62; NbExp=12; IntAct=EBI-16400, EBI-16632;
CC P32915; P33754: SEC66; NbExp=11; IntAct=EBI-16400, EBI-16647;
CC P32915; P35179: SSS1; NbExp=17; IntAct=EBI-16400, EBI-16406;
CC P32915; P39007: STT3; NbExp=2; IntAct=EBI-16400, EBI-18447;
CC P32915; Q02795: SWP1; NbExp=3; IntAct=EBI-16400, EBI-12666;
CC P32915; P33767: WBP1; NbExp=2; IntAct=EBI-16400, EBI-12658;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- MISCELLANEOUS: Present with 24800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; X62340; CAA44215.1; -; Genomic_DNA.
DR EMBL; U19104; AAB67276.1; -; Genomic_DNA.
DR EMBL; U19103; AAB67581.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09680.1; -; Genomic_DNA.
DR PIR; A60043; A60043.
DR RefSeq; NP_013482.1; NM_001182267.1.
DR PDB; 6N3Q; EM; 3.68 A; A=1-480.
DR PDB; 6ND1; EM; 4.10 A; B=1-480.
DR PDB; 7AFT; EM; 4.40 A; A=1-480.
DR PDB; 7KAH; EM; 3.10 A; A=1-480.
DR PDB; 7KAI; EM; 3.20 A; A=1-480.
DR PDB; 7KAJ; EM; 3.10 A; A=1-480.
DR PDB; 7KAO; EM; 4.00 A; A=1-480.
DR PDB; 7KAP; EM; 4.10 A; A=1-480.
DR PDB; 7KAQ; EM; 4.00 A; A=1-480.
DR PDB; 7KAR; EM; 4.00 A; A=1-480.
DR PDB; 7KAS; EM; 3.90 A; A/G=1-480.
DR PDB; 7KAT; EM; 4.40 A; A=1-480.
DR PDB; 7KAU; EM; 4.00 A; A=1-480.
DR PDB; 7KB5; EM; 3.80 A; A=1-480.
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; P32915; -.
DR SMR; P32915; -.
DR BioGRID; 31638; 785.
DR ComplexPortal; CPX-1833; SEC61 translocon complex.
DR ComplexPortal; CPX-3055; Translocon complex.
DR DIP; DIP-2433N; -.
DR IntAct; P32915; 21.
DR MINT; P32915; -.
DR STRING; 4932.YLR378C; -.
DR TCDB; 3.A.5.8.1; the general secretory pathway (sec) family.
DR MaxQB; P32915; -.
DR PaxDb; P32915; -.
DR PRIDE; P32915; -.
DR TopDownProteomics; P32915; -.
DR EnsemblFungi; YLR378C_mRNA; YLR378C; YLR378C.
DR GeneID; 851095; -.
DR KEGG; sce:YLR378C; -.
DR SGD; S000004370; SEC61.
DR VEuPathDB; FungiDB:YLR378C; -.
DR eggNOG; KOG1373; Eukaryota.
DR GeneTree; ENSGT00390000003721; -.
DR HOGENOM; CLU_031763_2_1_1; -.
DR InParanoid; P32915; -.
DR OMA; KWGIGSG; -.
DR BioCyc; YEAST:G3O-32445-MON; -.
DR PRO; PR:P32915; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32915; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA: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:0005784; C:Sec61 translocon complex; IDA:SGD.
DR GO; GO:0071256; C:translocon complex; IPI:ComplexPortal.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IMP:SGD.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IDA:SGD.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IDA:SGD.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IDA:SGD.
DR GO; GO:0070843; P:misfolded protein transport; IMP:SGD.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IDA:SGD.
DR GO; GO:0044743; P:protein transmembrane import into intracellular organelle; IMP:SGD.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:SGD.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IDA:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR Gene3D; 1.10.3370.10; -; 1.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR InterPro; IPR019561; Translocon_Sec61/SecY_plug_dom.
DR PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF10559; Plug_translocon; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 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..480
FT /note="Protein transport protein SEC61"
FT /id="PRO_0000131789"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 33..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000305"
FT TOPO_DOM 56..75
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000305"
FT TOPO_DOM 96..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 120..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000305"
FT TOPO_DOM 142..146
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 147..167
FT /note="Helical; Name=4"
FT /evidence="ECO:0000305"
FT TOPO_DOM 168..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000305"
FT TOPO_DOM 225..240
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 241..260
FT /note="Helical; Name=6"
FT /evidence="ECO:0000305"
FT TOPO_DOM 261..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 291..311
FT /note="Helical; Name=7"
FT /evidence="ECO:0000305"
FT TOPO_DOM 312..361
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 362..381
FT /note="Helical; Name=8"
FT /evidence="ECO:0000305"
FT TOPO_DOM 382..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 417..434
FT /note="Helical; Name=9"
FT /evidence="ECO:0000305"
FT TOPO_DOM 435..437
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 438..459
FT /note="Helical; Name=10"
FT /evidence="ECO:0000305"
FT TOPO_DOM 460..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MUTAGEN 273
FT /note="K->P,G: Severe growth defect."
FT /evidence="ECO:0000269|PubMed:15631991"
FT MUTAGEN 275
FT /note="R->D,G,P,Q,Y: Severe growth defect."
FT /evidence="ECO:0000269|PubMed:15631991"
FT MUTAGEN 275
FT /note="R->E,F,V: Severe growth defect; lowers SRP-dependent
FT and SRP-independent translocation."
FT /evidence="ECO:0000269|PubMed:15631991"
FT MUTAGEN 276
FT /note="G->P: Severe growth defect."
FT /evidence="ECO:0000269|PubMed:15631991"
FT MUTAGEN 405
FT /note="K->D,E,P: Severe growth defect."
FT /evidence="ECO:0000269|PubMed:15631991"
FT MUTAGEN 406
FT /note="R->D: Severe growth defect; lowers SRP-dependent
FT translocation."
FT /evidence="ECO:0000269|PubMed:15631991"
FT MUTAGEN 406
FT /note="R->E: Severe growth defect; lowers SRP-dependent and
FT SRP-independent translocation."
FT /evidence="ECO:0000269|PubMed:15631991"
FT MUTAGEN 406
FT /note="R->H,W: Severe growth defect."
FT /evidence="ECO:0000269|PubMed:15631991"
FT HELIX 29..46
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 83..97
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 109..136
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 148..173
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 244..259
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 264..276
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:7KAH"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 290..313
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:7KAJ"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:7KAJ"
FT HELIX 342..346
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 352..357
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 359..383
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 388..398
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 410..414
FT /evidence="ECO:0007829|PDB:7KAH"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 418..439
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 445..465
FT /evidence="ECO:0007829|PDB:7KAH"
SQ SEQUENCE 480 AA; 52937 MW; AB34F12FB7B3CBD4 CRC64;
MSSNRVLDLF KPFESFLPEV IAPERKVPYN QKLIWTGVSL LIFLILGQIP LYGIVSSETS
DPLYWLRAML ASNRGTLLEL GVSPIITSSM IFQFLQGTQL LQIRPESKQD RELFQIAQKV
CAIILILGQA LVVVMTGNYG APSDLGLPIC LLLIFQLMFA SLIVMLLDEL LSKGYGLGSG
ISLFTATNIA EQIFWRAFAP TTVNSGRGKE FEGAVIAFFH LLAVRKDKKR ALVEAFYRTN
LPNMFQVLMT VAIFLFVLYL QGFRYELPIR STKVRGQIGI YPIKLFYTSN TPIMLQSALT
SNIFLISQIL FQKYPTNPLI RLIGVWGIRP GTQGPQMALS GLAYYIQPLM SLSEALLDPI
KTIVYITFVL GSCAVFSKTW IEISGTSPRD IAKQFKDQGM VINGKRETSI YRELKKIIPT
AAAFGGATIG ALSVGSDLLG TLGSGASILM ATTTIYGYYE AAAKEGGFTK NLVPGFSDLM
