SSH1_YEAST
ID SSH1_YEAST Reviewed; 490 AA.
AC P38353; D6VQS8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Sec sixty-one protein homolog;
DE AltName: Full=Ssh1 complex subunit SSH1;
DE AltName: Full=Ssh1 complex subunit alpha;
GN Name=SSH1; OrderedLocusNames=YBR283C; ORFNames=YBR2020;
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=8612571; DOI=10.1002/j.1460-2075.1996.tb00492.x;
RA Finke K., Plath K., Panzner S., Prehn S., Rapoport T.A., Hartmann E.,
RA Sommer T.;
RT "A second trimeric complex containing homologs of the Sec61p complex
RT functions in protein transport across the ER membrane of S. cerevisiae.";
RL EMBO J. 15:1482-1494(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091861; DOI=10.1002/yea.320100007;
RA Holmstroem K., Brandt T., Kallesoe T.;
RT "The sequence of a 32,420 bp segment located on the right arm of chromosome
RT II from Saccharomyces cerevisiae.";
RL Yeast 10:S47-S62(1994).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-490.
RX PubMed=1764528; DOI=10.1016/0300-9084(91)90063-7;
RA Graack H.-R., Grohmann L., Kitakawa M.;
RT "The nuclear coded mitoribosomal proteins YmL27 and YmL31 are both
RT essential for mitochondrial function in yeast.";
RL Biochimie 73:837-844(1991).
RN [7]
RP FUNCTION.
RX PubMed=11702951; DOI=10.1016/s1534-5807(01)00043-0;
RA Wilkinson B.M., Tyson J.R., Stirling C.J.;
RT "Ssh1p determines the translocation and dislocation capacities of the yeast
RT endoplasmic reticulum.";
RL Dev. Cell 1:401-409(2001).
RN [8]
RP ASSOCIATION OF THE SSH1 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 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 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 endoplasmic
CC reticulum (ER) import. {ECO:0000269|PubMed:11702951}.
CC -!- SUBUNIT: Component of the heterotrimeric Ssh1 complex, which is
CC composed of SSH1, SBH2 and SSS1.
CC -!- INTERACTION:
CC P38353; P53337: ERV29; NbExp=3; IntAct=EBI-18175, EBI-23662;
CC P38353; P38264: PHO88; NbExp=3; IntAct=EBI-18175, EBI-13350;
CC P38353; P35179: SSS1; NbExp=8; IntAct=EBI-18175, EBI-16406;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- MISCELLANEOUS: Present with 704 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; U05336; AAB40986.1; -; Genomic_DNA.
DR EMBL; X76053; CAA53646.1; -; Genomic_DNA.
DR EMBL; Z36152; CAA85247.1; -; Genomic_DNA.
DR EMBL; AY692997; AAT93016.1; -; Genomic_DNA.
DR EMBL; S77888; AAB21097.2; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006936; DAA07398.1; -; Genomic_DNA.
DR PIR; S44545; S44545.
DR RefSeq; NP_009842.1; NM_001178631.1.
DR PDB; 2WW9; EM; 8.60 A; A=1-490.
DR PDB; 2WWA; EM; 8.90 A; A=1-490.
DR PDBsum; 2WW9; -.
DR PDBsum; 2WWA; -.
DR AlphaFoldDB; P38353; -.
DR SMR; P38353; -.
DR BioGRID; 32977; 287.
DR ComplexPortal; CPX-1834; SSH1 translocon complex.
DR DIP; DIP-4962N; -.
DR IntAct; P38353; 40.
DR MINT; P38353; -.
DR STRING; 4932.YBR283C; -.
DR MaxQB; P38353; -.
DR PaxDb; P38353; -.
DR PRIDE; P38353; -.
DR EnsemblFungi; YBR283C_mRNA; YBR283C; YBR283C.
DR GeneID; 852586; -.
DR KEGG; sce:YBR283C; -.
DR SGD; S000000487; SSH1.
DR VEuPathDB; FungiDB:YBR283C; -.
DR eggNOG; KOG1373; Eukaryota.
DR GeneTree; ENSGT00390000003721; -.
DR HOGENOM; CLU_031763_2_1_1; -.
DR InParanoid; P38353; -.
DR OMA; QAYCHIK; -.
DR BioCyc; YEAST:G3O-29203-MON; -.
DR EvolutionaryTrace; P38353; -.
DR PRO; PR:P38353; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38353; 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:0005784; C:Sec61 translocon complex; IBA:GO_Central.
DR GO; GO:0071261; C:Ssh1 translocon complex; IDA:SGD.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IDA:SGD.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IBA:GO_Central.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IMP:SGD.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
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 PROSITE; PS00755; SECY_1; 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..490
FT /note="Sec sixty-one protein homolog"
FT /id="PRO_0000131811"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..121
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..174
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..293
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..449
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 490 AA; 53312 MW; 48267EEA3E0191BD CRC64;
MSGFRLIDIV KPILPILPEV ELPFEKLPFD DKIVYTIFAG LIYLFAQFPL VGLPKATTPN
VNDPIYFLRG VFGCEPRTLL EFGLFPNISS GLILQLLAGL KVIKVNFKIQ SDRELFQSLT
KVFAIVQYVI LTNIFIFAGY FGDDLSVVQI GLINFQLVGA GIFTTLLAEV IDKGFGFSSG
AMIINTVVIA TNLVADTFGV SQIKVGEDDQ TEAQGALINL IQGLRSKHKT FIGGIISAFN
RDYLPNLTTT IIVLAIAIIV CYLQSVRVEL PIRSTRARGT NNVYPIKLLY TGCLSVLFSY
TILFYIHIFA FVLIQLVAKN EPTHIICKIM GHYENANNLL AVPTFPLSLL APPTSFFKGV
TQQPLTFITY SAFILVTGIW FADKWQAISG SSARDVALEF KDQGITLMGR REQNVAKELN
KVIPIAAVTG ASVLSLITVI GESLGLKGKA AGIVVGIAGG FSLLEVITIE YQQSGGQSAL
NQVLGVPGAM
