SC6B1_YEAST
ID SC6B1_YEAST Reviewed; 82 AA.
AC P52870; D3DLZ4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protein transport protein SBH1;
DE AltName: Full=Sec61 complex subunit SBH1;
DE AltName: Full=Sec61 complex subunit beta;
GN Name=SBH1; Synonyms=SEB1; OrderedLocusNames=YER087C-B; ORFNames=YER087BC;
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 [MRNA].
RX PubMed=8740416;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<425::aid-yea924>3.0.co;2-b;
RA Toikkanen J., Gatti E., Takei K., Saloheimo M., Olkkonen V.M.,
RA Soederlund H., de Camilli P., Keraenen S.;
RT "Yeast protein translocation complex: isolation of two genes SEB1 and SEB2
RT encoding proteins homologous to the Sec61 beta subunit.";
RL Yeast 12:425-438(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 BY MASS SPECTROMETRY [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).
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 INTERACTION WITH OST2; OST4 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 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.
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. SBH1 interacts OST2, OST4 and WBP1 components of
CC the OT complex. {ECO:0000269|PubMed:15831493}.
CC -!- INTERACTION:
CC P52870; P46964: OST2; NbExp=2; IntAct=EBI-16410, EBI-12673;
CC P52870; Q99380: OST4; NbExp=2; IntAct=EBI-16410, EBI-12689;
CC P52870; P33767: WBP1; NbExp=2; IntAct=EBI-16410, EBI-12658;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the SEC61-beta family. {ECO:0000305}.
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DR EMBL; Z47789; CAA87710.1; -; mRNA.
DR EMBL; U18839; AAB64663.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07748.1; -; Genomic_DNA.
DR PIR; S68162; S68162.
DR RefSeq; NP_011011.3; NM_001180032.3.
DR PDB; 6N3Q; EM; 3.68 A; B=1-82.
DR PDB; 6ND1; EM; 4.10 A; D=1-82.
DR PDB; 7AFT; EM; 4.40 A; B=1-82.
DR PDB; 7KAH; EM; 3.10 A; B=1-82.
DR PDB; 7KAI; EM; 3.20 A; B=1-82.
DR PDB; 7KAJ; EM; 3.10 A; B=1-82.
DR PDB; 7KAO; EM; 4.00 A; B=1-82.
DR PDB; 7KAP; EM; 4.10 A; B=1-82.
DR PDB; 7KAQ; EM; 4.00 A; B=1-82.
DR PDB; 7KAR; EM; 4.00 A; B=1-82.
DR PDB; 7KAS; EM; 3.90 A; B=1-82.
DR PDB; 7KAT; EM; 4.40 A; B=1-82.
DR PDB; 7KAU; EM; 4.00 A; B=1-82.
DR PDB; 7KB5; EM; 3.80 A; B=1-82.
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; P52870; -.
DR SMR; P52870; -.
DR BioGRID; 36832; 169.
DR ComplexPortal; CPX-1833; SEC61 translocon complex.
DR ComplexPortal; CPX-3055; Translocon complex.
DR DIP; DIP-5681N; -.
DR IntAct; P52870; 19.
DR MINT; P52870; -.
DR STRING; 4932.YER087C-B; -.
DR TCDB; 3.A.5.8.1; the general secretory pathway (sec) family.
DR iPTMnet; P52870; -.
DR MaxQB; P52870; -.
DR PaxDb; P52870; -.
DR PRIDE; P52870; -.
DR TopDownProteomics; P52870; -.
DR EnsemblFungi; YER087C-B_mRNA; YER087C-B; YER087C-B.
DR GeneID; 856821; -.
DR KEGG; sce:YER087C-B; -.
DR SGD; S000002128; SBH1.
DR VEuPathDB; FungiDB:YER087C-B; -.
DR eggNOG; KOG3457; Eukaryota.
DR GeneTree; ENSGT00940000176828; -.
DR HOGENOM; CLU_133423_1_1_1; -.
DR InParanoid; P52870; -.
DR OMA; GEFFLME; -.
DR BioCyc; YEAST:G3O-30349-MON; -.
DR PRO; PR:P52870; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P52870; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0016020; C:membrane; IBA:GO_Central.
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:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
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 GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IMP:SGD.
DR InterPro; IPR030671; Sec61-beta/Sbh.
DR InterPro; IPR016482; SecG/Sec61-beta/Sbh.
DR PANTHER; PTHR13509; PTHR13509; 1.
DR Pfam; PF03911; Sec61_beta; 1.
DR PIRSF; PIRSF006398; Sec61_beta_euk; 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..82
FT /note="Protein transport protein SBH1"
FT /id="PRO_0000157261"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 54..81
FT /evidence="ECO:0007829|PDB:7KAH"
SQ SEQUENCE 82 AA; 8711 MW; 23B0313EB37744FA CRC64;
MSSPTPPGGQ RTLQKRKQGS SQKVAASAPK KNTNSNNSIL KIYSDEATGL RVDPLVVLFL
AVGFIFSVVA LHVISKVAGK LF
