SEC11_YEAST
ID SEC11_YEAST Reviewed; 167 AA.
AC P15367; D6VVV3;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11;
DE EC=3.4.21.89 {ECO:0000269|PubMed:10206957};
DE AltName: Full=Secretory protein 11;
DE AltName: Full=Signal peptidase I;
GN Name=SEC11; OrderedLocusNames=YIR022W;
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], AND DISRUPTION PHENOTYPE.
RC STRAIN=PBY408A;
RX PubMed=3283143; DOI=10.1083/jcb.106.4.1035;
RA Boehni P.C., Deshaies R.J., Schekman R.W.;
RT "SEC11 is required for signal peptide processing and yeast cell growth.";
RL J. Cell Biol. 106:1035-1042(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2644273; DOI=10.1016/s0021-9258(19)81701-5;
RA YaDeau J.T., Blobel G.;
RT "Solubilization and characterization of yeast signal peptidase.";
RL J. Biol. Chem. 264:2928-2934(1989).
RN [6]
RP IDENTIFICATION IN THE SIGNAL PEPTIDASE COMPLEX.
RX PubMed=1846444; DOI=10.1073/pnas.88.2.517;
RA YaDeau J.T., Klein C., Blobel G.;
RT "Yeast signal peptidase contains a glycoprotein and the Sec11 gene
RT product.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:517-521(1991).
RN [7]
RP FUNCTION.
RX PubMed=7615509; DOI=10.1074/jbc.270.29.17139;
RA Mullins C., Lu Y., Campbell A., Fang H., Green N.;
RT "A mutation affecting signal peptidase inhibits degradation of an abnormal
RT membrane protein in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 270:17139-17147(1995).
RN [8]
RP IDENTIFICATION IN THE SIGNAL PEPTIDASE COMPLEX.
RX PubMed=9148931; DOI=10.1074/jbc.272.20.13159;
RA Meyer H.A., Hartmann E.;
RT "The yeast SPC22/23 homolog Spc3p is essential for signal peptidase
RT activity.";
RL J. Biol. Chem. 272:13159-13164(1997).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, INTERACTION WITH SPC3,
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND MUTAGENESIS OF SER-44; HIS-83;
RP ASP-103 AND ASP-109.
RX PubMed=10206957; DOI=10.1074/jbc.274.17.11519;
RA VanValkenburgh C., Chen X., Mullins C., Fang H., Green N.;
RT "The catalytic mechanism of endoplasmic reticulum signal peptidase appears
RT to be distinct from most eubacterial signal peptidases.";
RL J. Biol. Chem. 274:11519-11525(1999).
RN [10]
RP FUNCTION.
RX PubMed=11058593; DOI=10.1074/jbc.m007723200;
RA Chen X., VanValkenburgh C., Liang H., Fang H., Green N.;
RT "Signal peptidase and oligosaccharyltransferase interact in a sequential
RT and dependent manner within the endoplasmic reticulum.";
RL J. Biol. Chem. 276:2411-2416(2001).
RN [11]
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 [12]
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: Catalytic component of the signal peptidase complex (SPC)
CC which catalyzes the cleavage of N-terminal signal sequences from
CC nascent proteins as they are translocated into the lumen of the
CC endoplasmic reticulum (PubMed:2644273, PubMed:7615509, PubMed:10206957,
CC PubMed:11058593). Specifically cleaves N-terminal signal peptides that
CC contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino
CC acids (By similarity). {ECO:0000250|UniProtKB:P67812,
CC ECO:0000269|PubMed:10206957, ECO:0000269|PubMed:11058593,
CC ECO:0000269|PubMed:2644273, ECO:0000269|PubMed:7615509}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC Evidence={ECO:0000269|PubMed:10206957};
CC -!- SUBUNIT: Component of the signal peptidase complex (SPC) composed of a
CC catalytic subunit SEC11 and three accessory subunits SPC1, SPC2 and
CC SPC3 (PubMed:1846444, PubMed:9148931). The complex induces a local
CC thinning of the ER membrane which is used to measure the length of the
CC signal peptide (SP) h-region of protein substrates (By similarity).
CC This ensures the selectivity of the complex towards h-regions shorter
CC than 18-20 amino acids (By similarity). Interacts with SPC3
CC (PubMed:10206957). SPC associates with the translocon complex
CC (PubMed:1846444, PubMed:9148931). {ECO:0000250|UniProtKB:P67812,
CC ECO:0000269|PubMed:10206957, ECO:0000269|PubMed:1846444,
CC ECO:0000269|PubMed:9148931}.
CC -!- INTERACTION:
CC P15367; P46965: SPC1; NbExp=4; IntAct=EBI-16513, EBI-17823;
CC P15367; Q12133: SPC3; NbExp=3; IntAct=EBI-16513, EBI-17829;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10206957, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:2644273}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:10206957, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:2644273}.
CC -!- DOMAIN: The C-terminal short (CTS) helix is essential for catalytic
CC activity (By similarity). It may be accommodated as a transmembrane
CC helix in the thinned membrane environment of the complex, similarly to
CC the signal peptide in the complex substrates (By similarity).
CC {ECO:0000250|UniProtKB:P67812}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10206957}.
CC -!- DISRUPTION PHENOTYPE: Leads to accumulation of core-glycosylated
CC glycoprotein precursors. {ECO:0000269|PubMed:3283143}.
CC -!- MISCELLANEOUS: Present with 3150 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
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DR EMBL; X07694; CAA30533.1; -; Genomic_DNA.
DR EMBL; Z38061; CAA86182.1; -; Genomic_DNA.
DR EMBL; AY558239; AAS56565.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08569.1; -; Genomic_DNA.
DR PIR; S48484; S48484.
DR RefSeq; NP_012288.1; NM_001179544.1.
DR AlphaFoldDB; P15367; -.
DR SMR; P15367; -.
DR BioGRID; 35013; 230.
DR ComplexPortal; CPX-1835; Signal peptidase complex.
DR DIP; DIP-5667N; -.
DR IntAct; P15367; 6.
DR MINT; P15367; -.
DR STRING; 4932.YIR022W; -.
DR MEROPS; S26.010; -.
DR iPTMnet; P15367; -.
DR MaxQB; P15367; -.
DR PaxDb; P15367; -.
DR PRIDE; P15367; -.
DR TopDownProteomics; P15367; -.
DR EnsemblFungi; YIR022W_mRNA; YIR022W; YIR022W.
DR GeneID; 854840; -.
DR KEGG; sce:YIR022W; -.
DR SGD; S000001461; SEC11.
DR VEuPathDB; FungiDB:YIR022W; -.
DR eggNOG; KOG3342; Eukaryota.
DR GeneTree; ENSGT00390000015600; -.
DR HOGENOM; CLU_089996_0_0_1; -.
DR InParanoid; P15367; -.
DR OMA; YNVRGKD; -.
DR BioCyc; YEAST:YIR022W-MON; -.
DR BRENDA; 3.4.21.89; 984.
DR PRO; PR:P15367; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P15367; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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:0005787; C:signal peptidase complex; IDA:SGD.
DR GO; GO:0008233; F:peptidase activity; IMP:SGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045047; P:protein targeting to ER; IMP:SGD.
DR GO; GO:0006465; P:signal peptide processing; IDA:SGD.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR InterPro; IPR001733; Peptidase_S26B.
DR InterPro; IPR027245; Sec11.
DR PANTHER; PTHR10806; PTHR10806; 1.
DR PANTHER; PTHR10806:SF6; PTHR10806:SF6; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; SSF51306; 1.
DR TIGRFAMs; TIGR02228; sigpep_I_arch; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..167
FT /note="Signal peptidase complex catalytic subunit SEC11"
FT /id="PRO_0000109540"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..167
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 153..164
FT /note="C-terminal short (CTS) helix"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT ACT_SITE 44
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:10206957"
FT ACT_SITE 83
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:10206957"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:10206957"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 44
FT /note="S->A: Nonviable. Loss of catalytic activity. No
FT effect on protein stability and interaction with SPC3."
FT /evidence="ECO:0000269|PubMed:10206957"
FT MUTAGEN 44
FT /note="S->C: Nonviable."
FT /evidence="ECO:0000269|PubMed:10206957"
FT MUTAGEN 83
FT /note="H->A: Nonviable. Loss of protein stability."
FT /evidence="ECO:0000269|PubMed:10206957"
FT MUTAGEN 83
FT /note="H->F: Nonviable. Loss of catalytic activity. No
FT effect on protein stability."
FT /evidence="ECO:0000269|PubMed:10206957"
FT MUTAGEN 83
FT /note="H->K: Nonviable. Loss of catalytic activity. Loss of
FT protein stability."
FT /evidence="ECO:0000269|PubMed:10206957"
FT MUTAGEN 103
FT /note="D->E: Nonviable. Loss of catalytic activity. Loss of
FT protein stability."
FT /evidence="ECO:0000269|PubMed:10206957"
FT MUTAGEN 103
FT /note="D->N: Nonviable. Loss of catalytic activity. No
FT effect on protein stability and interaction with SPC3."
FT /evidence="ECO:0000269|PubMed:10206957"
FT MUTAGEN 109
FT /note="D->E: Nonviable. Loss of catalytic activity. No
FT effect on protein stability and interaction with SPC3."
FT /evidence="ECO:0000269|PubMed:10206957"
FT MUTAGEN 109
FT /note="D->N: Nonviable. Loss of catalytic activity. Loss of
FT protein stability."
FT /evidence="ECO:0000269|PubMed:10206957"
FT CONFLICT 162
FT /note="A -> R (in Ref. 1; CAA30533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 18762 MW; FC877232D6888DF3 CRC64;
MNLRFELQKL LNVCFLFASA YMFWQGLAIA TNSASPIVVV LSGSMEPAFQ RGDILFLWNR
NTFNQVGDVV VYEVEGKQIP IVHRVLRQHN NHADKQFLLT KGDNNAGNDI SLYANKKIYL
NKSKEIVGTV KGYFPQLGYI TIWISENKYA KFALLGMLGL SALLGGE
