SEC11_YEAS7
ID SEC11_YEAS7 Reviewed; 167 AA.
AC A6ZVU2;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11;
DE EC=3.4.21.89 {ECO:0000250|UniProtKB:P15367};
DE AltName: Full=Secretory protein 11;
DE AltName: Full=Signal peptidase I;
GN Name=SEC11; ORFNames=SCY_2808;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 (By similarity). Specifically cleaves N-terminal
CC signal peptides that contain a hydrophobic alpha-helix (h-region)
CC shorter than 18-20 amino acids (By similarity).
CC {ECO:0000250|UniProtKB:P15367, ECO:0000250|UniProtKB:P67812}.
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:0000250|UniProtKB:P15367};
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 (By similarity). The complex induces a local thinning of the ER
CC membrane which is used to measure the length of the signal peptide (SP)
CC h-region of protein substrates. This ensures the selectivity of the
CC complex towards h-regions shorter than 18-20 amino acids (By
CC similarity). SPC associates with the translocon complex (By
CC similarity). {ECO:0000250|UniProtKB:P15367,
CC ECO:0000250|UniProtKB:P67812}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P15367}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P15367}.
CC -!- DOMAIN: The C-terminal short (CTS) helix is essential for catalytic
CC activity. It may be accommodated as a transmembrane helix in the
CC thinned membrane environment of the complex, similarly to the signal
CC peptide in the complex substrates. {ECO:0000250|UniProtKB:P67812}.
CC -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
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DR EMBL; AAFW02000124; EDN61517.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZVU2; -.
DR SMR; A6ZVU2; -.
DR MEROPS; S26.010; -.
DR EnsemblFungi; EDN61517; EDN61517; SCY_2808.
DR HOGENOM; CLU_089996_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Protease;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..167
FT /note="Signal peptidase complex catalytic subunit SEC11"
FT /id="PRO_0000412361"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..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:0000250|UniProtKB:P15367"
FT ACT_SITE 83
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P15367"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P15367"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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
