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Database: UniProt
Entry: C7GLT4
LinkDB: C7GLT4
Original site: C7GLT4 
ID   SEC11_YEAS2             Reviewed;         167 AA.
AC   C7GLT4;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   26-NOV-2014, entry version 33.
DE   RecName: Full=Signal peptidase complex catalytic subunit SEC11;
DE            EC=3.4.21.89;
DE   AltName: Full=Secretory protein 11;
DE   AltName: Full=Signal peptidase I;
GN   Name=SEC11; ORFNames=C1Q_01195;
OS   Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=574961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAY291;
RX   PubMed=19812109; DOI=10.1101/gr.091777.109;
RA   Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M.,
RA   Netto O.V.C., Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O.,
RA   Noronha M.F., Dominska M., Andrietta M.G.S., Andrietta S.R.,
RA   Cunha A.F., Gomes L.H., Tavares F.C.A., Alcarde A.R., Dietrich F.S.,
RA   McCusker J.H., Petes T.D., Pereira G.A.G.;
RT   "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT   bioethanol production.";
RL   Genome Res. 19:2258-2270(2009).
CC   -!- FUNCTION: Catalytic component of the signal peptidase complex
CC       (SPC), which catalyzes the cleavage of N-terminal signal sequences
CC       of proteins targeted to the endoplasmic reticulum. Signal peptide
CC       cleavage occurs during the translocation (cotranslationally or
CC       post-translationally) through the translocon pore into the
CC       endoplasmic reticulum (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or
CC       leader sequences from secreted and periplasmic proteins.
CC   -!- SUBUNIT: Component of the signal peptidase complex (SPC), which
CC       consists of SPC1, SPC2, SPC3 and SEC11. SPC associates with the
CC       translocon complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
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DR   EMBL; ACFL01000039; EEU08253.1; -; Genomic_DNA.
DR   ProteinModelPortal; C7GLT4; -.
DR   OrthoDB; EOG7BCNQ4; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR019759; Peptidase_S24_S26.
DR   InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR   InterPro; IPR001733; Peptidase_S26B.
DR   PANTHER; PTHR10806; PTHR10806; 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   Complete proteome; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW   Membrane; Protease; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1    167       Signal peptidase complex catalytic
FT                                subunit SEC11.
FT                                /FTId=PRO_0000412356.
FT   TOPO_DOM      1      9       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     10     30       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     31    167       Lumenal. {ECO:0000255}.
FT   ACT_SITE     44     44       {ECO:0000250}.
FT   CARBOHYD    121    121       N-linked (GlcNAc...). {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
//
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