SC11C_CANLF
ID SC11C_CANLF Reviewed; 192 AA.
AC P13679;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11C;
DE EC=3.4.21.89 {ECO:0000269|PubMed:14559916, ECO:0000269|PubMed:3511473};
DE AltName: Full=Microsomal signal peptidase 21 kDa subunit;
DE Short=SPase 21 kDa subunit;
DE AltName: Full=SEC11 homolog C;
DE AltName: Full=SEC11-like protein 3;
DE AltName: Full=SPC21;
GN Name=SEC11C; Synonyms=SEC11L3, SPC21;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-31 AND 69-89.
RC TISSUE=Liver;
RX PubMed=2674115; DOI=10.1016/s0021-9258(18)71541-x;
RA Greenburg G., Shelness G.S., Blobel G.;
RT "A subunit of mammalian signal peptidase is homologous to yeast SEC11
RT protein.";
RL J. Biol. Chem. 264:15762-15765(1989).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE SIGNAL PEPTIDASE
RP COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=3511473; DOI=10.1073/pnas.83.3.581;
RA Evans E.A., Gilmore R., Blobel G.;
RT "Purification of microsomal signal peptidase as a complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:581-585(1986).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=8444896; DOI=10.1016/s0021-9258(18)53520-1;
RA Shelness G.S., Lin L., Nicchitta C.V.;
RT "Membrane topology and biogenesis of eukaryotic signal peptidase.";
RL J. Biol. Chem. 268:5201-5208(1993).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14559916; DOI=10.1074/jbc.m307542200;
RA Liang H., VanValkenburgh C., Chen X., Mullins C., Van Kaer L., Green N.,
RA Fang H.;
RT "Genetic complementation in yeast reveals functional similarities between
RT the catalytic subunits of mammalian signal peptidase complex.";
RL J. Biol. Chem. 278:50932-50939(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:3511473, PubMed:8444896,
CC PubMed:14559916). 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:14559916, ECO:0000269|PubMed:3511473,
CC ECO:0000269|PubMed:8444896}.
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:14559916, ECO:0000269|PubMed:3511473};
CC -!- SUBUNIT: Component of the signal peptidase complex paralog C (SPC-C)
CC composed of a catalytic subunit SEC11C and three accessory subunits
CC SPCS1, SPCS2 and SPCS3 (PubMed:3511473). Within the complex, interacts
CC with SPCS2 and SPCS3 (By similarity). 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). {ECO:0000250|UniProtKB:P67812,
CC ECO:0000269|PubMed:3511473}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:3511473, ECO:0000269|PubMed:8444896}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:8444896}.
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: May undergo processing at the N-terminus.
CC {ECO:0000250|UniProtKB:Q9BY50}.
CC -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
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DR EMBL; J05069; AAA30896.1; -; mRNA.
DR PIR; A34229; A34229.
DR RefSeq; NP_001003312.1; NM_001003312.1.
DR AlphaFoldDB; P13679; -.
DR SMR; P13679; -.
DR CORUM; P13679; -.
DR STRING; 9612.ENSCAFP00000000138; -.
DR MEROPS; S26.010; -.
DR PaxDb; P13679; -.
DR PRIDE; P13679; -.
DR GeneID; 404003; -.
DR KEGG; cfa:404003; -.
DR CTD; 90701; -.
DR eggNOG; KOG3342; Eukaryota.
DR HOGENOM; CLU_089996_0_0_1; -.
DR InParanoid; P13679; -.
DR OMA; PYIGMLT; -.
DR OrthoDB; 1486616at2759; -.
DR TreeFam; TF313648; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0006465; P:signal peptide processing; ISS:UniProtKB.
DR CDD; cd06530; S26_SPase_I; 1.
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; IPR019533; Peptidase_S26.
DR InterPro; IPR001733; Peptidase_S26B.
DR InterPro; IPR037710; SEC11C.
DR PANTHER; PTHR10806; PTHR10806; 1.
DR PANTHER; PTHR10806:SF12; PTHR10806:SF12; 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 Direct protein sequencing; Endoplasmic reticulum; Hydrolase; Membrane;
KW Protease; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2674115"
FT CHAIN 2..192
FT /note="Signal peptidase complex catalytic subunit SEC11C"
FT /id="PRO_0000109547"
FT TOPO_DOM 2..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8444896"
FT TRANSMEM 29..48
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..192
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:8444896"
FT REGION 177..188
FT /note="C-terminal short (CTS) helix"
FT /evidence="ECO:0000250|UniProtKB:Q9BY50"
FT ACT_SITE 68
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9BY50"
FT ACT_SITE 108
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9BY50"
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9BY50"
SQ SEQUENCE 192 AA; 21600 MW; 3C4933EAEAB5E58E CRC64;
MVRAGAVGTH LPASGLDIFG DLRKMNKRQL YYQVLNFAMI VSSALMIWKG LIVLTGSESP
IVVVLSGSME PAFHRGDLLF LTNFREDPIR AGEIVVFKVE GRDIPIVHRV IKVHEKDNGD
IKFLTKGDNN EVDDRGLYKE GQNWLEKKDV VGRARGFLPY VGMVTIIMND YPKFKYALLA
VMGAYVLLKR ES
