SC11A_CANLF
ID SC11A_CANLF Reviewed; 179 AA.
AC P67811; O75957; P21378;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11A;
DE EC=3.4.21.89 {ECO:0000269|PubMed:14559916, ECO:0000269|PubMed:3511473};
DE AltName: Full=Endopeptidase SP18;
DE AltName: Full=Microsomal signal peptidase 18 kDa subunit;
DE Short=SPase 18 kDa subunit;
DE AltName: Full=SEC11 homolog A;
DE AltName: Full=SEC11-like protein 1;
DE AltName: Full=SPC18;
GN Name=SEC11A; Synonyms=SEC11L1, SPC18;
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 1-34.
RC TISSUE=Liver;
RX PubMed=2188978; DOI=10.1016/s0021-9258(19)38879-9;
RA Shelness G.S., Blobel G.;
RT "Two subunits of the canine signal peptidase complex are homologous to
RT yeast SEC11 protein.";
RL J. Biol. Chem. 265:9512-9519(1990).
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 A (SPC-A)
CC composed of a catalytic subunit SEC11A 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 -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
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DR EMBL; J05466; AAA30895.1; -; mRNA.
DR PIR; A35309; A35309.
DR RefSeq; NP_001003313.1; NM_001003313.1.
DR AlphaFoldDB; P67811; -.
DR SMR; P67811; -.
DR CORUM; P67811; -.
DR STRING; 9615.ENSCAFP00000051306; -.
DR MEROPS; S26.009; -.
DR PaxDb; P67811; -.
DR PRIDE; P67811; -.
DR Ensembl; ENSCAFT00000092290; ENSCAFP00000051306; ENSCAFG00000012889.
DR Ensembl; ENSCAFT00030002465; ENSCAFP00030002195; ENSCAFG00030001355.
DR Ensembl; ENSCAFT00040006188; ENSCAFP00040005348; ENSCAFG00040003253.
DR Ensembl; ENSCAFT00845005172; ENSCAFP00845004107; ENSCAFG00845002905.
DR GeneID; 404004; -.
DR KEGG; cfa:404004; -.
DR CTD; 23478; -.
DR VEuPathDB; HostDB:ENSCAFG00845002905; -.
DR VGNC; VGNC:53239; SEC11A.
DR eggNOG; KOG3342; Eukaryota.
DR GeneTree; ENSGT00390000015600; -.
DR HOGENOM; CLU_089996_0_0_1; -.
DR InParanoid; P67811; -.
DR OMA; YNVRGKD; -.
DR OrthoDB; 1486616at2759; -.
DR TreeFam; TF313648; -.
DR Proteomes; UP000002254; Chromosome 3.
DR Bgee; ENSCAFG00000012889; Expressed in lymph node and 49 other tissues.
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; IPR037712; SEC11A.
DR PANTHER; PTHR10806; PTHR10806; 1.
DR PANTHER; PTHR10806:SF28; PTHR10806:SF28; 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 CHAIN 1..179
FT /note="Signal peptidase complex catalytic subunit SEC11A"
FT /id="PRO_0000109542"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8444896"
FT TRANSMEM 17..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..179
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:8444896"
FT REGION 165..176
FT /note="C-terminal short (CTS) helix"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT ACT_SITE 56
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT ACT_SITE 96
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P67812"
SQ SEQUENCE 179 AA; 20625 MW; DFD245A17BA3B47F CRC64;
MLSLDFLDDV RRMNKRQLYY QVLNFGMIVS SALMIWKGLM VITGSESPIV VVLSGSMEPA
FHRGDLLFLT NRVEDPIRVG EIVVFRIEGR EIPIVHRVLK IHEKQNGHIK FLTKGDNNAV
DDRGLYKQGQ HWLEKKDVVG RARGFVPYIG IVTILMNDYP KFKYAVLFLL GLFVLVHRE
