SC11A_BOVIN
ID SC11A_BOVIN Reviewed; 179 AA.
AC P67810; A6QQV7; O75957; P21378;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11A;
DE EC=3.4.21.89 {ECO:0000250|UniProtKB:P67812};
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11531706; DOI=10.1046/j.1365-2052.2001.0769b.x;
RA Ashwell M.S., Ashwell C.M., Garrett W.M., Bennett G.L.;
RT "Isolation, characterization and mapping of the bovine signal peptidase
RT subunit 18 gene.";
RL Anim. Genet. 32:232-233(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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. Specifically cleaves N-terminal signal peptides
CC that contain a hydrophobic alpha-helix (h-region) shorter than 18-20
CC amino acids. {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:P67812};
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. Within the complex, interacts with SPCS2 and
CC SPCS3. The complex induces a local thinning of the ER membrane which is
CC used to measure the length of the signal peptide (SP) h-region of
CC protein substrates. This ensures the selectivity of the complex towards
CC h-regions shorter than 18-20 amino acids.
CC {ECO:0000250|UniProtKB:P67812}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P67811}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P67811}.
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; AF221669; AAF34660.1; -; mRNA.
DR EMBL; BC150010; AAI50011.1; -; mRNA.
DR RefSeq; NP_776890.1; NM_174465.2.
DR AlphaFoldDB; P67810; -.
DR SMR; P67810; -.
DR STRING; 9913.ENSBTAP00000014925; -.
DR MEROPS; S26.009; -.
DR PaxDb; P67810; -.
DR PRIDE; P67810; -.
DR Ensembl; ENSBTAT00000014925; ENSBTAP00000014925; ENSBTAG00000011239.
DR GeneID; 282078; -.
DR KEGG; bta:282078; -.
DR CTD; 23478; -.
DR VEuPathDB; HostDB:ENSBTAG00000011239; -.
DR VGNC; VGNC:53951; SEC11A.
DR eggNOG; KOG3342; Eukaryota.
DR GeneTree; ENSGT00390000015600; -.
DR HOGENOM; CLU_089996_0_0_1; -.
DR InParanoid; P67810; -.
DR OMA; YNVRGKD; -.
DR OrthoDB; 1486616at2759; -.
DR TreeFam; TF313648; -.
DR Reactome; R-BTA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000011239; Expressed in granulosa cell and 104 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; ISS: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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..179
FT /note="Signal peptidase complex catalytic subunit SEC11A"
FT /id="PRO_0000109541"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P67811"
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:0000250|UniProtKB:P67811"
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
