ID SC11A_RAT Reviewed; 179 AA.
AC P42667;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 24-JAN-2024, entry version 143.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7854339; DOI=10.1007/bf00944199;
RA Signs S.A., Difeo-Jacquet R.;
RT "Induction of ethanol dependence increases signal peptidase mRNA levels in
RT rat brain.";
RL Mol. Cell. Biochem. 139:21-26(1994).
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; L11319; AAA64738.1; -; mRNA.
DR PIR; I57489; I57489.
DR AlphaFoldDB; P42667; -.
DR SMR; P42667; -.
DR IntAct; P42667; 1.
DR STRING; 10116.ENSRNOP00000015218; -.
DR MEROPS; S26.009; -.
DR iPTMnet; P42667; -.
DR PhosphoSitePlus; P42667; -.
DR jPOST; P42667; -.
DR PaxDb; 10116-ENSRNOP00000015218; -.
DR UCSC; RGD:69360; rat.
DR AGR; RGD:69360; -.
DR RGD; 69360; Sec11a.
DR eggNOG; KOG3342; Eukaryota.
DR InParanoid; P42667; -.
DR PhylomeDB; P42667; -.
DR Reactome; R-RNO-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR PRO; PR:P42667; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
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 Gene3D; 2.10.109.10; Umud Fragment, subunit A; 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 NCBIfam; TIGR02228; sigpep_I_arch; 1.
DR PANTHER; PTHR10806; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11; 1.
DR PANTHER; PTHR10806:SF28; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11B-RELATED; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 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_0000109546"
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; 20599 MW; DC6C032B0FFB167F CRC64;
MLSLDFLDDV RRMNKRQLYY QVLNFGMIVS SALMIWKGLM LITGSESPIV VVLSGSMEPA
FHRGDLLFLT NRVEDPIRVG EIVVFRIEGR EIPIVHRVLK IHEKQDGHIK FLTKGDNNAV
DDRGLYKQGQ HWLEKKDVVG RARGFVPYIG IVTILMNDYP KFSYAVLFLL GLFVLVHRE
//
