SC11C_RAT
ID SC11C_RAT Reviewed; 192 AA.
AC Q9WTR7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11C;
DE EC=3.4.21.89 {ECO:0000250|UniProtKB:Q9BY50};
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 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=Pituitary;
RA Shiizaki K.;
RT "Rat mRNA homologous to signal peptidase.";
RL Submitted (JAN-1999) 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:Q9BY50}.
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:Q9BY50};
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. 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:Q9BY50}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P13679}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P13679}.
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:Q9BY50}.
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; AB022714; BAA76439.1; -; mRNA.
DR RefSeq; NP_705892.1; NM_153628.2.
DR AlphaFoldDB; Q9WTR7; -.
DR SMR; Q9WTR7; -.
DR STRING; 10116.ENSRNOP00000022958; -.
DR MEROPS; S26.010; -.
DR jPOST; Q9WTR7; -.
DR PaxDb; Q9WTR7; -.
DR PRIDE; Q9WTR7; -.
DR GeneID; 266758; -.
DR KEGG; rno:266758; -.
DR UCSC; RGD:628665; rat.
DR CTD; 90701; -.
DR RGD; 628665; Sec11c.
DR eggNOG; KOG3342; Eukaryota.
DR InParanoid; Q9WTR7; -.
DR OrthoDB; 1486616at2759; -.
DR PhylomeDB; Q9WTR7; -.
DR Reactome; R-RNO-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR PRO; PR:Q9WTR7; -.
DR Proteomes; UP000002494; Unplaced.
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; 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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..192
FT /note="Signal peptidase complex catalytic subunit SEC11C"
FT /id="PRO_0000109551"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13679"
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:0000250|UniProtKB:P13679"
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; 21646 MW; 6D4650314EA9DEF0 CRC64;
MVRAGAVGTH LPTSSLDIFG DLRKMNKRQL YYQVLNFAMI VSSALMIWKG LIVLTGSESP
IVVVLSGSME PAFHRGDLLF LTNFREDPIR AGEIVVFKVE GRDIPIVHRV IKVHEKDNGD
IKFLTKGDNN EVDDRGLYKE GQNWLEKKDV VGRARGFLPY VGMVTIIMND YPKFKYALVA
VMGAYVLLKR ES
