SC11C_MOUSE
ID SC11C_MOUSE Reviewed; 192 AA.
AC Q9D8V7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK007641; BAB25156.1; -; mRNA.
DR EMBL; BC037187; AAH37187.1; -; mRNA.
DR CCDS; CCDS29309.1; -.
DR RefSeq; NP_079744.1; NM_025468.2.
DR AlphaFoldDB; Q9D8V7; -.
DR SMR; Q9D8V7; -.
DR BioGRID; 211357; 2.
DR IntAct; Q9D8V7; 1.
DR STRING; 10090.ENSMUSP00000025394; -.
DR MEROPS; S26.010; -.
DR PhosphoSitePlus; Q9D8V7; -.
DR EPD; Q9D8V7; -.
DR MaxQB; Q9D8V7; -.
DR PaxDb; Q9D8V7; -.
DR PeptideAtlas; Q9D8V7; -.
DR PRIDE; Q9D8V7; -.
DR ProteomicsDB; 253401; -.
DR Antibodypedia; 22969; 53 antibodies from 15 providers.
DR DNASU; 66286; -.
DR Ensembl; ENSMUST00000025394; ENSMUSP00000025394; ENSMUSG00000024516.
DR GeneID; 66286; -.
DR KEGG; mmu:66286; -.
DR UCSC; uc008ffh.1; mouse.
DR CTD; 90701; -.
DR MGI; MGI:1913536; Sec11c.
DR VEuPathDB; HostDB:ENSMUSG00000024516; -.
DR eggNOG; KOG3342; Eukaryota.
DR GeneTree; ENSGT00390000015600; -.
DR HOGENOM; CLU_089996_0_0_1; -.
DR InParanoid; Q9D8V7; -.
DR OMA; PYIGMLT; -.
DR OrthoDB; 1486616at2759; -.
DR PhylomeDB; Q9D8V7; -.
DR TreeFam; TF313648; -.
DR Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR BioGRID-ORCS; 66286; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Sec11c; mouse.
DR PRO; PR:Q9D8V7; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9D8V7; protein.
DR Bgee; ENSMUSG00000024516; Expressed in lacrimal gland and 252 other tissues.
DR ExpressionAtlas; Q9D8V7; baseline and differential.
DR Genevisible; Q9D8V7; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
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 1: Evidence at protein 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_0000109549"
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; 21660 MW; 6D4650314EB52CF0 CRC64;
MVRAGAVGTH LPTSSLDIFG DLRKMNKRQL YYQVLNFAMI VSSALMIWKG LIVLTGSESP
IVVVLSGSME PAFHRGDLLF LTNFREDPIR AGEIVVFKVE GRDIPIVHRV IKVHEKDNGD
IKFLTKGDNN EVDDRGLYKE GQNWLEKKDV VGRARGFLPY VGMVTIIMND YPKFKYALLA
VMGAYVLLKR ES
