SPCS1_MOUSE
ID SPCS1_MOUSE Reviewed; 161 AA.
AC Q9D958; Q8BJM2;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Signal peptidase complex subunit 1;
DE AltName: Full=Microsomal signal peptidase 12 kDa subunit;
DE Short=SPase 12 kDa subunit;
GN Name=Spcs1; Synonyms=Spc12;
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=Czech II; 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-161.
RC STRAIN=C57BL/6J; TISSUE=Embryo, and 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).
CC -!- FUNCTION: Component of the signal peptidase complex (SPC) which
CC catalyzes the cleavage of N-terminal signal sequences from nascent
CC proteins as they are translocated into the lumen of the endoplasmic
CC reticulum (By similarity). Dispensable for SPC enzymatic activity (By
CC similarity). {ECO:0000250|UniProtKB:P46965,
CC ECO:0000250|UniProtKB:Q9Y6A9}.
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. Component of the signal peptidase complex
CC paralog C (SPC-C) composed of a catalytic subunit SEC11C and three
CC accessory subunits SPCS1, SPCS2 and SPCS3. Within the complex,
CC interacts with SPCS2 and SPCS3. The complex induces a local thinning of
CC the ER membrane which is used to measure the length of the signal
CC peptide (SP) h-region of protein substrates. This ensures the
CC selectivity of the complex towards h-regions shorter than 18-20 amino
CC acids. {ECO:0000250|UniProtKB:Q9Y6A9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P83362}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P83362}.
CC -!- PTM: May be phosphorylated. {ECO:0000250|UniProtKB:Q9Y6A9}.
CC -!- SIMILARITY: Belongs to the SPCS1 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-60 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49895.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB24969.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC38696.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC034270; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC049895; AAH49895.1; ALT_INIT; mRNA.
DR EMBL; AK007336; BAB24969.1; ALT_INIT; mRNA.
DR EMBL; AK082928; BAC38696.1; ALT_INIT; mRNA.
DR CCDS; CCDS26903.2; -.
DR RefSeq; NP_081187.2; NM_026911.3.
DR AlphaFoldDB; Q9D958; -.
DR SMR; Q9D958; -.
DR BioGRID; 213174; 1.
DR STRING; 10090.ENSMUSP00000124428; -.
DR iPTMnet; Q9D958; -.
DR PhosphoSitePlus; Q9D958; -.
DR EPD; Q9D958; -.
DR jPOST; Q9D958; -.
DR MaxQB; Q9D958; -.
DR PaxDb; Q9D958; -.
DR PeptideAtlas; Q9D958; -.
DR PRIDE; Q9D958; -.
DR ProteomicsDB; 261120; -.
DR Antibodypedia; 46194; 86 antibodies from 19 providers.
DR DNASU; 69019; -.
DR Ensembl; ENSMUST00000186131; ENSMUSP00000139654; ENSMUSG00000021917.
DR Ensembl; ENSMUST00000226782; ENSMUSP00000154282; ENSMUSG00000021917.
DR GeneID; 69019; -.
DR KEGG; mmu:69019; -.
DR UCSC; uc007swe.2; mouse.
DR CTD; 28972; -.
DR MGI; MGI:1916269; Spcs1.
DR VEuPathDB; HostDB:ENSMUSG00000021917; -.
DR eggNOG; KOG4112; Eukaryota.
DR GeneTree; ENSGT00390000018321; -.
DR InParanoid; Q9D958; -.
DR OrthoDB; 1589808at2759; -.
DR PhylomeDB; Q9D958; -.
DR TreeFam; TF106122; -.
DR Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR BioGRID-ORCS; 69019; 7 hits in 58 CRISPR screens.
DR ChiTaRS; Spcs1; mouse.
DR PRO; PR:Q9D958; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9D958; protein.
DR Bgee; ENSMUSG00000021917; Expressed in seminal vesicle and 258 other tissues.
DR ExpressionAtlas; Q9D958; baseline and differential.
DR Genevisible; Q9D958; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005787; C:signal peptidase complex; ISO:MGI.
DR GO; GO:0043022; F:ribosome binding; IDA:MGI.
DR GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; ISO:MGI.
DR GO; GO:0019082; P:viral protein processing; ISO:MGI.
DR GO; GO:0019068; P:virion assembly; ISO:MGI.
DR InterPro; IPR037713; Spc1.
DR InterPro; IPR009542; Spc1/SPCS1.
DR PANTHER; PTHR13202; PTHR13202; 1.
DR PANTHER; PTHR13202:SF0; PTHR13202:SF0; 1.
DR Pfam; PF06645; SPC12; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..161
FT /note="Signal peptidase complex subunit 1"
FT /id="PRO_0000215155"
FT TOPO_DOM 1..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P83362"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P83362"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P83362"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 40
FT /note="T -> A (in Ref. 1; AAH49895)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="I -> V (in Ref. 2; BAB24969)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 18186 MW; C5AF0BDA801C1C04 CRC64;
MARGGARGCP CPSETSASGA TAEVKRSAGR PCSRYRPPQT LLLNNRLRPF RCRYRSSATM
LEHLSSLPTQ MDYKGQKLAE QMFQGIILFS AIVGFIYGYV AEQFGWTVYI VMAGFAFSCL
LTLPPWPIYR RHPLKWLPVQ DLGTEDKKSG DRKIKRHAKN N
