SPCS2_MOUSE
ID SPCS2_MOUSE Reviewed; 226 AA.
AC Q9CYN2; Q3THR2; Q80X74; Q921V8; Q9CXK1;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Signal peptidase complex subunit 2;
DE AltName: Full=Microsomal signal peptidase 25 kDa subunit;
DE Short=SPase 25 kDa subunit;
GN Name=Spcs2; Synonyms=Spc25;
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, and DBA/2J; TISSUE=Embryo, and Medulla oblongata;
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, and FVB/N; TISSUE=Blastocyst, and 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: 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). Enhances the enzymatic activity of SPC and
CC facilitates the interactions between different components of the
CC translocation site (By similarity). {ECO:0000250|UniProtKB:Q04969,
CC ECO:0000250|UniProtKB:Q15005}.
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 SEC11A or SEC11C and SPCS1. The complex induces a local
CC thinning of the ER membrane which is used to measure the length of the
CC signal 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:Q15005}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q28250}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q28250}.
CC -!- SIMILARITY: Belongs to the SPCS2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29262.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK014310; BAB29262.1; ALT_SEQ; mRNA.
DR EMBL; AK017504; BAB30777.1; -; mRNA.
DR EMBL; AK077510; BAC36836.1; -; mRNA.
DR EMBL; AK134578; BAE22190.1; -; mRNA.
DR EMBL; AK168173; BAE40134.1; -; mRNA.
DR EMBL; BC010547; AAH10547.2; -; mRNA.
DR EMBL; BC050150; AAH50150.1; -; mRNA.
DR CCDS; CCDS40033.1; -.
DR RefSeq; NP_079944.1; NM_025668.3.
DR AlphaFoldDB; Q9CYN2; -.
DR SMR; Q9CYN2; -.
DR BioGRID; 211603; 11.
DR IntAct; Q9CYN2; 9.
DR STRING; 10090.ENSMUSP00000041152; -.
DR iPTMnet; Q9CYN2; -.
DR PhosphoSitePlus; Q9CYN2; -.
DR SwissPalm; Q9CYN2; -.
DR EPD; Q9CYN2; -.
DR jPOST; Q9CYN2; -.
DR MaxQB; Q9CYN2; -.
DR PaxDb; Q9CYN2; -.
DR PeptideAtlas; Q9CYN2; -.
DR PRIDE; Q9CYN2; -.
DR ProteomicsDB; 261121; -.
DR TopDownProteomics; Q9CYN2; -.
DR Antibodypedia; 2848; 123 antibodies from 20 providers.
DR DNASU; 66624; -.
DR Ensembl; ENSMUST00000036274; ENSMUSP00000041152; ENSMUSG00000035227.
DR GeneID; 66624; -.
DR KEGG; mmu:66624; -.
DR UCSC; uc009imd.1; mouse.
DR CTD; 9789; -.
DR MGI; MGI:1913874; Spcs2.
DR VEuPathDB; HostDB:ENSMUSG00000035227; -.
DR eggNOG; KOG4072; Eukaryota.
DR GeneTree; ENSGT00440000038181; -.
DR HOGENOM; CLU_094622_0_0_1; -.
DR InParanoid; Q9CYN2; -.
DR OMA; DMRKYDD; -.
DR OrthoDB; 1395649at2759; -.
DR PhylomeDB; Q9CYN2; -.
DR TreeFam; TF314545; -.
DR Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR BioGRID-ORCS; 66624; 19 hits in 74 CRISPR screens.
DR ChiTaRS; Spcs2; mouse.
DR PRO; PR:Q9CYN2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CYN2; protein.
DR Bgee; ENSMUSG00000035227; Expressed in lacrimal gland and 257 other tissues.
DR ExpressionAtlas; Q9CYN2; baseline and differential.
DR Genevisible; Q9CYN2; 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; ISO:MGI.
DR GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; ISO:MGI.
DR InterPro; IPR009582; Spc2/SPCS2.
DR PANTHER; PTHR13085; PTHR13085; 1.
DR Pfam; PF06703; SPC25; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:16452087"
FT CHAIN 2..226
FT /note="Signal peptidase complex subunit 2"
FT /id="PRO_0000221160"
FT TOPO_DOM 2..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q28250"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..111
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q28250"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q28250"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 169
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15005"
FT MOD_RES 191
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15005"
FT CONFLICT 110
FT /note="S -> P (in Ref. 2; AAH50150)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="E -> D (in Ref. 1; BAB29262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 24978 MW; F8516C51FFED4DF9 CRC64;
MAASASQGGR SGGGGGSSGA GGGPSCGTSS SRSGLLDKWK IDDKPVKIDK WDGSAVKNSL
DDSAKKVLLE KYKYVENFGL IDGRLTICTI SCFFAIVALI WDYMHPFPES KPVLALCVIS
YFVMMGILTI YTSYKEKSIF LVAHRKDPTG MDPDDIWQLS SSLKRFDDKY TLKLTFISGR
TKQQREAEFT KSIAKFFDHS GTLVMDAYEP EISRLHDSLA TERKIK
