SPCS3_MOUSE
ID SPCS3_MOUSE Reviewed; 180 AA.
AC Q6ZWQ7; Q8C1D0;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Signal peptidase complex subunit 3 {ECO:0000312|MGI:MGI:1923937};
DE AltName: Full=Microsomal signal peptidase 22/23 kDa subunit {ECO:0000305};
DE Short=SPC22/23 {ECO:0000305};
DE Short=SPase 22/23 kDa subunit {ECO:0000305};
GN Name=Spcs3 {ECO:0000312|MGI:MGI:1923937};
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 {ECO:0000312|EMBL:BAC33224.1};
RN [1] {ECO:0000312|EMBL:BAB25035.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC33224.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAC33224.1},
RC Head {ECO:0000312|EMBL:BAC33224.1}, and
RC Pancreas {ECO:0000312|EMBL:BAB25035.1};
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] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:AAH54817.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3 {ECO:0000312|EMBL:AAH54817.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH54817.1};
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, 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: Essential 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 (By similarity). Essential for the SPC catalytic
CC activity, possibly by stabilizing and positioning the active center of
CC the complex close to the lumenal surface (By similarity).
CC {ECO:0000250|UniProtKB:P61009, ECO:0000250|UniProtKB:Q12133}.
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:P61009}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P61008}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P61008}.
CC -!- SIMILARITY: Belongs to the SPCS3 family. {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; AK007432; BAB25035.1; -; mRNA.
DR EMBL; AK028314; BAC25873.1; -; mRNA.
DR EMBL; AK048051; BAC33224.1; -; mRNA.
DR EMBL; AC102933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054817; AAH54817.1; -; mRNA.
DR CCDS; CCDS57621.1; -.
DR RefSeq; NP_083977.1; NM_029701.1.
DR AlphaFoldDB; Q6ZWQ7; -.
DR SMR; Q6ZWQ7; -.
DR STRING; 10090.ENSMUSP00000136527; -.
DR GlyGen; Q6ZWQ7; 1 site.
DR iPTMnet; Q6ZWQ7; -.
DR PhosphoSitePlus; Q6ZWQ7; -.
DR EPD; Q6ZWQ7; -.
DR jPOST; Q6ZWQ7; -.
DR MaxQB; Q6ZWQ7; -.
DR PaxDb; Q6ZWQ7; -.
DR PeptideAtlas; Q6ZWQ7; -.
DR PRIDE; Q6ZWQ7; -.
DR ProteomicsDB; 257555; -.
DR DNASU; 76687; -.
DR Ensembl; ENSMUST00000067476; ENSMUSP00000136527; ENSMUSG00000054408.
DR GeneID; 76687; -.
DR KEGG; mmu:76687; -.
DR UCSC; uc033jfo.1; mouse.
DR CTD; 60559; -.
DR MGI; MGI:1923937; Spcs3.
DR VEuPathDB; HostDB:ENSMUSG00000054408; -.
DR eggNOG; KOG3372; Eukaryota.
DR GeneTree; ENSGT00390000009223; -.
DR HOGENOM; CLU_068714_1_0_1; -.
DR OMA; FGCFVTT; -.
DR OrthoDB; 1514162at2759; -.
DR PhylomeDB; Q6ZWQ7; -.
DR TreeFam; TF300185; -.
DR Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR BioGRID-ORCS; 76687; 18 hits in 73 CRISPR screens.
DR ChiTaRS; Spcs3; mouse.
DR PRO; PR:Q6ZWQ7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6ZWQ7; protein.
DR Bgee; ENSMUSG00000054408; Expressed in lacrimal gland and 243 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0006465; P:signal peptide processing; ISO:MGI.
DR GO; GO:0019082; P:viral protein processing; ISO:MGI.
DR InterPro; IPR007653; SPC3.
DR PANTHER; PTHR12804; PTHR12804; 1.
DR Pfam; PF04573; SPC22; 1.
DR PIRSF; PIRSF016089; SPC22; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..180
FT /note="Signal peptidase complex subunit 3"
FT /id="PRO_0000438396"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P61008"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..180
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P61008"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 17
FT /note="S -> G (in Ref. 1; BAC25873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 20313 MW; 342AB8E0F3F6D71A CRC64;
MNTVLSRANS LFAFSLSVMA ALTFGCFITT AFKDRSVPVR LHVSRIMLKN VEDFTGPRER
SDLGFITFDI TADLENIFDW NVKQLFLYLS AEYSTKNNAL NQVVLWDKIV LRGDNPKLLL
KDMKTKYFFF DDGNGLKGNR NVTLTLSWNV VPNAGILPLV TGSGHVSVPF PDTYEITKSY
