ID A0A140LHR3_MOUSE Unreviewed; 190 AA.
AC A0A140LHR3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Signal peptidase complex subunit 2 {ECO:0000256|ARBA:ARBA00017057, ECO:0000256|RuleBase:RU368033};
GN Name=Spcs2 {ECO:0000313|Ensembl:ENSMUSP00000146514.2,
GN ECO:0000313|MGI:MGI:1913874};
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:0000313|Ensembl:ENSMUSP00000146514.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000146514.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000146514.2,
RC ECO:0000313|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 [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000146514.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000146514.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. Enhances the enzymatic activity of SPC and facilitates the
CC interactions between different components of the translocation site.
CC {ECO:0000256|RuleBase:RU368033}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368033}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU368033}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SPCS2 family.
CC {ECO:0000256|ARBA:ARBA00007324, ECO:0000256|RuleBase:RU368033}.
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 RefSeq; XP_006508180.1; XM_006508117.3.
DR AlphaFoldDB; A0A140LHR3; -.
DR SMR; A0A140LHR3; -.
DR jPOST; A0A140LHR3; -.
DR ProteomicsDB; 353186; -.
DR Antibodypedia; 2848; 147 antibodies from 20 providers.
DR DNASU; 66624; -.
DR Ensembl; ENSMUST00000207063.2; ENSMUSP00000146514.2; ENSMUSG00000035227.8.
DR AGR; MGI:1913874; -.
DR MGI; MGI:1913874; Spcs2.
DR VEuPathDB; HostDB:ENSMUSG00000035227; -.
DR GeneTree; ENSGT00440000038181; -.
DR OrthoDB; 2903540at2759; -.
DR BioGRID-ORCS; 66624; 19 hits in 79 CRISPR screens.
DR ChiTaRS; Spcs2; mouse.
DR Proteomes; UP000000589; Chromosome 7.
DR Bgee; ENSMUSG00000035227; Expressed in lacrimal gland and 260 other cell types or tissues.
DR ExpressionAtlas; A0A140LHR3; baseline and differential.
DR GO; GO:0005787; C:signal peptidase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006465; P:signal peptide processing; IEA:UniProtKB-UniRule.
DR InterPro; IPR009582; Spc2/SPCS2.
DR PANTHER; PTHR13085; MICROSOMAL SIGNAL PEPTIDASE 25 KDA SUBUNIT; 1.
DR PANTHER; PTHR13085:SF0; SIGNAL PEPTIDASE COMPLEX SUBUNIT 2; 1.
DR Pfam; PF06703; SPC25; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU368033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368033};
KW Proteomics identification {ECO:0007829|EPD:A0A140LHR3,
KW ECO:0007829|MaxQB:A0A140LHR3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368033}.
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368033"
FT TRANSMEM 77..95
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368033"
SQ SEQUENCE 190 AA; 21998 MW; 0B43955CBABCB38F CRC64;
MQWKIDDKPV KIDKWDGSAV KNSLDDSAKK VLLEKYKYVE NFGLIDGRLT ICTISCFFAI
VALIWDYMHP FPESKPVLAL CVISYFVMMG ILTIYTSYKE KSIFLVAHRK DPTGMDPDDI
WQLSSSLKRF DDKYTLKLTF ISGRTKQQRE AEFTKSIAKF FDHSGTLVMD AYEPEISRLH
DSLATERKIK
//
