SPCS2_CAEEL
ID SPCS2_CAEEL Reviewed; 180 AA.
AC Q9XWW1;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=spcs-2 {ECO:0000312|WormBase:Y37D8A.10};
GN Synonyms=hpo-21 {ECO:0000312|WormBase:Y37D8A.10};
GN ORFNames=Y37D8A.10 {ECO:0000312|WormBase:Y37D8A.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 (SPC) composed of a
CC catalytic subunit sec-11 and three accessory subunits spcs-1, spcs-2
CC and spcs-3. The complex induces a local thinning of the ER membrane
CC which is used to measure the length of the signal peptide (SP) h-region
CC of protein substrates. This ensures the selectivity of the complex
CC towards h-regions shorter than 18-20 amino acids.
CC {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}.
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DR EMBL; BX284603; CAA21529.1; -; Genomic_DNA.
DR PIR; T26628; T26628.
DR RefSeq; NP_499676.1; NM_067275.6.
DR AlphaFoldDB; Q9XWW1; -.
DR SMR; Q9XWW1; -.
DR BioGRID; 41876; 3.
DR DIP; DIP-25610N; -.
DR IntAct; Q9XWW1; 1.
DR STRING; 6239.Y37D8A.10; -.
DR EPD; Q9XWW1; -.
DR PaxDb; Q9XWW1; -.
DR PeptideAtlas; Q9XWW1; -.
DR EnsemblMetazoa; Y37D8A.10.1; Y37D8A.10.1; WBGene00012550.
DR GeneID; 176703; -.
DR KEGG; cel:CELE_Y37D8A.10; -.
DR UCSC; Y37D8A.10; c. elegans.
DR CTD; 176703; -.
DR WormBase; Y37D8A.10; CE20214; WBGene00012550; spcs-2.
DR eggNOG; KOG4072; Eukaryota.
DR GeneTree; ENSGT00440000038181; -.
DR HOGENOM; CLU_094622_0_0_1; -.
DR InParanoid; Q9XWW1; -.
DR OMA; DMRKYDD; -.
DR OrthoDB; 1395649at2759; -.
DR PhylomeDB; Q9XWW1; -.
DR PRO; PR:Q9XWW1; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00012550; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016529; C:sarcoplasmic reticulum; HDA:WormBase.
DR GO; GO:0005787; C:signal peptidase complex; IBA:GO_Central.
DR GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR InterPro; IPR009582; Spc2/SPCS2.
DR PANTHER; PTHR13085; PTHR13085; 1.
DR Pfam; PF06703; SPC25; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..180
FT /note="Signal peptidase complex subunit 2"
FT /id="PRO_0000221165"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q28250"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..72
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q28250"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q28250"
SQ SEQUENCE 180 AA; 20597 MW; BC02B027532D2A49 CRC64;
MTDEPVKVVN KWDGPTVKNA LDEVVKKILN DKVGWTESHN LMNLRLLISF IGVAFSAFAC
GYDYYEPFPK SKIVLAVCSV SYFICMGILQ MYQWYVEKDC IYEATEVDGK QSRKWAWSSE
IKAHDDKYTL SAEFKKEGRS GQGKITKSIG AYIDNDGEII VPLVKKEVDD LYNRLIRSEQ
