ID   SPCS2_CAEBR             Reviewed;         180 AA.
AC   Q615A2; A8XMR3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
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:CBG15767};
GN   Synonyms=hpo-21 {ECO:0000312|WormBase:CBG15767};
GN   ORFNames=CBG15767 {ECO:0000312|WormBase:CBG15767};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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; HE600979; CAP33939.1; -; Genomic_DNA.
DR   RefSeq; XP_002640876.1; XM_002640830.1.
DR   AlphaFoldDB; Q615A2; -.
DR   SMR; Q615A2; -.
DR   STRING; 6238.CBG15767; -.
DR   EnsemblMetazoa; CBG15767.1; CBG15767.1; WBGene00035909.
DR   GeneID; 8582870; -.
DR   KEGG; cbr:CBG_15767; -.
DR   CTD; 8582870; -.
DR   WormBase; CBG15767; CBP03769; WBGene00035909; Cbr-spcs-2.
DR   eggNOG; KOG4072; Eukaryota.
DR   HOGENOM; CLU_094622_0_0_1; -.
DR   InParanoid; Q615A2; -.
DR   OMA; DMRKYDD; -.
DR   OrthoDB; 1395649at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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_0000221164"
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;  20687 MW;  90EB56B4F6EF95F3 CRC64;
     MSDERITVVN KWDGPTVKNG LDEVVKKILN DKVGWTEQHN LMNLRLLISF IGVAFSAFAC
     GYDFYAPFPK SKIVLLVCSV SYFICMGVLQ LFQWYVEKDC FYEANEVDGK QTRKWAWSSE
     IKAHDDKYVL SAEFKKEGRS GQGKIIKSIG AYIDNDGEIM IPLVQREVDD LWARLIRSEQ