ID   SPCS1_CAEBR             Reviewed;         113 AA.
AC   Q61CQ8; A8XFM9;
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 1;
DE   AltName: Full=Microsomal signal peptidase 12 kDa subunit;
DE            Short=SPase 12 kDa subunit;
GN   Name=spcs-1 {ECO:0000312|WormBase:CBG12804};
GN   ORFNames=CBG12804 {ECO:0000312|WormBase:CBG12804};
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). Dispensable for SPC enzymatic activity (By
CC       similarity). {ECO:0000250|UniProtKB:P46965,
CC       ECO:0000250|UniProtKB:Q9Y6A9}.
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:Q9Y6A9}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P83362}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P83362}.
CC   -!- SIMILARITY: Belongs to the SPCS1 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; HE600940; CAP31725.3; -; Genomic_DNA.
DR   RefSeq; XP_002640278.1; XM_002640232.1.
DR   AlphaFoldDB; Q61CQ8; -.
DR   SMR; Q61CQ8; -.
DR   STRING; 6238.CBG12804; -.
DR   EnsemblMetazoa; CBG12804.1; CBG12804.1; WBGene00033695.
DR   GeneID; 8582274; -.
DR   KEGG; cbr:CBG_12804; -.
DR   CTD; 8582274; -.
DR   WormBase; CBG12804; CBP17677; WBGene00033695; Cbr-spcs-1.
DR   eggNOG; KOG4112; Eukaryota.
DR   HOGENOM; CLU_134505_1_1_1; -.
DR   InParanoid; Q61CQ8; -.
DR   OMA; WPIYRRS; -.
DR   OrthoDB; 1589808at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
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; IPR037713; Spc1.
DR   InterPro; IPR009542; Spc1/SPCS1.
DR   PANTHER; PTHR13202; PTHR13202; 1.
DR   PANTHER; PTHR13202:SF0; PTHR13202:SF0; 1.
DR   Pfam; PF06645; SPC12; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..113
FT                   /note="Signal peptidase complex subunit 1"
FT                   /id="PRO_0000215157"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..57
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..113
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   REGION          89..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   113 AA;  12729 MW;  FA8BB48DB5C245BB CRC64;
     MDGMIAMLPA PLQQLSSHID FQGQKVAERT YQVILTLAGI IGFFVGYSTQ QLSYAMYTVM
     GAAVFTALII LPPWPFLFRK NPIVWQTPIE EQEASSSSDN EKKDKKKETK KTK