ID   SPCS1_CAEEL             Reviewed;         105 AA.
AC   O44953;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
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:C34B2.10};
GN   ORFNames=C34B2.10 {ECO:0000312|WormBase:C34B2.10};
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). 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}.
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DR   EMBL; BX284601; CCD62128.1; -; Genomic_DNA.
DR   PIR; T32884; T32884.
DR   RefSeq; NP_492797.1; NM_060396.4.
DR   AlphaFoldDB; O44953; -.
DR   SMR; O44953; -.
DR   STRING; 6239.C34B2.10; -.
DR   EPD; O44953; -.
DR   PaxDb; O44953; -.
DR   PeptideAtlas; O44953; -.
DR   EnsemblMetazoa; C34B2.10.1; C34B2.10.1; WBGene00016395.
DR   GeneID; 172967; -.
DR   KEGG; cel:CELE_C34B2.10; -.
DR   UCSC; C34B2.10.1; c. elegans.
DR   CTD; 172967; -.
DR   WormBase; C34B2.10; CE16898; WBGene00016395; spcs-1.
DR   eggNOG; KOG4112; Eukaryota.
DR   GeneTree; ENSGT00390000018321; -.
DR   HOGENOM; CLU_134505_1_1_1; -.
DR   InParanoid; O44953; -.
DR   OMA; WPIYRRS; -.
DR   OrthoDB; 1589808at2759; -.
DR   PhylomeDB; O44953; -.
DR   PRO; PR:O44953; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00016395; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
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..105
FT                   /note="Signal peptidase complex subunit 1"
FT                   /id="PRO_0000215158"
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..56
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..105
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
SQ   SEQUENCE   105 AA;  11777 MW;  1C041B5D94A5C471 CRC64;
     MDGMIAMLPA PLQKLSSHID FQGQKVAERT YQVILTIAGI IGFLVGFWTQ QLSYAMFTVL
     GASAFTALII LPPWPFLFRK NPIVWHTPAE PQESGDKKKE TKKTK