ID   SPCS3_CAEBR             Reviewed;         180 AA.
AC   Q60MW2; A8Y3I8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Signal peptidase complex subunit 3;
DE   AltName: Full=Microsomal signal peptidase 22 kDa subunit;
DE            Short=SPC22;
DE            Short=SPase 22 kDa subunit;
GN   Name=spcs-3 {ECO:0000312|WormBase:CBG22979};
GN   ORFNames=CBG22979 {ECO:0000312|WormBase:CBG22979};
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: Essential component of the signal peptidase complex (SPC)
CC       which catalyzes the cleavage of N-terminal signal sequences from
CC       nascent proteins as they are translocated into the lumen of the
CC       endoplasmic reticulum (By similarity). Essential for the SPC catalytic
CC       activity, possibly by stabilizing and positioning the active center of
CC       the complex close to the lumenal surface (By similarity).
CC       {ECO:0000250|UniProtKB:P61009, ECO:0000250|UniProtKB:Q12133}.
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:P61009}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P61008}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:P61008}.
CC   -!- SIMILARITY: Belongs to the SPCS3 family. {ECO:0000305}.
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DR   EMBL; HE600964; CAP39457.1; -; Genomic_DNA.
DR   RefSeq; XP_002643062.1; XM_002643016.1.
DR   AlphaFoldDB; Q60MW2; -.
DR   SMR; Q60MW2; -.
DR   STRING; 6238.CBG22979; -.
DR   EnsemblMetazoa; CBG22979.1; CBG22979.1; WBGene00041418.
DR   GeneID; 8585056; -.
DR   KEGG; cbr:CBG_22979; -.
DR   CTD; 8585056; -.
DR   WormBase; CBG22979; CBP05465; WBGene00041418; Cbr-spcs-3.
DR   eggNOG; KOG3372; Eukaryota.
DR   HOGENOM; CLU_068714_1_0_1; -.
DR   InParanoid; Q60MW2; -.
DR   OMA; FGCFVTT; -.
DR   OrthoDB; 1514162at2759; -.
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; IPR007653; SPC3.
DR   PANTHER; PTHR12804; PTHR12804; 1.
DR   Pfam; PF04573; SPC22; 1.
DR   PIRSF; PIRSF016089; SPC22; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..180
FT                   /note="Signal peptidase complex subunit 3"
FT                   /id="PRO_0000218942"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P61008"
FT   TRANSMEM        13..33
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..180
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P61008"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   180 AA;  20747 MW;  9187D290A6ACCC19 CRC64;
     MHNLLSRANS LLAFTLWVMA AVTAACFLST VFLDYTVSNH LEVNDIKIRN VRDYATDDKQ
     ADLATLAFNL KVDFSRLFNW NVKQLFVYLV AEYKSAENAV NQVVIWDRIV ERAERVVMDE
     IGVKTKYYFL DDGAHLLKHD NVTFVLRYNV IPNAGYLRLV QSTNQLVVPF PTTYTTTRRS