SPCS3_CAEEL
ID SPCS3_CAEEL Reviewed; 180 AA.
AC P34525;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 137.
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:K12H4.4};
GN ORFNames=K12H4.4 {ECO:0000312|WormBase:K12H4.4};
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=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
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).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-141, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
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; BX284603; CCD71196.1; -; Genomic_DNA.
DR PIR; S44854; S44854.
DR RefSeq; NP_498755.1; NM_066354.4.
DR AlphaFoldDB; P34525; -.
DR SMR; P34525; -.
DR BioGRID; 41339; 2.
DR IntAct; P34525; 1.
DR STRING; 6239.K12H4.4; -.
DR MEROPS; X45.001; -.
DR iPTMnet; P34525; -.
DR EPD; P34525; -.
DR PaxDb; P34525; -.
DR PeptideAtlas; P34525; -.
DR EnsemblMetazoa; K12H4.4.1; K12H4.4.1; WBGene00019679.
DR GeneID; 176133; -.
DR KEGG; cel:CELE_K12H4.4; -.
DR UCSC; K12H4.4.1; c. elegans.
DR CTD; 176133; -.
DR WormBase; K12H4.4; CE00269; WBGene00019679; spcs-3.
DR eggNOG; KOG3372; Eukaryota.
DR GeneTree; ENSGT00940000169388; -.
DR HOGENOM; CLU_068714_1_0_1; -.
DR InParanoid; P34525; -.
DR OMA; FGCFVTT; -.
DR OrthoDB; 1514162at2759; -.
DR PhylomeDB; P34525; -.
DR BRENDA; 3.4.21.89; 1045.
DR PRO; PR:P34525; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00019679; Expressed in embryo and 4 other tissues.
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 1: Evidence at protein level;
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_0000218943"
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:0000269|PubMed:15888633"
SQ SEQUENCE 180 AA; 20687 MW; 4CAEB791F3374EB8 CRC64;
MHNLLSRANA LLAFTLWVMA AVTAACFLST VFLDYTVPTK LTVNDVKVRN VVDYATDEQQ
ADLATLNFNL KVDFSKIFNW NVKQLFVYLV AEYKSKVNEV NQVVLWDRIV ERADRVVMDE
IGVKSKYYFL DDGTNLLNHK NVTFVLRYNV IPNSGYLRLV QSSDQVVVPF PTTYTTTRRS
