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 10-APR-2019, entry version 123. DE RecName: Full=Probable signal peptidase complex subunit 3; DE EC=3.4.-.-; DE AltName: Full=Microsomal signal peptidase 22 kDa subunit; DE Short=SPC22; DE Short=SPase 22 kDa subunit; GN ORFNames=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., RA Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A., RA Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A., RA Fulton L., Gardner A., Green P., Hawkins T., Hillier L., Jier M., RA Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N., RA Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M., RA Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R., RA Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R., RA Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K., RA Waterston R., Watson A., Weinstock L., Wilkinson-Sproat J., RA 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 RT investigating biology."; RL Science 282:2012-2018(1998). RN [3] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-141, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=15888633; DOI=10.1093/glycob/cwi075; RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., RA Mahuran D.J.; RT "Identification of the hydrophobic glycoproteins of Caenorhabditis RT elegans."; RL Glycobiology 15:952-964(2005). CC -!- FUNCTION: Component of the microsomal signal peptidase complex CC which removes signal peptides and other N-terminal peptides from CC nascent proteins as they are translocated into the lumen of the CC endoplasmic reticulum. {ECO:0000250|UniProtKB:P61009}. CC -!- SUBUNIT: Complex of five different proteins: SEC11L1, SEC11L3, CC SPCS1, SPCS2 and SPCS3. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Microsome membrane CC {ECO:0000250|UniProtKB:P61008}; Single-pass type II membrane CC protein {ECO:0000305}. Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q12133}; Single-pass type II membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the SPCS3 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; FO081380; CCD71196.1; -; Genomic_DNA. DR PIR; S44854; S44854. DR RefSeq; NP_498755.1; NM_066354.4. DR UniGene; Cel.20528; -. DR IntAct; P34525; 1. DR STRING; 6239.K12H4.4; -. DR iPTMnet; P34525; -. DR EPD; P34525; -. DR PaxDb; P34525; -. DR PeptideAtlas; P34525; -. DR PRIDE; P34525; -. DR EnsemblMetazoa; K12H4.4; K12H4.4; 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; -. DR eggNOG; KOG3372; Eukaryota. DR eggNOG; ENOG4110TZP; LUCA. DR GeneTree; ENSGT00940000169388; -. DR HOGENOM; HOG000246793; -. DR InParanoid; P34525; -. DR KO; K12948; -. DR OMA; FKDRRVP; -. 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 5 organ(s), highest expression level in multi-cellular organism. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005787; C:signal peptidase complex; IBA:GO_Central. DR GO; GO:0008233; F:peptidase activity; 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 Complete proteome; Endoplasmic reticulum; Glycoprotein; Hydrolase; KW Membrane; Microsome; Protease; Reference proteome; Signal-anchor; KW Transmembrane; Transmembrane helix. FT CHAIN 1 180 Probable signal peptidase complex subunit FT 3. FT /FTId=PRO_0000218943. FT TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 13 33 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 34 180 Lumenal. {ECO:0000255}. FT CARBOHYD 141 141 N-linked (GlcNAc...) asparagine. FT {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 //