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 06-MAR-2013, entry version 88. 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 Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=94150718; 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 MEDLINE=99069613; 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 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., RA Mahuran D.J.; RT "Identification of the hydrophobic glycoproteins of Caenorhabditis RT elegans."; RL Glycobiology 15:952-964(2005). CC -!- FUNCTION: Microsomal signal peptidase is a membrane-bound CC endoproteinase that removes signal peptides from nascent proteins CC as they are translocated into the lumen of the endoplasmic CC reticulum (By similarity). CC -!- SUBUNIT: Complex of five different proteins: SEC11L1, SEC11L3, CC SPCS1, SPCS2 and SPCS3 (By similarity). CC -!- SUBCELLULAR LOCATION: Microsome membrane; Single-pass type II CC membrane protein (Potential). Endoplasmic reticulum membrane; CC Single-pass type II membrane protein (Potential). CC -!- SIMILARITY: Belongs to the SPCS3 family. 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 IntAct; P34525; 1. DR STRING; P34525; -. DR PaxDb; P34525; -. DR EnsemblMetazoa; K12H4.4.1; K12H4.4.1; K12H4.4. DR EnsemblMetazoa; K12H4.4.2; K12H4.4.2; K12H4.4. 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; NOG294543; -. DR GeneTree; ENSGT00390000009223; -. DR HOGENOM; HOG000246793; -. DR InParanoid; P34525; -. DR KO; K12948; -. DR OMA; LGFVTFD; -. DR BRENDA; 3.4.21.89; 1045. DR NextBio; 891268; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005787; C:signal peptidase complex; IEA:InterPro. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006915; P:apoptotic process; IMP:WormBase. DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase. DR GO; GO:0040011; P:locomotion; IMP:WormBase. DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase. DR GO; GO:0002119; P:nematode larval development; IMP:WormBase. DR GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:WormBase. DR GO; GO:0000003; P:reproduction; IMP:WormBase. DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro. DR InterPro; IPR007653; SPC22. 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 (Potential). FT TRANSMEM 13 33 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 34 180 Lumenal (Potential). FT CARBOHYD 141 141 N-linked (GlcNAc...). 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 //