PCP1_CAEEL
ID PCP1_CAEEL Reviewed; 565 AA.
AC P34610;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Putative serine protease pcp-1;
DE EC=3.4.-.-;
DE Flags: Precursor;
GN Name=pcp-1; ORFNames=ZK112.1;
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-257, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- SIMILARITY: Belongs to the peptidase S28 family. {ECO:0000305}.
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DR EMBL; FO080308; CCD62762.1; -; Genomic_DNA.
DR PIR; S44886; S44886.
DR RefSeq; NP_498688.1; NM_066287.5.
DR AlphaFoldDB; P34610; -.
DR SMR; P34610; -.
DR BioGRID; 41294; 1.
DR STRING; 6239.ZK112.1; -.
DR ESTHER; caeel-yog1; Prolylcarboxypeptidase.
DR MEROPS; S28.A17; -.
DR iPTMnet; P34610; -.
DR EPD; P34610; -.
DR PaxDb; P34610; -.
DR PeptideAtlas; P34610; -.
DR EnsemblMetazoa; ZK112.1.1; ZK112.1.1; WBGene00003956.
DR GeneID; 176086; -.
DR KEGG; cel:CELE_ZK112.1; -.
DR UCSC; ZK112.1; c. elegans.
DR CTD; 176086; -.
DR WormBase; ZK112.1; CE25679; WBGene00003956; pcp-1.
DR eggNOG; KOG2183; Eukaryota.
DR HOGENOM; CLU_020959_0_1_1; -.
DR InParanoid; P34610; -.
DR OMA; DNASCHA; -.
DR OrthoDB; 555765at2759; -.
DR PhylomeDB; P34610; -.
DR PRO; PR:P34610; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003956; Expressed in larva and 3 other tissues.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.980; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR008758; Peptidase_S28.
DR InterPro; IPR042269; Ser_carbopepase_S28_SKS.
DR Pfam; PF05577; Peptidase_S28; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Serine protease;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..565
FT /note="Putative serine protease pcp-1"
FT /id="PRO_0000027323"
FT ACT_SITE 177
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 451
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 479
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 565 AA; 62838 MW; 52D689472013B759 CRC64;
MRWFLVLLLV ALVSVEASRR SRLFKKLYQK ASNYDAAPSN VQTVWYKNMK LDHFTWGDTR
TFDMRVMWNN TFYKPGGPIF FYTGNEGGLE SFVTATGMMF DLAPMFNASI IFAEHRFYGQ
TQPFGNQSYA SLANVGYLTS EQALADYAEL LTELKRDNNQ FKMTFPAATQ VISFGGSYGG
MLSAWFRQKY PHIVKGAWAG SAPLIYMNGG GVDPGAFDHI TSRTYIDNGC NRFILANAWN
ATLNLSSTDA GRQWLNNNTV FKLDPRTKIR NQTDGWNLNA YLREAIEYMA MVDYPYPTGF
LEPLPAWPVT VACGYMNANG TSFSDKDLVK AVANAANIYY NYNRDPNFTY CIDFSICGDQ
GTGGLGGDEL GWPWQECSEI IMAMCASGGS NDVFWNECGK DIYQTLQQGC VSIFKSMGWT
PKNWNIDAVK TLYGYDLSGS SNLILTQGHL DPWSGGGYKV DQNNAARGIY VLEIPGSAHH
LDLRQPNTCD PNTVTNARFQ IIQILKCWVD PNCNTIPTIS PLPSISIPNG DCKDVVGGYP
WGQTTGATVS NSFILAILAS LYAMF
