PCP5_CAEEL
ID PCP5_CAEEL Reviewed; 507 AA.
AC P34676; Q95PW3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Prolyl carboxy peptidase like protein 5;
DE EC=3.4.-.-;
DE Flags: Precursor;
GN Name=pcp-5; Synonyms=tag-282; ORFNames=ZK688.6;
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], AND ALTERNATIVE SPLICING.
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-125, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125 AND ASN-332, AND
RP IDENTIFICATION BY MASS 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P34676-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P34676-2; Sequence=VSP_005371;
CC -!- SIMILARITY: Belongs to the peptidase S28 family. {ECO:0000305}.
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DR EMBL; FO080277; CCD62538.1; -; Genomic_DNA.
DR EMBL; FO080277; CCD62539.1; -; Genomic_DNA.
DR PIR; S44916; S44916.
DR RefSeq; NP_498718.1; NM_066317.1.
DR RefSeq; NP_498719.1; NM_066318.4.
DR AlphaFoldDB; P34676; -.
DR SMR; P34676; -.
DR BioGRID; 41318; 2.
DR STRING; 6239.ZK688.6b; -.
DR ESTHER; caeel-PCP5; Prolylcarboxypeptidase.
DR MEROPS; S28.A21; -.
DR iPTMnet; P34676; -.
DR EPD; P34676; -.
DR PaxDb; P34676; -.
DR PeptideAtlas; P34676; -.
DR EnsemblMetazoa; ZK688.6.1; ZK688.6.1; WBGene00022801. [P34676-1]
DR EnsemblMetazoa; ZK688.6.2; ZK688.6.2; WBGene00022801. [P34676-1]
DR WormBase; ZK688.6a; CE00464; WBGene00022801; pcp-5. [P34676-1]
DR WormBase; ZK688.6b; CE29648; WBGene00022801; pcp-5. [P34676-2]
DR eggNOG; KOG2183; Eukaryota.
DR GeneTree; ENSGT00940000158099; -.
DR HOGENOM; CLU_020959_0_0_1; -.
DR InParanoid; P34676; -.
DR OMA; TLEDYAM; -.
DR OrthoDB; 555765at2759; -.
DR PhylomeDB; P34676; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:P34676; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022801; Expressed in embryo and 4 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 Alternative splicing; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Serine protease; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..507
FT /note="Prolyl carboxy peptidase like protein 5"
FT /id="PRO_0000027324"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 439
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 466
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MSKNPVQEGFSGYHCLFFTKRKPSKLCWALGKPINKGSSSNCHFIDR
FT FHSFNPLYCIEKHKM (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_005371"
SQ SEQUENCE 507 AA; 56934 MW; F33A8D995B1A9271 CRC64;
MNIFISLAIL IATTHCLTLL RDPVTQNGAS KFEKSIGKYK YEEGYLKAPI DPFAFTNDLE
FDLRYFLNID HYETGGPILF YTGNEGSLEA FAENTGFMWD LAPELKAAVV FVEHRFYGKS
QPFKNESYTD IRHLGYLSSQ QALADFALSV QFFKNEKIKG AQKSAVIAFG GSYGGMLSAW
FRIKYPHIVD GAIAASAPVF WFTDSNIPED VYDFIVTRAF LDAGCNRKAI EKGWIALDEL
AKSDSGRQYL NVLYKLDPKS KLENKDDIGF LKQYIRESME AMAMVNYPYP TSFLSSLPAW
PVKEACKSAS QPGKTQEESA EQLYKIVNLY YNYTGDKSTH CANAAKCDSA YGSLGDPLGW
PFQTCTEMVM PLCGSGYPND FFWKDCPFTS EKYAEFCMQT FSSIHYNKTL LRPLAGGLAF
GATSLPSASN IVFSNGYLDP WSGGGYDHSD KVQGSVISVI LKQGAHHYDL RGAHPQDTEE
VKKVRAMETQ AIKKWIKEKA RNSWRYD
