CPI1_CAEEL
ID CPI1_CAEEL Reviewed; 139 AA.
AC G5EDZ9;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cystatin cpi-1 {ECO:0000305};
DE AltName: Full=Cysele1 {ECO:0000303|PubMed:12704112};
DE Flags: Precursor;
GN Name=cpi-1 {ECO:0000312|WormBase:K08B4.6};
GN ORFNames=K08B4.6 {ECO:0000312|WormBase:K08B4.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:CAC33821.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=12704112; DOI=10.1128/iai.71.5.2422-2429.2003;
RA Schierack P.S., Lucius R., Sonnenburg B., Schilling K., Hartmann S.;
RT "Parasite-specific immunomodulatory functions of filarial cystatin.";
RL Infect. Immun. 71:2422-2429(2003).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION.
RX PubMed=15664654; DOI=10.1016/j.molbiopara.2004.11.008;
RA Murray J., Manoury B., Balic A., Watts C., Maizels R.M.;
RT "Bm-CPI-2, a cystatin from Brugia malayi nematode parasites, differs from
RT Caenorhabditis elegans cystatins in a specific site mediating inhibition of
RT the antigen-processing enzyme AEP.";
RL Mol. Biochem. Parasitol. 139:197-203(2005).
RN [4] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=16857685; DOI=10.1074/jbc.m600254200;
RA Hashmi S., Zhang J., Oksov Y., Ji Q., Lustigman S.;
RT "The Caenorhabditis elegans CPI-2a cystatin-like inhibitor has an essential
RT regulatory role during oogenesis and fertilization.";
RL J. Biol. Chem. 281:28415-28429(2006).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=24001183; DOI=10.1017/s0031182013001364;
RA Phiri A.M., De Pomerai D., Buttle D.J., Behnke J.M.;
RT "Developing a rapid throughput screen for detection of nematicidal activity
RT of plant cysteine proteinases: the role of Caenorhabditis elegans
RT cystatins.";
RL Parasitology 141:164-180(2014).
CC -!- FUNCTION: Cysteine protease inhibitor which inhibits members of the
CC peptidase C1 family (PubMed:12704112, PubMed:15664654). Does not
CC inhibit asparaginyl endopeptidase (PubMed:15664654). May play a
CC protective role against exogenous cysteine proteases derived from soil
CC bacteria or fungi, or rotting fruits and vegetation (PubMed:24001183).
CC {ECO:0000269|PubMed:12704112, ECO:0000269|PubMed:15664654,
CC ECO:0000269|PubMed:24001183}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adults (at
CC protein level). Expression transiently increases prior to the larval
CC L2/L3, L3/L4 and L4/adult molts. {ECO:0000269|PubMed:16857685}.
CC -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000255,
CC ECO:0000255|RuleBase:RU362130}.
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DR EMBL; AJ310669; CAC33821.1; -; mRNA.
DR EMBL; BX284604; CCD72381.1; -; Genomic_DNA.
DR PIR; T33740; T33740.
DR RefSeq; NP_500915.1; NM_068514.5.
DR AlphaFoldDB; G5EDZ9; -.
DR SMR; G5EDZ9; -.
DR IntAct; G5EDZ9; 1.
DR STRING; 6239.K08B4.6; -.
DR MEROPS; I25.032; -.
DR EPD; G5EDZ9; -.
DR PaxDb; G5EDZ9; -.
DR PeptideAtlas; G5EDZ9; -.
DR EnsemblMetazoa; K08B4.6.1; K08B4.6.1; WBGene00000535.
DR GeneID; 177372; -.
DR KEGG; cel:CELE_K08B4.6; -.
DR CTD; 177372; -.
DR WormBase; K08B4.6; CE18035; WBGene00000535; cpi-1.
DR eggNOG; ENOG502SC50; Eukaryota.
DR GeneTree; ENSGT00390000011592; -.
DR HOGENOM; CLU_1847012_0_0_1; -.
DR InParanoid; G5EDZ9; -.
DR OMA; QITTANC; -.
DR OrthoDB; 1565344at2759; -.
DR PRO; PR:G5EDZ9; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000535; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IBA:GO_Central.
DR CDD; cd00042; CY; 1.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR Pfam; PF00031; Cystatin; 1.
DR SMART; SM00043; CY; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW Signal; Thiol protease inhibitor.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..139
FT /note="Cystatin cpi-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5015019726"
FT MOTIF 65..69
FT /note="Secondary area of contact"
FT /evidence="ECO:0000305"
FT SITE 23
FT /note="Reactive site"
FT /evidence="ECO:0000305"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 83..99
FT /evidence="ECO:0000250|UniProtKB:P01038"
SQ SEQUENCE 139 AA; 15091 MW; 796F1CD81166CEFE CRC64;
MRFILLIALV FAVLDGINCQ IAGGLSDVNA SEYTGAAWNS VPEINSKNNG QNYMVPIKVV
KAQVQVVAGT NTVLEVLVGE STCPRQGSVQ ASQVTAANCP LKSGGKRELY KVSIWEKPWE
NFKQTKAEKI RGVKPDEKI
