CPI2_CAEEL
ID CPI2_CAEEL Reviewed; 143 AA.
AC G5ECM9;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cystatin cpi-2 {ECO:0000305};
DE Short=Ce-cpi-2a {ECO:0000303|PubMed:16857685};
DE AltName: Full=Cysele2 {ECO:0000303|PubMed:12704112};
DE Flags: Precursor;
GN Name=cpi-2 {ECO:0000312|WormBase:R01B10.1a};
GN ORFNames=R01B10.1 {ECO:0000312|WormBase:R01B10.1a};
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:CAC33822.1}
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, AND DEVELOPMENTAL STAGE.
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP 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). Required for the
CC uptake and/or processing of yolk proteins during the development of
CC oocytes, probably by regulating the catalytic activity of cysteine
CC proteases cpl-1 and cpz-1 (PubMed:16857685). May play a protective role
CC against exogenous cysteine proteases derived from soil bacteria or
CC fungi, or rotting fruits and vegetation (PubMed:24001183).
CC {ECO:0000269|PubMed:12704112, ECO:0000269|PubMed:15664654,
CC ECO:0000269|PubMed:16857685, ECO:0000269|PubMed:24001183}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16857685}. Secreted
CC {ECO:0000269|PubMed:16857685}. Cytoplasmic granule
CC {ECO:0000269|PubMed:16857685}. Note=Localizes to the sheath cell
CC cytoplasm surrounding germ cells and oocytes. Localizes to yolk
CC granules in the developing oocyte. {ECO:0000269|PubMed:16857685}.
CC -!- TISSUE SPECIFICITY: Expressed in germ cells, developing oocytes and
CC sperm, sheath cells surrounding germ cells and oocytes and in the
CC eggshell (at protein level) (PubMed:16857685). Expressed in the
CC pharyngeal gland, pharyngeal muscles and some hypodermal cells in the
CC tail (PubMed:16857685). {ECO:0000269|PubMed:16857685}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adults (at
CC protein level) (PubMed:15664654, PubMed:16857685). Expressed in the
CC ecdysed cuticle during molting (at protein level) (PubMed:16857685). In
CC embryos and larvae, expressed in intestinal, hypodermal and pharyngeal
CC cells (PubMed:16857685). Expression transiently increases during early
CC embryonic stages and prior to the larval L1/L2, L2/L3, L3/L4 and
CC L4/adult molts (PubMed:16857685). {ECO:0000269|PubMed:15664654,
CC ECO:0000269|PubMed:16857685}.
CC -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000255,
CC ECO:0000255|RuleBase:RU362130}.
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DR EMBL; AJ310670; CAC33822.1; -; mRNA.
DR EMBL; BX284605; CCD70263.1; -; Genomic_DNA.
DR PIR; T33301; T33301.
DR RefSeq; NP_504565.1; NM_072164.7.
DR AlphaFoldDB; G5ECM9; -.
DR SMR; G5ECM9; -.
DR STRING; 6239.R01B10.1a; -.
DR MEROPS; I25.032; -.
DR EPD; G5ECM9; -.
DR PaxDb; G5ECM9; -.
DR PeptideAtlas; G5ECM9; -.
DR EnsemblMetazoa; R01B10.1a.1; R01B10.1a.1; WBGene00000534.
DR GeneID; 178992; -.
DR KEGG; cel:CELE_R01B10.1; -.
DR CTD; 178992; -.
DR WormBase; R01B10.1a; CE25962; WBGene00000534; cpi-2.
DR eggNOG; ENOG502SC50; Eukaryota.
DR GeneTree; ENSGT00390000011592; -.
DR HOGENOM; CLU_1847012_0_0_1; -.
DR InParanoid; G5ECM9; -.
DR OMA; QVTIWEK; -.
DR OrthoDB; 1565344at2759; -.
DR PhylomeDB; G5ECM9; -.
DR Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR PRO; PR:G5ECM9; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000534; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0042718; C:yolk granule; IDA:UniProtKB.
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 GO; GO:1903188; P:positive regulation of vitellogenesis; IMP:UniProtKB.
DR GO; GO:0060281; P:regulation of oocyte development; IMP:UniProtKB.
DR GO; GO:0070613; P:regulation of protein processing; IMP:UniProtKB.
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 Cytoplasm; Disulfide bond; Protease inhibitor; Reference proteome;
KW Secreted; Signal; Thiol protease inhibitor.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..143
FT /note="Cystatin cpi-2"
FT /evidence="ECO:0000255"
FT /id="PRO_5015019724"
FT MOTIF 70..74
FT /note="Secondary area of contact"
FT /evidence="ECO:0000305"
FT SITE 24
FT /note="Reactive site"
FT /evidence="ECO:0000305"
FT DISULFID 88..103
FT /evidence="ECO:0000250|UniProtKB:P01038"
SQ SEQUENCE 143 AA; 15697 MW; 38DF9B87918AC5A0 CRC64;
MKAILVFALI AISIISVNAG MMTGGSVEQD ASQKEYSDKA WKAVKGINDQ ASNNGPYYYA
PIKVTKASTQ VVAGISTKLE VLVGESNCKK GELQAHEITS SNCQIKDGGS RALYQVTIWE
KPWENFEQFT VEKIRDVTAD EQF
