TIMPL_CAEEL
ID TIMPL_CAEEL Reviewed; 158 AA.
AC Q21265;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Putative metalloproteinase inhibitor tag-225;
DE AltName: Full=TIMP-like protein;
DE Flags: Precursor;
GN Name=tag-225; ORFNames=K07C11.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAG50211.1};
RN [1]
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 [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Bristol N2;
RA Kohara Y., Shin'i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA Thierry-Mieg D., Thierry-Mieg J.;
RT "The Caenorhabditis elegans transcriptome project, a complementary view of
RT the genome.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79, 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-79, 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 -!- FUNCTION: Complexes with metalloproteinases and irreversibly
CC inactivates them by binding to their catalytic zinc cofactor.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P16035,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC {ECO:0000305}.
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DR EMBL; FO080570; CCD64760.1; -; Genomic_DNA.
DR EMBL; AF303253; AAG50211.1; -; mRNA.
DR PIR; F89123; F89123.
DR RefSeq; NP_505113.1; NM_072712.5.
DR AlphaFoldDB; Q21265; -.
DR SMR; Q21265; -.
DR BioGRID; 44239; 4.
DR STRING; 6239.K07C11.5; -.
DR iPTMnet; Q21265; -.
DR EPD; Q21265; -.
DR PaxDb; Q21265; -.
DR PeptideAtlas; Q21265; -.
DR EnsemblMetazoa; K07C11.5.1; K07C11.5.1; WBGene00019478.
DR GeneID; 179197; -.
DR KEGG; cel:CELE_K07C11.5; -.
DR UCSC; K07C11.5; c. elegans.
DR CTD; 179197; -.
DR WormBase; K07C11.5; CE07348; WBGene00019478; cri-2.
DR eggNOG; KOG4745; Eukaryota.
DR GeneTree; ENSGT00940000169308; -.
DR HOGENOM; CLU_1688854_0_0_1; -.
DR InParanoid; Q21265; -.
DR OMA; TVLCGQV; -.
DR OrthoDB; 1387411at2759; -.
DR PhylomeDB; Q21265; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-1592389; Activation of Matrix Metalloproteinases.
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:Q21265; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00019478; Expressed in larva and 4 other tissues.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; IBA:GO_Central.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IBA:GO_Central.
DR GO; GO:0010033; P:response to organic substance; IBA:GO_Central.
DR Gene3D; 2.40.50.120; -; 1.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR001820; TIMP.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11844; PTHR11844; 1.
DR Pfam; PF00965; TIMP; 1.
DR SMART; SM00206; NTR; 1.
DR SUPFAM; SSF50242; SSF50242; 1.
DR PROSITE; PS50189; NTR; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Metal-binding; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Protease inhibitor; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..158
FT /note="Putative metalloproteinase inhibitor tag-225"
FT /id="PRO_0000034352"
FT DOMAIN 21..158
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 21..25
FT /note="Involved in metalloproteinase-binding"
FT /evidence="ECO:0000250"
FT REGION 93..94
FT /note="Involved in metalloproteinase-binding"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared with metalloproteinase partner"
FT /evidence="ECO:0000250"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT DISULFID 21..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 23..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 33..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
SQ SEQUENCE 158 AA; 17465 MW; 38439011EEAD8181 CRC64;
MQNLSLSLVI LSVLIAVTLA CKCREQSTKE SFCNAHWVSH VKVKVRVGKQ GLPEGSERKG
LNNLRYTVQH VEVFKKPSNM TTLPDEIFTP SEAPACGLKI AAGHEYLLAG RVEGPNALYT
VLCGQVLPDD RSQTSFENVL EWKNVPQTLQ SQVKSIKC
