ID   TIMP3_XENLA             Reviewed;         214 AA.
AC   O73746; Q5D064;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Metalloproteinase inhibitor 3;
DE   AltName: Full=Tissue inhibitor of metalloproteinases 3;
DE            Short=TIMP-3;
DE   Flags: Precursor;
GN   Name=timp3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=9573343; DOI=10.1016/s0378-1119(98)00077-8;
RA   Yang M., Kurkinen M.;
RT   "Cloning and developmental regulation of tissue inhibitor of
RT   metalloproteinases-3 (TIMP3) in Xenopus laevis early embryos.";
RL   Gene 211:95-100(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Complexes with metalloproteinases (such as collagenases) and
CC       irreversibly inactivates them by binding to their catalytic zinc
CC       cofactor. May form part of a tissue-specific acute response to
CC       remodeling stimuli.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC       {ECO:0000305}.
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DR   EMBL; AF042493; AAC41286.1; -; mRNA.
DR   EMBL; BC060423; AAH60423.1; -; mRNA.
DR   RefSeq; NP_001079064.1; NM_001085595.1.
DR   AlphaFoldDB; O73746; -.
DR   SMR; O73746; -.
DR   MEROPS; I35.003; -.
DR   DNASU; 373596; -.
DR   GeneID; 373596; -.
DR   CTD; 373596; -.
DR   Xenbase; XB-GENE-864869; timp3.L.
DR   OrthoDB; 222248at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 373596; Expressed in brain and 19 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   Gene3D; 2.40.50.120; -; 1.
DR   Gene3D; 3.90.370.10; -; 1.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR001820; TIMP.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   InterPro; IPR015612; TIMP3.
DR   InterPro; IPR027465; TIMP_C.
DR   InterPro; IPR030490; TIMP_CS.
DR   PANTHER; PTHR11844; PTHR11844; 1.
DR   PANTHER; PTHR11844:SF22; PTHR11844:SF22; 1.
DR   Pfam; PF00965; TIMP; 1.
DR   SMART; SM00206; NTR; 1.
DR   SUPFAM; SSF50242; SSF50242; 1.
DR   PROSITE; PS50189; NTR; 1.
DR   PROSITE; PS00288; TIMP; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Metal-binding;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..214
FT                   /note="Metalloproteinase inhibitor 3"
FT                   /id="PRO_0000034348"
FT   DOMAIN          27..146
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   REGION          27..30
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   REGION          91..92
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared with metalloproteinase partner"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   SITE            40
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   DISULFID        27..94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        29..121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        39..146
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        148..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        153..158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        166..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
SQ   SEQUENCE   214 AA;  24456 MW;  787AE26E032D712D CRC64;
     MSVCALTLIL GCFLLFLGDI SKPAEGCTCA PSHPQDAFCN SDIVIRAKVV GKKLMKDGPF
     GTMRYTVKQM KMYRGFNKMP QVQYIYTEAS ESLCGVKLEV NKYQYLITGR VYEGKVYTGL
     CNLIERWEKL TFAQRKGLNH RYPLGCTCKI KPCYYLPCFI TSKNECLWTD MLSNFGYPGY
     QSKNYACIKQ KEGYCSWYRG WAPPDKTTIN TTDP