ID   TIMP3_SCYTO             Reviewed;         214 AA.
AC   Q9W6B4;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 89.
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   Scyliorhinus torazame (Cloudy catshark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC   Scyliorhinus.
OX   NCBI_TaxID=75743;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cartilage;
RX   PubMed=11342115; DOI=10.1016/s0167-4781(00)00255-4;
RA   Kim J.T., Kim M.-S., Bae M.-K., Song H.S., Ahn M.-Y., Kim Y.-J., Lee S.-J.,
RA   Kim K.-W.;
RT   "Cloning and characterization of tissue inhibitor of metalloproteinase-3
RT   (TIMP-3) from shark, Scyliorhinus torazame.";
RL   Biochim. Biophys. Acta 1517:311-315(2001).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed abundantly in brain and cartilage.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC       {ECO:0000305}.
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DR   EMBL; AF110767; AAD26150.1; -; mRNA.
DR   AlphaFoldDB; Q9W6B4; -.
DR   SMR; Q9W6B4; -.
DR   MEROPS; I35.003; -.
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; Glycoprotein; Metal-binding;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..214
FT                   /note="Metalloproteinase inhibitor 3"
FT                   /id="PRO_0000034347"
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   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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;  24498 MW;  BCAD300B8E483557 CRC64;
     MVFSTTAALS LLLALSSMQL SEVSEACTCM PNHPQEAFCN SDIVIRAKVV GKKLLKDGPF
     GTMRYTIKQM KMYRGFSKMQ QVQYIYTEAA ESLCGVRLQV NKFQYLITGR VFDGEVYTGV
     CNFIVPWDRL TLSQRKGLNH RYQYGCNCKI KPCYYLPCFV TAKNECFWTD MLSDQGYMGH
     QAKHYVCIRQ KEGYCSWYRG AAPPDKTRIN ATDP