ID   TIMP3_RABIT             Reviewed;         151 AA.
AC   O97590;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Metalloproteinase inhibitor 3;
DE   AltName: Full=Tissue inhibitor of metalloproteinases 3;
DE            Short=TIMP-3;
DE   Flags: Fragment;
GN   Name=TIMP3;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white;
RX   PubMed=9837780; DOI=10.1006/bbrc.1998.9734;
RA   Reno C., Boykiw R., Martinez M.L., Hart D.A.;
RT   "Temporal alterations in mRNA levels for proteinases and inhibitors and
RT   their potential regulators in the healing medial collateral ligament.";
RL   Biochem. Biophys. Res. Commun. 252:757-763(1998).
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   -!- SUBUNIT: Interacts with EFEMP1. {ECO:0000250}.
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; AF069714; AAC95006.1; -; mRNA.
DR   AlphaFoldDB; O97590; -.
DR   SMR; O97590; -.
DR   STRING; 9986.ENSOCUP00000007183; -.
DR   MEROPS; I35.003; -.
DR   PRIDE; O97590; -.
DR   eggNOG; KOG4745; Eukaryota.
DR   InParanoid; O97590; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
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   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.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Metalloenzyme inhibitor;
KW   Metalloprotease inhibitor; Protease inhibitor; Reference proteome;
KW   Secreted.
FT   CHAIN           <1..>151
FT                   /note="Metalloproteinase inhibitor 3"
FT                   /id="PRO_0000220985"
FT   DOMAIN          <1..108
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   REGION          53..54
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   REGION          71..151
FT                   /note="Mediates interaction with EFEMP1"
FT                   /evidence="ECO:0000250"
FT   SITE            2
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   DISULFID        1..108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        115..120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        128..149
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   NON_TER         1
FT   NON_TER         151
SQ   SEQUENCE   151 AA;  17595 MW;  B5BAC65EFF0AC6EC CRC64;
     CNSDIVIRAK VVGKKLVKEG PFGTMVYTVK QMKMYRGFTK MPHVQYIHTE ASESLCGLKL
     EVNKYQYLLT GRVYDGKVYT GLCNFVERWD QLTLSQRKGL NYRYHLGCNC KIKSCYYLPC
     FVTSKNECLW TDMLSNFGYP GYQSKHYACI R