ID   TIMP4_RABIT             Reviewed;         170 AA.
AC   O97591;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Metalloproteinase inhibitor 4;
DE   AltName: Full=Tissue inhibitor of metalloproteinases 4;
DE            Short=TIMP-4;
DE   Flags: Fragment;
GN   Name=TIMP4;
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.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC       {ECO:0000305}.
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DR   EMBL; AF069715; AAC95007.1; -; mRNA.
DR   AlphaFoldDB; O97591; -.
DR   SMR; O97591; -.
DR   STRING; 9986.ENSOCUP00000013706; -.
DR   MEROPS; I35.004; -.
DR   PRIDE; O97591; -.
DR   eggNOG; KOG4745; Eukaryota.
DR   InParanoid; O97591; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR015614; TIMP4.
DR   InterPro; IPR027465; TIMP_C.
DR   PANTHER; PTHR11844; PTHR11844; 1.
DR   PANTHER; PTHR11844:SF26; PTHR11844:SF26; 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; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW   Protease inhibitor; Reference proteome; Secreted.
FT   CHAIN           <1..>170
FT                   /note="Metalloproteinase inhibitor 4"
FT                   /id="PRO_0000220987"
FT   DOMAIN          <1..105
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   REGION          6..9
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   REGION          48..49
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   DISULFID        107..154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        112..117
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        125..146
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   NON_TER         1
FT   NON_TER         170
SQ   SEQUENCE   170 AA;  19811 MW;  6D6EEA8D9A363050 CRC64;
     ISSEKVVPAS ADPADTQRMI RYEIKQIKMF KGFEKIKDVQ YIYTPFDSSL CGVKLEANSQ
     KQYLLTGQVL SDGKVFIHLC NYIEPWEDLS LVQRESLNHH YHLNCVCQIT TCYTVPCTIS
     APNECLWTDW LLERKLYGYQ AQHYVCMKHA DGTCSWYQGR LPLRKEFVDI