ID   TIMP2_HORSE             Reviewed;          91 AA.
AC   O77717;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Metalloproteinase inhibitor 2;
DE   AltName: Full=Tissue inhibitor of metalloproteinases 2;
DE            Short=TIMP-2;
DE   Flags: Fragment;
GN   Name=TIMP2; Synonyms=TIMP-2;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Articular cartilage;
RX   PubMed=10328846; DOI=10.1053/tvjl.1998.0328;
RA   Clegg P.D., Radford A.D., Carter S.D.;
RT   "Molecular studies of matrix metalloproteinases and tissue inhibitors of
RT   metalloproteinases in equine joints.";
RL   Vet. J. 157:336-338(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF N-TERMINUS.
RX   PubMed=9758100; DOI=10.1111/j.2042-3306.1998.tb04512.x;
RA   Clegg P.D., Coughlan A.R., Carter S.D.;
RT   "Equine TIMP-1 and TIMP-2: identification, activity and cellular sources.";
RL   Equine Vet. J. 30:416-423(1998).
CC   -!- FUNCTION: Complexes with metalloproteinases (such as collagenases) and
CC       irreversibly inactivates them.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: The activity of TIMP2 is dependent on the presence of disulfide
CC       bonds.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC       {ECO:0000305}.
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DR   EMBL; AJ010315; CAA09080.1; -; mRNA.
DR   AlphaFoldDB; O77717; -.
DR   SMR; O77717; -.
DR   STRING; 9796.ENSECAP00000048160; -.
DR   PaxDb; O77717; -.
DR   InParanoid; O77717; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0034097; P:response to cytokine; IBA:GO_Central.
DR   GO; GO:0009725; P:response to hormone; 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   InterPro; IPR015613; TIMP2.
DR   PANTHER; PTHR11844; PTHR11844; 1.
DR   PANTHER; PTHR11844:SF24; PTHR11844:SF24; 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   Direct protein sequencing; Disulfide bond; Metalloenzyme inhibitor;
KW   Metalloprotease inhibitor; Protease inhibitor; Reference proteome;
KW   Secreted.
FT   CHAIN           <1..>91
FT                   /note="Metalloproteinase inhibitor 2"
FT                   /id="PRO_0000220983"
FT   DOMAIN          <1..>91
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   NON_TER         1
FT   NON_TER         91
SQ   SEQUENCE   91 AA;  9998 MW;  94E1C40AA3AB5CFE CRC64;
     KAVSEKEVDS GNDIYGNPIK RIQYEIKQIK MFKGPDKDIE FIYTAPSSAV CGVSLDVGGK
     KEYLIAGKAD GNGKMHITLC DFIVPWDTLS T