ID   TIMP3_HORSE             Reviewed;         211 AA.
AC   Q9TUL9;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 128.
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   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].
RA   Kyaw-Tanner M.T., Mungall B.A., Pollitt C.C.;
RT   "Molecular cloning and sequencing of the cDNA encoding equine tissue
RT   inhibitor of metalloproteinase-3 (TIMP-3).";
RL   Submitted (JUN-1999) 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   -!- SUBUNIT: Interacts with EFEMP1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC       {ECO:0000305}.
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DR   EMBL; AJ243283; CAB51854.1; -; mRNA.
DR   RefSeq; NP_001075339.1; NM_001081870.2.
DR   AlphaFoldDB; Q9TUL9; -.
DR   SMR; Q9TUL9; -.
DR   STRING; 9796.ENSECAP00000015840; -.
DR   MEROPS; I35.003; -.
DR   GlyCosmos; Q9TUL9; 1 site, No reported glycans.
DR   PaxDb; 9796-ENSECAP00000015840; -.
DR   Ensembl; ENSECAT00000084385.1; ENSECAP00000075183.1; ENSECAG00000018314.4.
DR   GeneID; 100033947; -.
DR   KEGG; ecb:100033947; -.
DR   CTD; 7078; -.
DR   VGNC; VGNC:24109; TIMP3.
DR   GeneTree; ENSGT00940000159601; -.
DR   HOGENOM; CLU_084029_0_0_1; -.
DR   InParanoid; Q9TUL9; -.
DR   OMA; RGFDKMP; -.
DR   OrthoDB; 5403389at2759; -.
DR   TreeFam; TF317409; -.
DR   Proteomes; UP000002281; Chromosome 28.
DR   Bgee; ENSECAG00000018314; Expressed in articular cartilage of joint and 21 other cell types or tissues.
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:0008270; F:zinc ion binding; ISS:UniProtKB.
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   CDD; cd03585; NTR_TIMP; 1.
DR   Gene3D; 2.40.50.120; -; 1.
DR   Gene3D; 3.90.370.10; Tissue inhibitor of metalloproteinase-1. Chain B, domain 1; 1.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR001820; TIMP.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   InterPro; IPR027465; TIMP_C.
DR   InterPro; IPR030490; TIMP_CS.
DR   PANTHER; PTHR11844; METALLOPROTEASE INHIBITOR; 1.
DR   PANTHER; PTHR11844:SF22; METALLOPROTEINASE INHIBITOR 3; 1.
DR   Pfam; PF00965; TIMP; 1.
DR   SMART; SM00206; NTR; 1.
DR   SUPFAM; SSF50242; TIMP-like; 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   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..211
FT                   /note="Metalloproteinase inhibitor 3"
FT                   /id="PRO_0000034340"
FT   DOMAIN          24..143
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   REGION          24..27
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   REGION          88..89
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   REGION          105..188
FT                   /note="Mediates interaction with EFEMP1"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
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            37
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16035"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        24..91
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        26..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        36..143
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        145..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        150..155
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        163..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
SQ   SEQUENCE   211 AA;  24147 MW;  1E9C5A6D2FC766DF CRC64;
     MTPWLGLVVL LGSWSLGDWG AEACTCSPSH PQDAFCNSDI VIRAKVVGKK LVKEGPFGTL
     VYTIKQMKMY RGFTKMPHVQ YIHTEASESL CGLKLEVNKY QYLLTGRVYD GKMYTGLCNF
     VERWDQLTLS QRKGLNYRYH LGCNCKIKSC YYLPCYVTSK NECLWTDMLS NFGYPGYQSK
     HYACIRQKGG YCSWYRGWAP PDKSIINATD P
//