TIMP3_MACMU
ID TIMP3_MACMU Reviewed; 211 AA.
AC Q5PXZ9;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cao W.G., Jia Y.B., Slayden O.D., Mah K., Brenner R.M.;
RT "TIMP3 DNA sequence from Rhesus monkey endometrium.";
RL Submitted (NOV-2004) 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. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9,
CC MMP-13, MMP-14 and MMP-15 (By similarity). {ECO:0000250}.
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; AY821556; AAV70658.1; -; mRNA.
DR RefSeq; NP_001028128.1; NM_001032956.1.
DR AlphaFoldDB; Q5PXZ9; -.
DR SMR; Q5PXZ9; -.
DR STRING; 9544.ENSMMUP00000008861; -.
DR MEROPS; I35.003; -.
DR PRIDE; Q5PXZ9; -.
DR Ensembl; ENSMMUT00000097441; ENSMMUP00000067268; ENSMMUG00000062825.
DR GeneID; 574381; -.
DR KEGG; mcc:574381; -.
DR CTD; 7078; -.
DR VEuPathDB; HostDB:ENSMMUG00000062825; -.
DR VGNC; VGNC:108066; TIMP3.
DR eggNOG; KOG4745; Eukaryota.
DR GeneTree; ENSGT00940000159601; -.
DR HOGENOM; CLU_084029_0_0_1; -.
DR InParanoid; Q5PXZ9; -.
DR OrthoDB; 1122531at2759; -.
DR Proteomes; UP000006718; Chromosome 10.
DR Bgee; ENSMMUG00000062825; Expressed in lung and 21 other tissues.
DR ExpressionAtlas; Q5PXZ9; baseline.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
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:0071310; P:cellular response to organic substance; IEA:Ensembl.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IBA:GO_Central.
DR GO; GO:1904684; P:negative regulation of metalloendopeptidase activity; IEA:Ensembl.
DR GO; GO:1903984; P:positive regulation of TRAIL-activated apoptotic signaling pathway; IEA:Ensembl.
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 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 Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..211
FT /note="Metalloproteinase inhibitor 3"
FT /id="PRO_0000034343"
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; 24145 MW; 15CF831028BABF7A CRC64;
MTPWLGLIVL LGSWSLGDWG AEACTCSPSH PQDAFCNSDI VIRAKVVGKK LVKEGPFGTL
VYTIKQMKMY RGFTKMPHVQ YIHTEASESL CGLKLEVNKY QYLLTGRVYD GKMYTGLCNF
VERWDQLTLS QRKGLNYRYH LGCNCKIKSC YYLPCFVTSK NECLWTDMLS NFGYPGYQSK
HYACIRQKGG YCSWYRGWAP PDKSIINATD P
