TIMP3_MACFA
ID TIMP3_MACFA Reviewed; 211 AA.
AC P61269;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Umeda S., Suzuki M.T., Yoshikawa Y., Tanaka Y., Iwata T.;
RT "Molecular cloning of TIMP3 gene from Cynomolgus monkey (Macaca
RT fascicularis).";
RL Submitted (DEC-2002) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY207384; AAO65587.1; -; Genomic_DNA.
DR EMBL; AY207381; AAO65587.1; JOINED; Genomic_DNA.
DR EMBL; AY207382; AAO65587.1; JOINED; Genomic_DNA.
DR EMBL; AY207383; AAO65587.1; JOINED; Genomic_DNA.
DR EMBL; AY207385; AAO65588.1; -; mRNA.
DR RefSeq; NP_001274235.1; NM_001287306.1.
DR AlphaFoldDB; P61269; -.
DR SMR; P61269; -.
DR STRING; 9541.XP_005567536.1; -.
DR MEROPS; I35.003; -.
DR Ensembl; ENSMFAT00000088501; ENSMFAP00000052902; ENSMFAG00000061913.
DR GeneID; 102141270; -.
DR CTD; 7078; -.
DR VEuPathDB; HostDB:ENSMFAG00000030203; -.
DR eggNOG; KOG4745; Eukaryota.
DR GeneTree; ENSGT00940000159601; -.
DR OMA; QVQYIYT; -.
DR OrthoDB; 1122531at2759; -.
DR Proteomes; UP000233100; Chromosome 10.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
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:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
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 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_0000034342"
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
