TIMP4_MOUSE
ID TIMP4_MOUSE Reviewed; 224 AA.
AC Q9JHB3; Q924B7;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Metalloproteinase inhibitor 4;
DE AltName: Full=Tissue inhibitor of metalloproteinases 4;
DE Short=TIMP-4;
DE Flags: Precursor;
GN Name=Timp4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Brain, and Heart;
RX PubMed=9013889; DOI=10.1016/s0014-5793(96)01474-3;
RA Leco K.J., Apte S.S., Taniguchi G.T., Hawkes S.P., Khokha R., Schultz G.A.,
RA Edwards D.R.;
RT "Murine tissue inhibitor of metalloproteinases-4 (Timp-4): cDNA isolation
RT and expression in adult mouse tissues.";
RL FEBS Lett. 401:213-217(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Rahkonen O.P., Koskivirta I.M., Vuorio E.I.;
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- TISSUE SPECIFICITY: Expressed in brain, heart, ovary and skeletal
CC muscle.
CC -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC {ECO:0000305}.
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DR EMBL; AF282730; AAF97239.1; -; mRNA.
DR EMBL; AF345865; AAK62886.1; -; Genomic_DNA.
DR EMBL; AF345864; AAK62886.1; JOINED; Genomic_DNA.
DR EMBL; BC064046; AAH64046.1; -; mRNA.
DR CCDS; CCDS20438.1; -.
DR RefSeq; NP_542370.3; NM_080639.3.
DR AlphaFoldDB; Q9JHB3; -.
DR SMR; Q9JHB3; -.
DR BioGRID; 225738; 1.
DR STRING; 10090.ENSMUSP00000032462; -.
DR MEROPS; I35.004; -.
DR PhosphoSitePlus; Q9JHB3; -.
DR PaxDb; Q9JHB3; -.
DR PRIDE; Q9JHB3; -.
DR ProteomicsDB; 259453; -.
DR Antibodypedia; 3455; 593 antibodies from 36 providers.
DR DNASU; 110595; -.
DR Ensembl; ENSMUST00000032462; ENSMUSP00000032462; ENSMUSG00000030317.
DR GeneID; 110595; -.
DR KEGG; mmu:110595; -.
DR UCSC; uc009dip.1; mouse.
DR CTD; 7079; -.
DR MGI; MGI:109125; Timp4.
DR VEuPathDB; HostDB:ENSMUSG00000030317; -.
DR eggNOG; KOG4745; Eukaryota.
DR GeneTree; ENSGT00940000159798; -.
DR HOGENOM; CLU_084029_0_0_1; -.
DR InParanoid; Q9JHB3; -.
DR OMA; EPWDNLS; -.
DR OrthoDB; 1122531at2759; -.
DR PhylomeDB; Q9JHB3; -.
DR TreeFam; TF317409; -.
DR BioGRID-ORCS; 110595; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Timp4; mouse.
DR PRO; PR:Q9JHB3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JHB3; protein.
DR Bgee; ENSMUSG00000030317; Expressed in prostate gland ventral lobe and 154 other tissues.
DR ExpressionAtlas; Q9JHB3; baseline and differential.
DR Genevisible; Q9JHB3; MM.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0030017; C:sarcomere; ISO:MGI.
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: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:0007219; P:Notch signaling pathway; IDA:MGI.
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; IPR015614; TIMP4.
DR InterPro; IPR027465; TIMP_C.
DR InterPro; IPR030490; TIMP_CS.
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.
DR PROSITE; PS00288; TIMP; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Metal-binding; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Protease inhibitor; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..224
FT /note="Metalloproteinase inhibitor 4"
FT /id="PRO_0000034350"
FT DOMAIN 30..156
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 30..33
FT /note="Involved in metalloproteinase-binding"
FT /evidence="ECO:0000250|UniProtKB:P16035"
FT REGION 99..100
FT /note="Involved in metalloproteinase-binding"
FT /evidence="ECO:0000250|UniProtKB:P16035"
FT BINDING 30
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 69
FT /note="Involved in metalloproteinase-binding"
FT /evidence="ECO:0000250|UniProtKB:P16035"
FT DISULFID 30..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 32..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 42..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 158..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 163..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 176..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT CONFLICT 118..123
FT /note="GQILSD -> ARFSG (in Ref. 2; AAK62886)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..138
FT /note="LCNYIEPWE -> FVPTYIKPWK (in Ref. 2; AAK62886)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="C -> L (in Ref. 2; AAK62886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 25774 MW; D66867C71E0C4AD9 CRC64;
MPWSPLAALS WALVLRLLAL LWPPGRGEAC SCAPAHPQQH FCHSALVIRA KISSEKVVPA
SKDPADTQKL IRYEIKQIKM FKGFEKAKDI QYVYTPFDSS LCGVKLETNS HKQYLLTGQI
LSDGKVFIHL CNYIEPWEDL SLVQRESLNH HYHQNCGCQI TTCYAVPCTI SAPNECLWTD
WLLERKLYGY QAQHYVCMKH VDGICSWYRG HLHLRKEYVD IIQP
