ID TIMP4_BOVIN Reviewed; 224 AA.
AC O97563; Q2KHW6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 08-NOV-2023, entry version 123.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 71-177.
RC TISSUE=Adrenal cortex;
RA Hosseini G.H., Pepper M.S.;
RL Submitted (DEC-1997) 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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC {ECO:0000305}.
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DR EMBL; BC112857; AAI12858.1; -; mRNA.
DR EMBL; AF037273; AAD02097.1; -; mRNA.
DR RefSeq; NP_001039336.1; NM_001045871.2.
DR AlphaFoldDB; O97563; -.
DR SMR; O97563; -.
DR STRING; 9913.ENSBTAP00000026999; -.
DR MEROPS; I35.004; -.
DR PaxDb; 9913-ENSBTAP00000026999; -.
DR GeneID; 317694; -.
DR KEGG; bta:317694; -.
DR CTD; 7079; -.
DR eggNOG; KOG4745; Eukaryota.
DR InParanoid; O97563; -.
DR OrthoDB; 5403389at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; 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 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:SF26; METALLOPROTEINASE INHIBITOR 4; 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; 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_0000220986"
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 113
FT /note="R -> Q (in Ref. 2; AAD02097)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="H -> R (in Ref. 2; AAD02097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 25593 MW; 49BB075ABCB82CF3 CRC64;
MPQSPRPVPS WALLLRLLAL LRPPGLGEAC SCAPAHPQQH VCHSALAIRA KISSEKVVPA
STDPADPQKM IRYEIKQIKM FKGFEKVNDI QYIYTPFDSS LCGVKLEANS QKRYLLTGQI
LSDGKVFVHL CNYIEPWENL SFLQRESLNH HYHLNCGCQI TTCYAVPCTI SAPNECLWTD
WLLERKLYGY QAQHYVCMKH VDGSCSWYQG RLPLRKEFVD IIQP
//
