TIMP3_CHICK
ID TIMP3_CHICK Reviewed; 212 AA.
AC P26652;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Metalloproteinase inhibitor 3;
DE AltName: Full=21 kDa protein of extracellular matrix;
DE AltName: Full=Tissue inhibitor of metalloproteinases 3;
DE Short=TIMP-3;
DE Flags: Precursor;
GN Name=TIMP3; Synonyms=IMP-3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic fibroblast;
RX PubMed=1512267; DOI=10.1016/s0021-9258(18)41928-x;
RA Pavloff N., Staskus P.W., Kishanani N.S., Hawkes S.P.;
RT "A new inhibitor of metalloproteinases from chicken: ChIMP-3. A third
RT member of the TIMP family.";
RL J. Biol. Chem. 267:17321-17326(1992).
RN [2]
RP PROTEIN SEQUENCE OF 25-53.
RC TISSUE=Fibroblast;
RX PubMed=1845973; DOI=10.1016/s0021-9258(18)52455-8;
RA Staskus P.W., Masiarz F.R., Pallanck L.J., Hawkes S.P.;
RT "The 21-kDa protein is a transformation-sensitive metalloproteinase
RT inhibitor of chicken fibroblasts.";
RL J. Biol. Chem. 266:449-454(1991).
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC {ECO:0000305}.
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DR EMBL; M94531; AAA48813.1; -; mRNA.
DR PIR; A43429; A43429.
DR RefSeq; NP_990818.1; NM_205487.2.
DR AlphaFoldDB; P26652; -.
DR SMR; P26652; -.
DR STRING; 9031.ENSGALP00000040866; -.
DR MEROPS; I35.003; -.
DR PaxDb; P26652; -.
DR PRIDE; P26652; -.
DR Ensembl; ENSGALT00000046125; ENSGALP00000040866; ENSGALG00000028627.
DR GeneID; 396483; -.
DR KEGG; gga:396483; -.
DR CTD; 7078; -.
DR VEuPathDB; HostDB:geneid_396483; -.
DR eggNOG; KOG4745; Eukaryota.
DR GeneTree; ENSGT00940000159601; -.
DR HOGENOM; CLU_084029_0_0_1; -.
DR InParanoid; P26652; -.
DR OMA; QVQYIYT; -.
DR OrthoDB; 1122531at2759; -.
DR PhylomeDB; P26652; -.
DR TreeFam; TF317409; -.
DR Reactome; R-GGA-114608; Platelet degranulation.
DR PRO; PR:P26652; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000028627; Expressed in lung and 13 other tissues.
DR ExpressionAtlas; P26652; baseline and differential.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Metal-binding; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW Protease inhibitor; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:1845973"
FT CHAIN 25..212
FT /note="Metalloproteinase inhibitor 3"
FT /id="PRO_0000034346"
FT DOMAIN 25..144
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 25..28
FT /note="Involved in metalloproteinase-binding"
FT /evidence="ECO:0000250|UniProtKB:P16035"
FT REGION 89..90
FT /note="Involved in metalloproteinase-binding"
FT /evidence="ECO:0000250|UniProtKB:P16035"
FT BINDING 25
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 38
FT /note="Involved in metalloproteinase-binding"
FT /evidence="ECO:0000250|UniProtKB:P16035"
FT DISULFID 25..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 27..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 37..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 146..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 151..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 164..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
SQ SEQUENCE 212 AA; 24505 MW; 17F159ADE108D618 CRC64;
MTAWLGFLAV FLCSWSLRDL VAEACTCVPI HPQDAFCNSD IVIRAKVVGK KLMKDGPFGT
MRYTVKQMKM YRGFQIMPHV QYIYTEASES LCGVKLEVNK YQYLITGRVY EGKVYTGLCN
WYEKWDRLTL SQRKGLNHRY HLGCGCKIRP CYYLPCFATS KNECIWTDML SNFGHSGHQA
KHYACIQRVE GYCSWYRGWA PPDKTIINAT DP
