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Metalloproteinase inhibitor 1 (Collagenase inhibitor 16C8 fibroblast) (Erythroid-potentiating activity) (EPA) (TPA-S1) (TPA-induced protein) (Tissue inhibitor of metalloproteinases 1) (TIMP-1)

 TIMP1_MOUSE             Reviewed;         205 AA.
P12032; P20064; Q61720;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 2.
23-MAY-2018, entry version 164.
RecName: Full=Metalloproteinase inhibitor 1;
AltName: Full=Collagenase inhibitor 16C8 fibroblast;
AltName: Full=Erythroid-potentiating activity;
Short=EPA;
AltName: Full=TPA-S1;
AltName: Full=TPA-induced protein;
AltName: Full=Tissue inhibitor of metalloproteinases 1;
Short=TIMP-1;
Flags: Precursor;
Name=Timp1; Synonyms=Timp, Timp-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3034603;
Gewert D.R., Coulombe B., Castelino M., Skup D., Williams B.R.G.;
"Characterization and expression of a murine gene homologous to human
EPA/TIMP: a virus-induced gene in the mouse.";
EMBO J. 6:651-657(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=3024122; DOI=10.1093/nar/14.22.8863;
Edwards D.R., Waterhouse P., Holman M.L., Denhardt D.T.;
"A growth-responsive gene (16C8) in normal mouse fibroblasts
homologous to a human collagenase inhibitor with erythroid-
potentiating activity: evidence for inducible and constitutive
transcripts.";
Nucleic Acids Res. 14:8863-8878(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/HeJ;
PubMed=3670294; DOI=10.1128/MCB.7.8.2821;
Johnson M.D., Housey G.M., Kirschmeier P.T., Weinstein I.B.;
"Molecular cloning of gene sequences regulated by tumor promoters and
mitogens through protein kinase C.";
Mol. Cell. Biol. 7:2821-2829(1987).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland, and Osteoblast;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PARTIAL NUCLEOTIDE SEQUENCE, AND DEVELOPMENTAL STAGE.
TISSUE=Embryo;
PubMed=2744464; DOI=10.1101/gad.3.6.848;
Brenner C.A., Adler R.R., Rappolee D.A., Pedersen R.A., Werb Z.;
"Genes for extracellular-matrix-degrading metalloproteinases and their
inhibitor, TIMP, are expressed during early mammalian development.";
Genes Dev. 3:848-859(1989).
[6]
NUCLEOTIDE SEQUENCE OF 168-205.
PubMed=6179042; DOI=10.1093/nar/10.10.3069;
Skup D., Windass J.D., Sor F.S., George H., Williams B.R.,
Fukuhara H., de Maeyer-Guignard J., de Maeyer E.;
"Molecular cloning of partial cDNA copies of two distinct mouse IFN-
beta mRNAs.";
Nucleic Acids Res. 10:3069-3084(1982).
[7]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CD63, AND
IDENTIFICATION IN A COMPLEX WITH CD63 AND ITGB1.
PubMed=23522389; DOI=10.1186/1476-4598-12-22;
Toricelli M., Melo F.H., Peres G.B., Silva D.C., Jasiulionis M.G.;
"Timp1 interacts with beta-1 integrin and CD63 along melanoma genesis
and confers anoikis resistance by activating PI3-K signaling pathway
independently of Akt phosphorylation.";
Mol. Cancer 12:22-22(2013).
-!- FUNCTION: Metalloproteinase inhibitor that functions by forming
one to one complexes with target metalloproteinases, such as
collagenases, and irreversibly inactivates them by binding to
their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7,
MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on
MMP14 (By similarity). Also functions as a growth factor that
regulates cell differentiation, migration and cell death and
activates cellular signaling cascades via CD63 and ITGB1. Plays a
role in integrin signaling. {ECO:0000250,
ECO:0000269|PubMed:23522389}.
-!- SUBUNIT: Interacts with MMP1, MMP3, MMP10 and MMP13, but has only
very low affinity for MMP14 (By similarity). Interacts with CD63;
identified in a complex with CD63 and ITGB1. {ECO:0000250,
ECO:0000269|PubMed:23522389}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23522389}.
-!- TISSUE SPECIFICITY: Found in fetal and adult tissues. Highest
levels are found in bone. Also found in lung, ovary and uterus.
-!- DEVELOPMENTAL STAGE: Present in unfertilized eggs and at the
zygote and cleavage stages. Levels increase at the blastocyst
stage and with endoderm differentiation.
{ECO:0000269|PubMed:2744464}.
-!- INDUCTION: Regulated by tumor promoters and mitogens through
protein kinase C. Also induced by viruses.
-!- PTM: The activity of TIMP1 is dependent on the presence of
disulfide bonds. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M28312; AAB42179.1; -; Genomic_DNA.
EMBL; M28308; AAB42179.1; JOINED; Genomic_DNA.
EMBL; M28309; AAB42179.1; JOINED; Genomic_DNA.
EMBL; M28310; AAB42179.1; JOINED; Genomic_DNA.
EMBL; M28311; AAB42179.1; JOINED; Genomic_DNA.
EMBL; X04684; CAA28387.1; -; mRNA.
EMBL; M17243; AAA40471.1; -; mRNA.
EMBL; BC008107; AAH08107.1; -; mRNA.
EMBL; BC034260; AAH34260.1; -; mRNA.
EMBL; BC051260; AAH51260.1; -; mRNA.
EMBL; V00755; CAA24132.1; -; mRNA.
CCDS; CCDS30046.1; -.
PIR; A26917; A26106.
RefSeq; NP_001037849.1; NM_001044384.1.
RefSeq; NP_035723.2; NM_011593.2.
UniGene; Mm.8245; -.
ProteinModelPortal; P12032; -.
SMR; P12032; -.
STRING; 10090.ENSMUSP00000009530; -.
PhosphoSitePlus; P12032; -.
MaxQB; P12032; -.
PaxDb; P12032; -.
PeptideAtlas; P12032; -.
PRIDE; P12032; -.
Ensembl; ENSMUST00000009530; ENSMUSP00000009530; ENSMUSG00000001131.
Ensembl; ENSMUST00000115342; ENSMUSP00000110999; ENSMUSG00000001131.
GeneID; 21857; -.
KEGG; mmu:21857; -.
UCSC; uc009sty.1; mouse.
CTD; 7076; -.
MGI; MGI:98752; Timp1.
eggNOG; KOG4745; Eukaryota.
eggNOG; ENOG41103NU; LUCA.
GeneTree; ENSGT00390000004555; -.
HOGENOM; HOG000285981; -.
HOVERGEN; HBG068749; -.
InParanoid; P12032; -.
KO; K16451; -.
OMA; WRRTQLY; -.
OrthoDB; EOG091G0NIC; -.
PhylomeDB; P12032; -.
TreeFam; TF317409; -.
Reactome; R-MMU-114608; Platelet degranulation.
Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
PRO; PR:P12032; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000001131; -.
CleanEx; MM_TIMP1; -.
Genevisible; P12032; MM.
GO; GO:0005604; C:basement membrane; IDA:MGI.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0005125; F:cytokine activity; ISS:UniProtKB.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISS:UniProtKB.
GO; GO:0002020; F:protease binding; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0010951; P:negative regulation of endopeptidase activity; ISS:UniProtKB.
GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; ISO:MGI.
GO; GO:1905049; P:negative regulation of metallopeptidase activity; ISO:MGI.
GO; GO:1901164; P:negative regulation of trophoblast cell migration; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:2001044; P:regulation of integrin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
GO; GO:0009725; P:response to hormone; IBA:GO_Central.
Gene3D; 3.90.370.10; -; 1.
InterPro; IPR001134; Netrin_domain.
InterPro; IPR001820; TIMP.
InterPro; IPR008993; TIMP-like_OB-fold.
InterPro; IPR015611; TIMP1.
InterPro; IPR027465; TIMP_C.
InterPro; IPR030490; TIMP_CS.
PANTHER; PTHR11844; PTHR11844; 1.
PANTHER; PTHR11844:SF20; PTHR11844:SF20; 1.
Pfam; PF00965; TIMP; 1.
SMART; SM00206; NTR; 1.
SUPFAM; SSF50242; SSF50242; 1.
PROSITE; PS50189; NTR; 1.
PROSITE; PS00288; TIMP; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Growth factor;
Metal-binding; Metalloenzyme inhibitor; Metalloprotease inhibitor;
Phosphoprotein; Protease inhibitor; Reference proteome; Secreted;
Signal; Zinc.
SIGNAL 1 24
CHAIN 25 205 Metalloproteinase inhibitor 1.
/FTId=PRO_0000034325.
DOMAIN 25 148 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
REGION 25 28 Involved in metalloproteinase-binding.
{ECO:0000250|UniProtKB:P16035}.
REGION 91 92 Involved in metalloproteinase-binding.
{ECO:0000250|UniProtKB:P16035}.
METAL 25 25 Zinc; via amino nitrogen and carbonyl
oxygen; shared with metalloproteinase
partner. {ECO:0000250|UniProtKB:P16035}.
SITE 38 38 Involved in metalloproteinase-binding.
{ECO:0000250|UniProtKB:P16035}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000250|UniProtKB:P01033}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 25 94 {ECO:0000255|PROSITE-ProRule:PRU00295}.
DISULFID 27 123 {ECO:0000255|PROSITE-ProRule:PRU00295}.
DISULFID 37 148 {ECO:0000255|PROSITE-ProRule:PRU00295}.
DISULFID 151 197 {ECO:0000255|PROSITE-ProRule:PRU00295}.
DISULFID 156 161 {ECO:0000255|PROSITE-ProRule:PRU00295}.
DISULFID 169 189 {ECO:0000255|PROSITE-ProRule:PRU00295}.
CONFLICT 52 52 E -> R (in Ref. 1; AAB42179).
{ECO:0000305}.
CONFLICT 66 66 M -> MM (in Ref. 1; AAB42179).
{ECO:0000305}.
CONFLICT 117 118 NL -> KF (in Ref. 1; AAB42179).
{ECO:0000305}.
CONFLICT 121 121 S -> N (in Ref. 1; AAB42179).
{ECO:0000305}.
CONFLICT 139 139 A -> V (in Ref. 1). {ECO:0000305}.
CONFLICT 143 143 T -> KN (in Ref. 1). {ECO:0000305}.
CONFLICT 194 194 P -> L (in Ref. 1 and 6). {ECO:0000305}.
SEQUENCE 205 AA; 22628 MW; FACA952D49A50FD7 CRC64;
MMAPFASLAS GILLLLSLIA SSKACSCAPP HPQTAFCNSD LVIRAKFMGS PEINETTLYQ
RYKIKMTKML KGFKAVGNAA DIRYAYTPVM ESLCGYAHKS QNRSEEFLIT GRLRNGNLHI
SACSFLVPWR TLSPAQQRAF SKTYSAGCGV CTVFPCLSIP CKLESDTHCL WTDQVLVGSE
DYQSRHFACL PRNPGLCTWR SLGAR


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