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Metalloproteinase inhibitor 1 (Erythroid-potentiating activity) (EPA) (Fibroblast collagenase inhibitor) (Collagenase inhibitor) (Tissue inhibitor of metalloproteinases 1) (TIMP-1)

 TIMP1_HUMAN             Reviewed;         207 AA.
P01033; Q14252; Q9UCU1;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
20-JUN-2018, entry version 203.
RecName: Full=Metalloproteinase inhibitor 1;
AltName: Full=Erythroid-potentiating activity;
Short=EPA;
AltName: Full=Fibroblast collagenase inhibitor;
Short=Collagenase inhibitor;
AltName: Full=Tissue inhibitor of metalloproteinases 1;
Short=TIMP-1;
Flags: Precursor;
Name=TIMP1; Synonyms=CLGI, TIMP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-51, FUNCTION,
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=3903517; DOI=10.1038/318066a0;
Docherty A.J.P., Lyons A., Smith B.J., Wright E.M., Stephens P.E.,
Harris T.J.R., Murphy G., Reynolds J.J.;
"Sequence of human tissue inhibitor of metalloproteinases and its
identity to erythroid-potentiating activity.";
Nature 318:66-69(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-49, SUBCELLULAR
LOCATION, GLYCOSYLATION, AND FUNCTION.
PubMed=3839290; DOI=10.1038/315768a0;
Gasson J.C., Golde D.W., Kaufman S.E., Westbrook C.A., Hewick R.M.,
Kaufman R.J., Wong G.G., Temple P.A., Leary A.C., Brown E.L.,
Orr E.C., Clark S.C.;
"Molecular characterization and expression of the gene encoding human
erythroid-potentiating activity.";
Nature 315:768-771(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-207, DISULFIDE
BOND, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=3010309; DOI=10.1073/pnas.83.8.2407;
Carmichael D.F., Sommer A., Thompson R.C., Anderson D.C., Smith C.G.,
Welgus H.G., Stricklin G.P.;
"Primary structure and cDNA cloning of human fibroblast collagenase
inhibitor.";
Proc. Natl. Acad. Sci. U.S.A. 83:2407-2411(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Kaczorek M., Honore N., Ribes V., Dehoux P., Cornet P., Cartwright T.,
Streeck R.E.;
"Molecular cloning and synthesis of biologically active human tissue
inhibitor of metalloproteinases in yeast.";
Biotechnology (N.Y.) 5:595-598(1987).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=2171551; DOI=10.1089/dna.1990.9.479;
Rapp G., Freudenstein J., Klaudiny J., Mucha J., Wempe F., Zimmer M.,
Scheit K.H.;
"Characterization of three abundant mRNAs from human ovarian granulosa
cells.";
DNA Cell Biol. 9:479-485(1990).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7507419; DOI=10.3109/02713689309020394;
Opbroek A., Kenney M.C., Brown D.;
"Characterization of a human corneal metalloproteinase inhibitor
(TIMP-1).";
Curr. Eye Res. 12:877-883(1993).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix;
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
PubMed=9286280;
Hardcastle A.J., Thiselton D.L., Nayudu M., Hampson R.M.,
Bhattacharya S.S.;
"Genomic organization of the human TIMP-1 gene. Investigation of a
causative role in the pathogenesis of X-linked retinitis pigmentosa
2.";
Invest. Ophthalmol. Vis. Sci. 38:1893-1896(1997).
[9]
PROTEIN SEQUENCE OF 24-38, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND FUNCTION.
TISSUE=Synovial fluid;
PubMed=1730286; DOI=10.1016/0014-5793(92)80393-U;
Osthues A., Knaueper V., Oberhoff R., Reinke H., Tschesche H.;
"Isolation and characterization of tissue inhibitors of
metalloproteinases (TIMP-1 and TIMP-2) from human rheumatoid synovial
fluid.";
FEBS Lett. 296:16-20(1992).
[10]
PROTEIN SEQUENCE OF 24-52.
PubMed=1653055; DOI=10.1016/1043-4666(91)90021-5;
van Ranst M., Norga K., Masure S., Proost P., Vandekerckhove F.,
Auwerx J., van Damme J., Opdenakker G.;
"The cytokine-protease connection: identification of a 96-kD THP-1
gelatinase and regulation by interleukin-1 and cytokine inducers.";
Cytokine 3:231-239(1991).
[11]
PROTEIN SEQUENCE OF 24-38.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-207.
Matsuda T., Kohno K., Kuwano M.;
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
[13]
DISULFIDE BONDS, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2163605; DOI=10.1042/bj2680267;
Williamson R.A., Martson F.A.O., Angal S., Koklitis P., Panico M.,
Morris H.R., Carne A.F., Smith B.J., Harris T.J.R., Freedman R.B.;
"Disulphide bond assignment in human tissue inhibitor of
metalloproteinases (TIMP).";
Biochem. J. 268:267-274(1990).
[14]
MUTAGENESIS, AND FUNCTION.
PubMed=1420137; DOI=10.1021/bi00157a002;
O'Shea M., Willenbrock F., Williamson R.A., Cockett M.I.,
Freedman R.B., Reynolds J.J., Docherty A.J.P., Murphy G.;
"Site-directed mutations that alter the inhibitory activity of the
tissue inhibitor of metalloproteinases-1: importance of the N-terminal
region between cysteine 3 and cysteine 13.";
Biochemistry 31:10146-10152(1992).
[15]
FUNCTION AS A GROWTH FACTOR AND PROTEASE INHIBITOR, INTERACTION WITH
MMP3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-30 AND GLN-32.
PubMed=8541540;
Chesler L., Golde D.W., Bersch N., Johnson M.D.;
"Metalloproteinase inhibition and erythroid potentiation are
independent activities of tissue inhibitor of metalloproteinases-1.";
Blood 86:4506-4515(1995).
[16]
INTERACTION WITH MMP13, AND FUNCTION.
PubMed=8576151; DOI=10.1074/jbc.271.3.1544;
Knaeuper V., Lopez-Otin C., Smith B., Knight G., Murphy G.;
"Biochemical characterization of human collagenase-3.";
J. Biol. Chem. 271:1544-1550(1996).
[17]
INTERACTION WITH MMP13, AND FUNCTION.
PubMed=9065415; DOI=10.1074/jbc.272.12.7608;
Knaeuper V., Cowell S., Smith B., Lopez-Otin C., O'Shea M., Morris H.,
Zardi L., Murphy G.;
"The role of the C-terminal domain of human collagenase-3 (MMP-13) in
the activation of procollagenase-3, substrate specificity, and tissue
inhibitor of metalloproteinase interaction.";
J. Biol. Chem. 272:7608-7616(1997).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[19]
FUNCTION, AND INTERACTION WITH CD63.
PubMed=16917503; DOI=10.1038/sj.emboj.7601281;
Jung K.K., Liu X.W., Chirco R., Fridman R., Kim H.R.;
"Identification of CD63 as a tissue inhibitor of metalloproteinase-1
interacting cell surface protein.";
EMBO J. 25:3934-3942(2006).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53 AND ASN-101.
TISSUE=Saliva;
PubMed=16740002; DOI=10.1021/pr050492k;
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
Loo J.A.;
"Identification of N-linked glycoproteins in human saliva by
glycoprotein capture and mass spectrometry.";
J. Proteome Res. 5:1493-1503(2006).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[22]
GLYCOSYLATION AT ASN-53.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[25]
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).
[26]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24635319; DOI=10.1042/BJ20131119;
Lee S.Y., Kim J.M., Cho S.Y., Kim H.S., Shin H.S., Jeon J.Y.,
Kausar R., Jeong S.Y., Lee Y.S., Lee M.A.;
"TIMP-1 modulates chemotaxis of human neural stem cells through CD63
and integrin signalling.";
Biochem. J. 459:565-576(2014).
[27]
REVIEW.
PubMed=23982756; DOI=10.1007/s00018-013-1457-3;
Ries C.;
"Cytokine functions of TIMP-1.";
Cell. Mol. Life Sci. 71:659-672(2014).
[28]
PHOSPHORYLATION AT SER-178.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[29]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 24-207 IN COMPLEX WITH MMP3,
AND INTERACTION WITH MMP3.
PubMed=9288970; DOI=10.1038/37995;
Gomis-Rueth F.-X., Maskos K., Betz M., Bergner A., Huber R.,
Suzuki K., Yoshida N., Nagase H., Brew K., Bourenkov G.P.,
Bartunik H., Bode W.;
"Mechanism of inhibition of the human matrix metalloproteinase
stromelysin-1 by TIMP-1.";
Nature 389:77-81(1997).
[30]
STRUCTURE BY NMR OF 24-149, AND DISULFIDE BOND.
PubMed=10623524; DOI=10.1006/jmbi.1999.3362;
Wu B., Arumugam S., Gao G., Lee G.I., Semenchenko V., Huang W.,
Brew K., Van Doren S.R.;
"NMR structure of tissue inhibitor of metalloproteinases-1 implicates
localized induced fit in recognition of matrix metalloproteinases.";
J. Mol. Biol. 295:257-268(2000).
[31]
STRUCTURE BY NMR OF 24-149 IN COMPLEX WITH MMP3, AND INTERACTION WITH
MMP3.
PubMed=12834347; DOI=10.1021/bi034545s;
Arumugam S., Van Doren S.R.;
"Global orientation of bound MMP-3 and N-TIMP-1 in solution via
residual dipolar couplings.";
Biochemistry 42:7950-7958(2003).
[32]
X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 24-149 IN COMPLEX WITH MMP1,
FUNCTION, INTERACTION WITH MMP1 AND MMP3, DISULFIDE BOND, AND
MUTAGENESIS OF THR-25.
PubMed=17050530; DOI=10.1074/jbc.M607625200;
Iyer S., Wei S., Brew K., Acharya K.R.;
"Crystal structure of the catalytic domain of matrix
metalloproteinase-1 in complex with the inhibitory domain of tissue
inhibitor of metalloproteinase-1.";
J. Biol. Chem. 282:364-371(2007).
[33]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 24-148 OF MUTANT LEU-121 IN
COMPLEX WITH MMP14, FUNCTION, INTERACTION WITH MMP14, DISULFIDE BOND,
AND MUTAGENESIS OF THR-121.
PubMed=20545310; DOI=10.1021/bi902141x;
Grossman M., Tworowski D., Dym O., Lee M.H., Levy Y., Murphy G.,
Sagi I.;
"The intrinsic protein flexibility of endogenous protease inhibitor
TIMP-1 controls its binding interface and affects its function.";
Biochemistry 49:6184-6192(2010).
[34]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 24-207 IN COMPLEX WITH
MMP10, FUNCTION, INTERACTION WITH MMP10, AND DISULFIDE BOND.
PubMed=22427646; DOI=10.1074/jbc.M112.341156;
Batra J., Robinson J., Soares A.S., Fields A.P., Radisky D.C.,
Radisky E.S.;
"Matrix metalloproteinase-10 (MMP10) interaction with tissue
inhibitors of metalloproteinases TIMP-1 and TIMP-2: binding studies
and crystal structure.";
J. Biol. Chem. 287:15935-15946(2012).
-!- 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. 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. Mediates erythropoiesis in vitro; but, unlike IL3, it
is species-specific, stimulating the growth and differentiation of
only human and murine erythroid progenitors.
{ECO:0000269|PubMed:1420137, ECO:0000269|PubMed:16917503,
ECO:0000269|PubMed:17050530, ECO:0000269|PubMed:1730286,
ECO:0000269|PubMed:20545310, ECO:0000269|PubMed:22427646,
ECO:0000269|PubMed:24635319, ECO:0000269|PubMed:3839290,
ECO:0000269|PubMed:3903517, ECO:0000269|PubMed:8541540,
ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:9065415}.
-!- SUBUNIT: Interacts with MMP1, MMP3, MMP10 and MMP13, but has only
very low affinity for MMP14. Interacts with CD63; identified in a
complex with CD63 and ITGB1. {ECO:0000269|PubMed:12834347,
ECO:0000269|PubMed:16917503, ECO:0000269|PubMed:17050530,
ECO:0000269|PubMed:20545310, ECO:0000269|PubMed:22427646,
ECO:0000269|PubMed:23522389, ECO:0000269|PubMed:8541540,
ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:9065415,
ECO:0000269|PubMed:9288970}.
-!- INTERACTION:
P08962:CD63; NbExp=5; IntAct=EBI-712536, EBI-762053;
P20908:COL5A1; NbExp=2; IntAct=EBI-712536, EBI-2464511;
P14780:MMP9; NbExp=2; IntAct=EBI-712536, EBI-1382326;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1730286,
ECO:0000269|PubMed:24635319, ECO:0000269|PubMed:3010309,
ECO:0000269|PubMed:3839290, ECO:0000269|PubMed:3903517,
ECO:0000269|PubMed:8541540}.
-!- TISSUE SPECIFICITY: Detected in rheumatoid synovial fluid (at
protein level). {ECO:0000269|PubMed:1730286}.
-!- PTM: The activity of TIMP1 is dependent on the presence of
disulfide bonds. {ECO:0000269|PubMed:10623524,
ECO:0000269|PubMed:20545310, ECO:0000269|PubMed:2163605,
ECO:0000269|PubMed:22427646, ECO:0000269|PubMed:3010309}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:3010309,
ECO:0000269|PubMed:3839290, ECO:0000269|PubMed:3903517}.
-!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
{ECO:0000305}.
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EMBL; X03124; CAA26902.1; -; mRNA.
EMBL; X02598; CAA26443.1; -; mRNA.
EMBL; M12670; AAA52436.1; -; mRNA.
EMBL; M59906; AAA63234.1; -; mRNA.
EMBL; S68252; AAD14009.1; -; mRNA.
EMBL; BC000866; AAH00866.1; -; mRNA.
EMBL; L47361; AAA75558.1; -; Genomic_DNA.
EMBL; D11139; BAA01913.1; -; Genomic_DNA.
CCDS; CCDS14281.1; -.
PIR; A93372; ZYHUEP.
RefSeq; NP_003245.1; NM_003254.2.
UniGene; Hs.522632; -.
PDB; 1D2B; NMR; -; A=24-149.
PDB; 1LQN; Model; -; A=1-207.
PDB; 1OO9; NMR; -; B=24-149.
PDB; 1UEA; X-ray; 2.80 A; B/D=24-207.
PDB; 2J0T; X-ray; 2.54 A; D/E/F=24-149.
PDB; 3MA2; X-ray; 2.05 A; B/C=24-148.
PDB; 3V96; X-ray; 1.90 A; A=24-207.
PDBsum; 1D2B; -.
PDBsum; 1LQN; -.
PDBsum; 1OO9; -.
PDBsum; 1UEA; -.
PDBsum; 2J0T; -.
PDBsum; 3MA2; -.
PDBsum; 3V96; -.
ProteinModelPortal; P01033; -.
SMR; P01033; -.
BioGrid; 112932; 14.
CORUM; P01033; -.
DIP; DIP-1107N; -.
IntAct; P01033; 7.
MINT; P01033; -.
STRING; 9606.ENSP00000218388; -.
MEROPS; I35.001; -.
GlyConnect; 367; -.
iPTMnet; P01033; -.
PhosphoSitePlus; P01033; -.
SwissPalm; P01033; -.
UniCarbKB; P01033; -.
BioMuta; TIMP1; -.
DMDM; 135850; -.
EPD; P01033; -.
PaxDb; P01033; -.
PeptideAtlas; P01033; -.
PRIDE; P01033; -.
ProteomicsDB; 51310; -.
DNASU; 7076; -.
Ensembl; ENST00000218388; ENSP00000218388; ENSG00000102265.
GeneID; 7076; -.
KEGG; hsa:7076; -.
CTD; 7076; -.
DisGeNET; 7076; -.
EuPathDB; HostDB:ENSG00000102265.11; -.
GeneCards; TIMP1; -.
HGNC; HGNC:11820; TIMP1.
HPA; CAB022360; -.
HPA; HPA053417; -.
MIM; 305370; gene.
neXtProt; NX_P01033; -.
OpenTargets; ENSG00000102265; -.
PharmGKB; PA36526; -.
eggNOG; KOG4745; Eukaryota.
eggNOG; ENOG41103NU; LUCA.
GeneTree; ENSGT00390000004555; -.
HOGENOM; HOG000285981; -.
HOVERGEN; HBG068749; -.
InParanoid; P01033; -.
KO; K16451; -.
OMA; WRRTQLY; -.
OrthoDB; EOG091G0NIC; -.
PhylomeDB; P01033; -.
TreeFam; TF317409; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; P01033; -.
EvolutionaryTrace; P01033; -.
GeneWiki; TIMP1; -.
GenomeRNAi; 7076; -.
PMAP-CutDB; P01033; -.
PRO; PR:P01033; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102265; -.
CleanEx; HS_TIMP1; -.
ExpressionAtlas; P01033; baseline and differential.
Genevisible; P01033; HS.
GO; GO:0005604; C:basement membrane; IEA:Ensembl.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0005125; F:cytokine activity; IDA:UniProtKB.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0030414; F:peptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0051216; P:cartilage development; IEA:Ensembl.
GO; GO:0001775; P:cell activation; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0002248; P:connective tissue replacement involved in inflammatory response wound healing; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IDA:UniProtKB.
GO; GO:1905049; P:negative regulation of metallopeptidase activity; IDA:UniProtKB.
GO; GO:1901164; P:negative regulation of trophoblast cell migration; IMP:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:2001044; P:regulation of integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
GO; GO:0009725; P:response to hormone; IBA:GO_Central.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
Gene3D; 3.90.370.10; -; 2.
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;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Growth factor; Metal-binding;
Metalloenzyme inhibitor; Metalloprotease inhibitor; Phosphoprotein;
Protease inhibitor; Reference proteome; Secreted; Signal; Zinc.
SIGNAL 1 23 {ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:1653055,
ECO:0000269|PubMed:1730286,
ECO:0000269|PubMed:3010309,
ECO:0000269|PubMed:3839290,
ECO:0000269|PubMed:3903517}.
CHAIN 24 207 Metalloproteinase inhibitor 1.
/FTId=PRO_0000034323.
DOMAIN 24 147 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
REGION 24 27 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:3V96,
ECO:0000269|PubMed:22427646}.
REGION 90 91 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:3V96,
ECO:0000269|PubMed:22427646}.
REGION 179 180 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:3V96,
ECO:0000269|PubMed:22427646}.
METAL 24 24 Zinc; via amino nitrogen and carbonyl
oxygen; shared with metalloproteinase
partner. {ECO:0000269|PubMed:22427646}.
SITE 57 57 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:3V96,
ECO:0000269|PubMed:22427646}.
SITE 158 158 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:3V96,
ECO:0000269|PubMed:22427646}.
MOD_RES 178 178 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
CARBOHYD 53 53 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:19139490}.
/FTId=CAR_000002.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16740002}.
/FTId=CAR_000003.
DISULFID 24 93 {ECO:0000255|PROSITE-ProRule:PRU00295,
ECO:0000269|PubMed:2163605}.
DISULFID 26 122 {ECO:0000269|PubMed:10623524,
ECO:0000269|PubMed:20545310,
ECO:0000269|PubMed:2163605,
ECO:0000269|PubMed:22427646,
ECO:0000269|PubMed:3010309}.
DISULFID 36 147 {ECO:0000269|PubMed:10623524,
ECO:0000269|PubMed:20545310,
ECO:0000269|PubMed:2163605,
ECO:0000269|PubMed:22427646,
ECO:0000269|PubMed:3010309}.
DISULFID 150 197 {ECO:0000269|PubMed:10623524,
ECO:0000269|PubMed:20545310,
ECO:0000269|PubMed:2163605,
ECO:0000269|PubMed:22427646,
ECO:0000269|PubMed:3010309}.
DISULFID 155 160 {ECO:0000269|PubMed:10623524,
ECO:0000269|PubMed:20545310,
ECO:0000269|PubMed:2163605,
ECO:0000269|PubMed:22427646,
ECO:0000269|PubMed:3010309}.
DISULFID 168 189 {ECO:0000269|PubMed:10623524,
ECO:0000269|PubMed:20545310,
ECO:0000269|PubMed:2163605,
ECO:0000269|PubMed:22427646,
ECO:0000269|PubMed:3010309}.
MUTAGEN 25 25 T->E,G,K,Q,R: Reduced interaction with
metalloproteinase.
{ECO:0000269|PubMed:17050530}.
MUTAGEN 25 25 T->V: Normal interaction with
metalloproteinase.
{ECO:0000269|PubMed:17050530}.
MUTAGEN 30 30 H->A: Nearly abolishes metalloproteinase
inhibition. {ECO:0000269|PubMed:8541540}.
MUTAGEN 32 32 Q->A: Nearly abolishes metalloproteinase
inhibition. {ECO:0000269|PubMed:8541540}.
MUTAGEN 121 121 T->L: Decreases protein flexibility and
increases affinity for MMP14.
{ECO:0000269|PubMed:20545310}.
CONFLICT 23 23 A -> P (in Ref. 2; CAA26443).
{ECO:0000305}.
CONFLICT 44 44 A -> P (in Ref. 12; BAA01913).
{ECO:0000305}.
HELIX 31 37 {ECO:0000244|PDB:3V96}.
STRAND 39 46 {ECO:0000244|PDB:3V96}.
STRAND 57 70 {ECO:0000244|PDB:3V96}.
HELIX 72 74 {ECO:0000244|PDB:1D2B}.
TURN 77 79 {ECO:0000244|PDB:1UEA}.
STRAND 83 89 {ECO:0000244|PDB:3V96}.
HELIX 90 92 {ECO:0000244|PDB:3V96}.
STRAND 105 113 {ECO:0000244|PDB:3V96}.
STRAND 116 118 {ECO:0000244|PDB:3V96}.
STRAND 125 127 {ECO:0000244|PDB:3V96}.
HELIX 128 130 {ECO:0000244|PDB:3V96}.
HELIX 133 140 {ECO:0000244|PDB:3V96}.
HELIX 143 145 {ECO:0000244|PDB:3V96}.
TURN 146 149 {ECO:0000244|PDB:3V96}.
STRAND 151 154 {ECO:0000244|PDB:3V96}.
STRAND 157 159 {ECO:0000244|PDB:3V96}.
STRAND 167 170 {ECO:0000244|PDB:3V96}.
HELIX 172 176 {ECO:0000244|PDB:3V96}.
STRAND 177 181 {ECO:0000244|PDB:3V96}.
HELIX 182 186 {ECO:0000244|PDB:3V96}.
STRAND 188 193 {ECO:0000244|PDB:3V96}.
STRAND 196 200 {ECO:0000244|PDB:3V96}.
SEQUENCE 207 AA; 23171 MW; 5AE4F90FFAB2ECDC CRC64;
MAPFEPLASG ILLLLWLIAP SRACTCVPPH PQTAFCNSDL VIRAKFVGTP EVNQTTLYQR
YEIKMTKMYK GFQALGDAAD IRFVYTPAME SVCGYFHRSH NRSEEFLIAG KLQDGLLHIT
TCSFVAPWNS LSLAQRRGFT KTYTVGCEEC TVFPCLSIPC KLQSGTHCLW TDQLLQGSEK
GFQSRHLACL PREPGLCTWQ SLRSQIA


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