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Metalloproteinase inhibitor 2 (CSC-21K) (Tissue inhibitor of metalloproteinases 2) (TIMP-2)

 TIMP2_HUMAN             Reviewed;         220 AA.
P16035; Q16121; Q93006; Q9UDF7;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 2.
23-MAY-2018, entry version 188.
RecName: Full=Metalloproteinase inhibitor 2;
AltName: Full=CSC-21K;
AltName: Full=Tissue inhibitor of metalloproteinases 2;
Short=TIMP-2;
Flags: Precursor;
Name=TIMP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
PubMed=2380196;
Stetler-Stevenson W.G., Brown P.D., Onisto M., Levy A.T., Liotta L.A.;
"Tissue inhibitor of metalloproteinases-2 (TIMP-2) mRNA expression in
tumor cell lines and human tumor tissues.";
J. Biol. Chem. 265:13933-13938(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2157214; DOI=10.1073/pnas.87.7.2800;
Boone T.C., Johnson M.J., de Clerck Y.A., Langley K.E.;
"cDNA cloning and expression of a metalloproteinase inhibitor related
to tissue inhibitor of metalloproteinases.";
Proc. Natl. Acad. Sci. U.S.A. 87:2800-2804(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=8810321; DOI=10.1074/jbc.271.41.25498;
Hammani K., Blakis A., Morsette D., Bowcock A., Schmutte C.,
Henriet P., Declerck Y.A.;
"Structure and characterization of the human tissue inhibitor of
metalloproteinases-2 gene.";
J. Biol. Chem. 271:25498-25505(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Skin;
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]
NUCLEOTIDE SEQUENCE OF 30-214.
Malik K., Sejima H., Aoki T., Iwata K.;
Submitted (AUG-1990) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 27-219, AND FUNCTION.
PubMed=2793861;
Stetler-Stevenson W.G., Krutzsch H.C., Liotta L.A.;
"Tissue inhibitor of metalloproteinase (TIMP-2). A new member of the
metalloproteinase inhibitor family.";
J. Biol. Chem. 264:17374-17378(1989).
[7]
PROTEIN SEQUENCE OF 27-219.
PubMed=1480041;
Stetler-Stevenson W.G., Krutzsch H.C., Liotta L.A.;
"TIMP-2: identification and characterization of a new member of the
metalloproteinase inhibitor family.";
Matrix Suppl. 1:299-306(1992).
[8]
PROTEIN SEQUENCE OF 30-51; 124-141 AND 159-173, AND FUNCTION.
PubMed=2554304; DOI=10.1073/pnas.86.21.8207;
Goldberg G.I., Marmer B.L., Grant G.A., Eisen A.Z., Wilhelm S., He C.;
"Human 72-kilodalton type IV collagenase forms a complex with a tissue
inhibitor of metalloproteases designated TIMP-2.";
Proc. Natl. Acad. Sci. U.S.A. 86:8207-8211(1989).
[9]
PROTEIN SEQUENCE OF 27-41.
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
PubMed=8112602; DOI=10.1016/0378-1119(94)90753-6;
de Clerck Y.A., Darville M.I., Eeckhout Y., Rousseau G.G.;
"Characterization of the promoter of the gene encoding human tissue
inhibitor of metalloproteinases-2 (TIMP-2).";
Gene 139:185-191(1994).
[11]
INTERACTION WITH MMP2.
PubMed=1655733;
Howard E.W., Banda M.J.;
"Binding of tissue inhibitor of metalloproteinases 2 to two distinct
sites on human 72-kDa gelatinase. Identification of a stabilization
site.";
J. Biol. Chem. 266:17972-17977(1991).
[12]
INTERACTION WITH MMP2, AND FUNCTION.
PubMed=11710594; DOI=10.1007/s004320100271;
Chattopadhyay N., Mitra A., Frei E., Chatterjee A.;
"Human cervical tumor cell (SiHa) surface alphavbeta3 integrin
receptor has associated matrix metalloproteinase (MMP-2) activity.";
J. Cancer Res. Clin. Oncol. 127:653-658(2001).
[13]
STRUCTURE BY NMR OF 27-153.
PubMed=7918391; DOI=10.1021/bi00205a010;
Williamson R.A., Martorell G., Carr M.D., Murphy G., Docherty A.J.P.,
Freedman R.B., Feeney J.;
"Solution structure of the active domain of tissue inhibitor of
metalloproteinases-2. A new member of the OB fold protein family.";
Biochemistry 33:11745-11759(1994).
[14]
STRUCTURE BY NMR OF 27-153.
PubMed=9705310; DOI=10.1074/jbc.273.34.21736;
Muskett F.W., Frenkiel T.A., Feeney J., Freedman R.B., Carr M.D.,
Williamson R.A.;
"High resolution structure of the N-terminal domain of tissue
inhibitor of metalloproteinases-2 and characterization of its
interaction site with matrix metalloproteinase-3.";
J. Biol. Chem. 273:21736-21743(1998).
[15]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-220.
PubMed=9837731; DOI=10.1006/jmbi.1998.2223;
Tuuttila A., Morgunova E., Bergmann U., Lindqvist Y., Maskos K.,
Fernandez-Catalan C., Bode W., Tryggvason K., Schneider G.;
"Three-dimensional structure of human tissue inhibitor of
metalloproteinases-2 at 2.1-A resolution.";
J. Mol. Biol. 284:1133-1140(1998).
[16]
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH MMP-2, AND
DISULFIDE BOND.
PubMed=12032297; DOI=10.1073/pnas.102185399;
Morgunova E., Tuuttila A., Bergmann U., Tryggvason K.;
"Structural insight into the complex formation of latent matrix
metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.";
Proc. Natl. Acad. Sci. U.S.A. 99:7414-7419(2002).
[17]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-220 IN COMPLEX WITH MMP10
AND ZINC.
PubMed=24073280; DOI=10.1371/journal.pone.0075836;
Batra J., Soares A.S., Mehner C., Radisky E.S.;
"Matrix metalloproteinase-10/TIMP-2 structure and analyses define
conserved core interactions and diverse exosite interactions in
MMP/TIMP complexes.";
PLoS ONE 8:E75836-E75836(2013).
-!- FUNCTION: Complexes with metalloproteinases (such as collagenases)
and irreversibly inactivates them by binding to their catalytic
zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8,
MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.
{ECO:0000269|PubMed:11710594, ECO:0000269|PubMed:2554304,
ECO:0000269|PubMed:2793861}.
-!- SUBUNIT: Interacts (via the C-terminal) with MMP2 (via the C-
terminal PEX domain); the interaction inhibits the MMP2 activity.
{ECO:0000269|PubMed:11710594, ECO:0000269|PubMed:12032297,
ECO:0000269|PubMed:1655733}.
-!- INTERACTION:
P50281:MMP14; NbExp=2; IntAct=EBI-1033507, EBI-992788;
-!- SUBCELLULAR LOCATION: Secreted.
-!- INDUCTION: Down-regulated by TGFB1. {ECO:0000269|PubMed:2380196}.
-!- PTM: The activity of TIMP2 is dependent on the presence of
disulfide bonds.
-!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TIMP2ID42572ch17q25.html";
-----------------------------------------------------------------------
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EMBL; J05593; AAA61186.1; -; mRNA.
EMBL; S48568; AAB19474.1; -; mRNA.
EMBL; U44385; AAC50729.1; -; Genomic_DNA.
EMBL; U44381; AAC50729.1; JOINED; Genomic_DNA.
EMBL; U44382; AAC50729.1; JOINED; Genomic_DNA.
EMBL; U44383; AAC50729.1; JOINED; Genomic_DNA.
EMBL; M32304; AAA59581.1; -; mRNA.
EMBL; BC052605; AAH52605.1; -; mRNA.
EMBL; BC071586; AAH71586.1; -; mRNA.
EMBL; X54533; CAA38400.1; -; mRNA.
EMBL; S68860; AAD14025.1; -; Genomic_DNA.
CCDS; CCDS11758.1; -.
PIR; A37128; A37128.
PIR; I53729; I53729.
RefSeq; NP_003246.1; NM_003255.4.
UniGene; Hs.633514; -.
PDB; 1BR9; X-ray; 2.10 A; A=27-220.
PDB; 1GXD; X-ray; 3.10 A; C/D=27-220.
PDB; 2TMP; NMR; -; A=27-153.
PDB; 4ILW; X-ray; 2.10 A; A/B=27-220.
PDBsum; 1BR9; -.
PDBsum; 1GXD; -.
PDBsum; 2TMP; -.
PDBsum; 4ILW; -.
ProteinModelPortal; P16035; -.
SMR; P16035; -.
BioGrid; 112933; 10.
IntAct; P16035; 4.
MINT; P16035; -.
STRING; 9606.ENSP00000262768; -.
MEROPS; I35.002; -.
iPTMnet; P16035; -.
PhosphoSitePlus; P16035; -.
BioMuta; TIMP2; -.
DMDM; 135854; -.
DOSAC-COBS-2DPAGE; P16035; -.
EPD; P16035; -.
MaxQB; P16035; -.
PaxDb; P16035; -.
PeptideAtlas; P16035; -.
PRIDE; P16035; -.
TopDownProteomics; P16035; -.
DNASU; 7077; -.
Ensembl; ENST00000262768; ENSP00000262768; ENSG00000035862.
GeneID; 7077; -.
KEGG; hsa:7077; -.
UCSC; uc002jwf.4; human.
CTD; 7077; -.
DisGeNET; 7077; -.
EuPathDB; HostDB:ENSG00000035862.12; -.
GeneCards; TIMP2; -.
HGNC; HGNC:11821; TIMP2.
HPA; CAB010203; -.
MIM; 188825; gene.
neXtProt; NX_P16035; -.
OpenTargets; ENSG00000035862; -.
PharmGKB; PA36527; -.
eggNOG; KOG4745; Eukaryota.
eggNOG; ENOG41103NU; LUCA.
GeneTree; ENSGT00390000004555; -.
HOGENOM; HOG000285981; -.
HOVERGEN; HBG068749; -.
InParanoid; P16035; -.
OMA; KMFKGPE; -.
OrthoDB; EOG091G0NIC; -.
PhylomeDB; P16035; -.
TreeFam; TF317409; -.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; P16035; -.
ChiTaRS; TIMP2; human.
EvolutionaryTrace; P16035; -.
GeneWiki; TIMP2; -.
GenomeRNAi; 7077; -.
PRO; PR:P16035; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000035862; -.
CleanEx; HS_TIMP2; -.
ExpressionAtlas; P16035; baseline and differential.
Genevisible; P16035; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0031012; C:extracellular matrix; HDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005578; C:proteinaceous extracellular matrix; IBA:GO_Central.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IBA:GO_Central.
GO; GO:1905049; P:negative regulation of metallopeptidase activity; IDA:UniProtKB.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0032487; P:regulation of Rap protein signal transduction; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0009725; P:response to hormone; IBA:GO_Central.
Gene3D; 3.90.370.10; -; 2.
InterPro; IPR001134; Netrin_domain.
InterPro; IPR001820; TIMP.
InterPro; IPR008993; TIMP-like_OB-fold.
InterPro; IPR015613; TIMP2.
InterPro; IPR027465; TIMP_C.
InterPro; IPR030490; TIMP_CS.
PANTHER; PTHR11844; PTHR11844; 1.
PANTHER; PTHR11844:SF24; PTHR11844:SF24; 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; Metal-binding; Metalloenzyme inhibitor;
Metalloprotease inhibitor; Protease inhibitor; Reference proteome;
Secreted; Signal; Zinc.
SIGNAL 1 26 {ECO:0000269|PubMed:1480041,
ECO:0000269|PubMed:1730286,
ECO:0000269|PubMed:2793861}.
CHAIN 27 220 Metalloproteinase inhibitor 2.
/FTId=PRO_0000034335.
DOMAIN 27 152 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
REGION 27 30 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:4ILW,
ECO:0000269|PubMed:24073280}.
REGION 95 96 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:4ILW,
ECO:0000269|PubMed:24073280}.
METAL 27 27 Zinc; via amino nitrogen and carbonyl
oxygen; shared with metalloproteinase
partner. {ECO:0000244|PDB:4ILW,
ECO:0000269|PubMed:24073280}.
SITE 40 40 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:4ILW,
ECO:0000269|PubMed:24073280}.
SITE 61 61 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:4ILW,
ECO:0000269|PubMed:24073280}.
SITE 67 67 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:4ILW,
ECO:0000269|PubMed:24073280}.
DISULFID 27 98 {ECO:0000255|PROSITE-ProRule:PRU00295,
ECO:0000269|PubMed:12032297}.
DISULFID 29 127 {ECO:0000255|PROSITE-ProRule:PRU00295,
ECO:0000269|PubMed:12032297}.
DISULFID 39 152 {ECO:0000255|PROSITE-ProRule:PRU00295,
ECO:0000269|PubMed:12032297}.
DISULFID 154 201 {ECO:0000255|PROSITE-ProRule:PRU00295,
ECO:0000269|PubMed:12032297}.
DISULFID 159 164 {ECO:0000255|PROSITE-ProRule:PRU00295,
ECO:0000269|PubMed:12032297}.
DISULFID 172 193 {ECO:0000255|PROSITE-ProRule:PRU00295,
ECO:0000269|PubMed:12032297}.
CONFLICT 17 19 LAT -> P (in Ref. 3; AAC50729).
{ECO:0000305}.
CONFLICT 44 50 VIRAKAV -> GKESGDP (in Ref. 10).
{ECO:0000305}.
CONFLICT 78 78 M -> K (in Ref. 6; AA sequence and 7; AA
sequence). {ECO:0000305}.
CONFLICT 82 82 P -> I (in Ref. 6; AA sequence and 7; AA
sequence). {ECO:0000305}.
CONFLICT 96 96 A -> V (in Ref. 5; CAA38400).
{ECO:0000305}.
CONFLICT 101 101 S -> E (in Ref. 6; AA sequence and 7; AA
sequence). {ECO:0000305}.
CONFLICT 118 118 Missing (in Ref. 6; AA sequence and 7; AA
sequence). {ECO:0000305}.
CONFLICT 122 122 M -> R (in Ref. 6; AA sequence and 7; AA
sequence). {ECO:0000305}.
CONFLICT 150 150 M -> Q (in Ref. 6; AA sequence and 7; AA
sequence). {ECO:0000305}.
CONFLICT 175 175 M -> T (in Ref. 6; AA sequence and 7; AA
sequence). {ECO:0000305}.
HELIX 34 40 {ECO:0000244|PDB:1BR9}.
STRAND 41 59 {ECO:0000244|PDB:1BR9}.
STRAND 61 63 {ECO:0000244|PDB:4ILW}.
STRAND 65 81 {ECO:0000244|PDB:1BR9}.
STRAND 88 91 {ECO:0000244|PDB:1BR9}.
HELIX 95 97 {ECO:0000244|PDB:1BR9}.
TURN 104 107 {ECO:0000244|PDB:4ILW}.
STRAND 109 118 {ECO:0000244|PDB:1BR9}.
STRAND 121 123 {ECO:0000244|PDB:1BR9}.
STRAND 130 132 {ECO:0000244|PDB:1BR9}.
HELIX 133 135 {ECO:0000244|PDB:1BR9}.
HELIX 138 143 {ECO:0000244|PDB:1BR9}.
TURN 144 148 {ECO:0000244|PDB:1BR9}.
HELIX 149 151 {ECO:0000244|PDB:1BR9}.
STRAND 154 158 {ECO:0000244|PDB:1BR9}.
STRAND 161 163 {ECO:0000244|PDB:1BR9}.
STRAND 171 174 {ECO:0000244|PDB:1BR9}.
HELIX 176 180 {ECO:0000244|PDB:1BR9}.
STRAND 181 185 {ECO:0000244|PDB:1GXD}.
HELIX 186 190 {ECO:0000244|PDB:1BR9}.
STRAND 192 195 {ECO:0000244|PDB:1BR9}.
STRAND 197 199 {ECO:0000244|PDB:4ILW}.
STRAND 201 204 {ECO:0000244|PDB:1BR9}.
SEQUENCE 220 AA; 24399 MW; 603E5B1C9F94735D CRC64;
MGAAARTLRL ALGLLLLATL LRPADACSCS PVHPQQAFCN ADVVIRAKAV SEKEVDSGND
IYGNPIKRIQ YEIKQIKMFK GPEKDIEFIY TAPSSAVCGV SLDVGGKKEY LIAGKAEGDG
KMHITLCDFI VPWDTLSTTQ KKSLNHRYQM GCECKITRCP MIPCYISSPD ECLWMDWVTE
KNINGHQAKF FACIKRSDGS CAWYRGAAPP KQEFLDIEDP


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