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Metalloproteinase inhibitor 2 (Collagenase inhibitor) (Tissue inhibitor of metalloproteinases 2) (TIMP-2)

 TIMP2_BOVIN             Reviewed;         220 AA.
P16368; Q3SZU3; Q9TVB1;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 2.
20-JUN-2018, entry version 146.
RecName: Full=Metalloproteinase inhibitor 2;
AltName: Full=Collagenase inhibitor;
AltName: Full=Tissue inhibitor of metalloproteinases 2;
Short=TIMP-2;
Flags: Precursor;
Name=TIMP2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 22-218.
TISSUE=Skeletal muscle;
Balcerzak D., Querengesser L., Dixon W.T., Baracos V.E.;
"Involvement of fibroblasts and muscle cells in the expression of an
extracellular proteolytic cascade in bovine skeletal muscle.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 27-71.
TISSUE=Cartilage;
PubMed=3005321;
Murray J.B., Allison K., Sudhalter J., Langer R.;
"Purification and partial amino acid sequence of a bovine cartilage-
derived collagenase inhibitor.";
J. Biol. Chem. 261:4154-4159(1986).
[5]
PROTEIN SEQUENCE OF 27-71.
PubMed=2551903;
de Clerck Y.A., Yean T.D., Ratzkin B.J., Lu H.S., Langley K.E.;
"Purification and characterization of two related but distinct
metalloproteinase inhibitors secreted by bovine aortic endothelial
cells.";
J. Biol. Chem. 264:17445-17453(1989).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 27-71.
PubMed=8424773; DOI=10.1042/bj2890065;
De Clerck Y.A., Yean T.D., Lee Y., Tomich J.M., Langley K.E.;
"Characterization of the functional domain of tissue inhibitor of
metalloproteinases-2 (TIMP-2).";
Biochem. J. 289:65-69(1993).
[7]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 27-210 IN COMPLEX WITH
MMP-1.
PubMed=9724659; DOI=10.1093/emboj/17.17.5238;
Fernandez-Catalan C., Bode W., Huber R., Turk D., Calvete J.J.,
Lichte A., Tschesche H., Maskos K.;
"Crystal structure of the complex formed by the membrane type 1-matrix
metalloproteinase with the tissue inhibitor of metalloproteinases-2,
the soluble progelatinase A receptor.";
EMBO J. 17:5238-5248(1998).
[8]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-206 IN COMPLEX WITH
MMP-13, AND DISULFIDE BOND.
PubMed=17196980; DOI=10.1016/j.jmb.2006.11.072;
Maskos K., Lang R., Tschesche H., Bode W.;
"Flexibility and variability of TIMP binding: X-ray structure of the
complex between collagenase-3/MMP-13 and TIMP-2.";
J. Mol. Biol. 366:1222-1231(2007).
-!- FUNCTION: Complexes with metalloproteinases (such as collagenases)
and irreversibly inactivates them by binding to their catalytic
zinc cofactor.
-!- SUBUNIT: Interacts (via the C-terminal) with MMP2 (via the C-
terminal PEX domain); the interaction inhibits the MMP2 activity.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: The activity of TIMP2 is dependent on the presence of
disulfide bonds.
-!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M32303; AAA30636.1; -; mRNA.
EMBL; BC102710; AAI02711.1; -; mRNA.
EMBL; AF144764; AAD30304.1; -; mRNA.
PIR; A35996; A35996.
RefSeq; NP_776897.2; NM_174472.4.
UniGene; Bt.111410; -.
PDB; 1BQQ; X-ray; 2.75 A; T=27-210.
PDB; 1BUV; X-ray; 2.75 A; T=27-210.
PDB; 2E2D; X-ray; 2.00 A; C=27-206.
PDBsum; 1BQQ; -.
PDBsum; 1BUV; -.
PDBsum; 2E2D; -.
ProteinModelPortal; P16368; -.
SMR; P16368; -.
IntAct; P16368; 1.
STRING; 9913.ENSBTAP00000014476; -.
MEROPS; I35.002; -.
PaxDb; P16368; -.
PRIDE; P16368; -.
GeneID; 282093; -.
KEGG; bta:282093; -.
CTD; 7077; -.
eggNOG; KOG4745; Eukaryota.
eggNOG; ENOG41103NU; LUCA.
HOGENOM; HOG000285981; -.
HOVERGEN; HBG068749; -.
InParanoid; P16368; -.
KO; K22583; -.
EvolutionaryTrace; P16368; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IBA:GO_Central.
GO; GO:0002020; F:protease binding; IBA:GO_Central.
GO; GO:0043086; P:negative regulation of catalytic activity; IBA:GO_Central.
GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IBA:GO_Central.
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; -; 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:2551903,
ECO:0000269|PubMed:3005321}.
CHAIN 27 220 Metalloproteinase inhibitor 2.
/FTId=PRO_0000034331.
DOMAIN 27 152 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
REGION 27 30 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:2E2D,
ECO:0000269|PubMed:17196980}.
METAL 27 27 Zinc; via amino nitrogen and carbonyl
oxygen; shared with metalloproteinase
partner. {ECO:0000244|PDB:2E2D,
ECO:0000269|PubMed:17196980}.
SITE 64 64 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:2E2D,
ECO:0000269|PubMed:17196980}.
SITE 96 96 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:2E2D,
ECO:0000269|PubMed:17196980}.
SITE 158 158 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:2E2D,
ECO:0000269|PubMed:17196980}.
SITE 177 177 Involved in metalloproteinase-binding.
{ECO:0000244|PDB:2E2D,
ECO:0000269|PubMed:17196980}.
DISULFID 27 98 {ECO:0000244|PDB:2E2D,
ECO:0000269|PubMed:17196980}.
DISULFID 29 127 {ECO:0000244|PDB:2E2D,
ECO:0000269|PubMed:17196980}.
DISULFID 39 152 {ECO:0000244|PDB:2E2D,
ECO:0000269|PubMed:17196980}.
DISULFID 154 201 {ECO:0000244|PDB:2E2D,
ECO:0000269|PubMed:17196980}.
DISULFID 159 164 {ECO:0000244|PDB:2E2D,
ECO:0000269|PubMed:17196980}.
DISULFID 172 193 {ECO:0000244|PDB:2E2D,
ECO:0000269|PubMed:17196980}.
CONFLICT 15 15 L -> M (in Ref. 2; AAI02711).
{ECO:0000305}.
CONFLICT 42 42 D -> C (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 56 56 D -> E (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 68 68 R -> S (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 88 88 F -> L (in Ref. 2; AAI02711).
{ECO:0000305}.
CONFLICT 94 95 AA -> SS (in Ref. 2; AAI02711).
{ECO:0000305}.
HELIX 34 40 {ECO:0000244|PDB:2E2D}.
STRAND 42 59 {ECO:0000244|PDB:2E2D}.
STRAND 61 64 {ECO:0000244|PDB:1BQQ}.
STRAND 65 81 {ECO:0000244|PDB:2E2D}.
STRAND 88 91 {ECO:0000244|PDB:2E2D}.
HELIX 95 97 {ECO:0000244|PDB:2E2D}.
STRAND 105 107 {ECO:0000244|PDB:2E2D}.
STRAND 109 116 {ECO:0000244|PDB:2E2D}.
STRAND 118 120 {ECO:0000244|PDB:1BQQ}.
STRAND 121 123 {ECO:0000244|PDB:2E2D}.
STRAND 130 132 {ECO:0000244|PDB:2E2D}.
HELIX 133 135 {ECO:0000244|PDB:2E2D}.
HELIX 138 143 {ECO:0000244|PDB:2E2D}.
TURN 144 146 {ECO:0000244|PDB:2E2D}.
HELIX 147 151 {ECO:0000244|PDB:2E2D}.
STRAND 154 158 {ECO:0000244|PDB:2E2D}.
STRAND 160 162 {ECO:0000244|PDB:2E2D}.
STRAND 171 174 {ECO:0000244|PDB:2E2D}.
HELIX 176 179 {ECO:0000244|PDB:2E2D}.
STRAND 183 185 {ECO:0000244|PDB:1BQQ}.
HELIX 186 190 {ECO:0000244|PDB:2E2D}.
STRAND 192 195 {ECO:0000244|PDB:2E2D}.
STRAND 197 204 {ECO:0000244|PDB:2E2D}.
SEQUENCE 220 AA; 24355 MW; 9A5438737110E7B7 CRC64;
MGAAARSLPL AFCLLLLGTL LPRADACSCS PVHPQQAFCN ADIVIRAKAV NKKEVDSGND
IYGNPIKRIQ YEIKQIKMFK GPDQDIEFIY TAPAAAVCGV SLDIGGKKEY LIAGKAEGNG
NMHITLCDFI VPWDTLSATQ KKSLNHRYQM GCECKITRCP MIPCYISSPD ECLWMDWVTE
KNINGHQAKF FACIKRSDGS CAWYRGAAPP KQEFLDIEDP


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