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P30121

- TIMP2_RAT

UniProt

P30121 - TIMP2_RAT

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Protein

Metalloproteinase inhibitor 2

Gene

Timp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partnerBy similarity

GO - Molecular functioni

  1. enzyme activator activity Source: Ensembl
  2. integrin binding Source: RGD
  3. metal ion binding Source: UniProtKB-KW
  4. metalloendopeptidase inhibitor activity Source: RGD

GO - Biological processi

  1. aging Source: RGD
  2. cellular response to organic substance Source: Ensembl
  3. central nervous system development Source: RGD
  4. negative regulation of cell proliferation Source: RGD
  5. negative regulation of endopeptidase activity Source: GOC
  6. negative regulation of mitotic cell cycle Source: RGD
  7. negative regulation of proteolysis Source: RGD
  8. negative regulation of Ras protein signal transduction Source: RGD
  9. positive regulation of adenylate cyclase activity Source: RGD
  10. positive regulation of MAPK cascade Source: RGD
  11. positive regulation of neuron differentiation Source: RGD
  12. regulation of Rap protein signal transduction Source: RGD
  13. response to cytokine Source: RGD
  14. response to drug Source: RGD
  15. spermatogenesis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_198590. Activation of Matrix Metalloproteinases.

Protein family/group databases

MEROPSiI35.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Metalloproteinase inhibitor 2
Alternative name(s):
Tissue inhibitor of metalloproteinases 2
Short name:
TIMP-2
Gene namesi
Name:Timp2
Synonyms:Timp-2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi61312. Timp2.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: Ensembl
  2. cell surface Source: RGD
  3. extracellular space Source: RGD
  4. extracellular vesicular exosome Source: Ensembl
  5. growth cone Source: RGD
  6. neuronal cell body Source: RGD
  7. neuron projection Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 220194Metalloproteinase inhibitor 2PRO_0000034337Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 98PROSITE-ProRule annotation
Disulfide bondi29 ↔ 127PROSITE-ProRule annotation
Disulfide bondi39 ↔ 152PROSITE-ProRule annotation
Disulfide bondi154 ↔ 201PROSITE-ProRule annotation
Disulfide bondi159 ↔ 164PROSITE-ProRule annotation
Disulfide bondi172 ↔ 193PROSITE-ProRule annotation

Post-translational modificationi

The activity of TIMP2 is dependent on the presence of disulfide bonds.

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP30121.

Expressioni

Gene expression databases

GenevestigatoriP30121.

Interactioni

Subunit structurei

Interacts (via the C-terminal) with MMP2 (via the C-terminal PEX domain); the interaction inhibits the MMP2 activity.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004290.

Structurei

3D structure databases

ProteinModelPortaliP30121.
SMRiP30121. Positions 27-208.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 152126NTRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni27 – 315Involved in metalloproteinase-bindingBy similarity
Regioni95 – 962Involved in metalloproteinase-bindingBy similarity

Sequence similaritiesi

Contains 1 NTR domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG243625.
GeneTreeiENSGT00390000004555.
HOGENOMiHOG000285981.
HOVERGENiHBG068749.
InParanoidiP30121.
OMAiSAPEECL.
OrthoDBiEOG79GT74.
PhylomeDBiP30121.

Family and domain databases

Gene3Di3.90.370.10. 1 hit.
InterProiIPR001134. Netrin_domain.
IPR001820. Prot_inh_TIMP.
IPR008993. TIMP-like_OB-fold.
IPR015613. TIMP2.
IPR027465. TIMP_C_dom.
[Graphical view]
PANTHERiPTHR11844. PTHR11844. 1 hit.
PTHR11844:SF7. PTHR11844:SF7. 1 hit.
PfamiPF00965. TIMP. 1 hit.
[Graphical view]
SMARTiSM00206. NTR. 1 hit.
[Graphical view]
SUPFAMiSSF50242. SSF50242. 1 hit.
PROSITEiPS50189. NTR. 1 hit.
PS00288. TIMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30121-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAAARSLRL ALGLLLLATL LRPADACSCS PVHPQQAFCN ADVVIRAKAV
60 70 80 90 100
SEKEVDSGND IYGNPIKRIQ YEIKQIKMFK GPDKDIEFIY TAPSSAVCGV
110 120 130 140 150
SLDVGGKKEY LIAGKAEGDG KMHITLCDFI VPWDTLSITQ KKSLNHRYQM
160 170 180 190 200
GCECKITRCP MIPCYISSPD ECLWMDWVTE KSINGHQAKF FACIKRSDGS
210 220
CAWYRGAAPP KQEFLDIEDP
Length:220
Mass (Da):24,356
Last modified:October 1, 1996 - v3
Checksum:i1C97A3F050C3AE7D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71S → T in AAA21553. (PubMed:8203893)Curated
Sequence conflicti153 – 1531E → Q in AAA21553. (PubMed:8203893)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U14526 mRNA. Translation: AAA21553.1.
L31884 mRNA. Translation: AAA84581.1.
S72594 mRNA. Translation: AAC60687.1.
S82718 mRNA. Translation: AAB49507.1.
AJ409332 mRNA. Translation: CAC35060.1.
BC084714 mRNA. Translation: AAH84714.1.
PIRiS45683.
RefSeqiNP_068824.1. NM_021989.2.
UniGeneiRn.10161.

Genome annotation databases

EnsembliENSRNOT00000004290; ENSRNOP00000004290; ENSRNOG00000003148.
GeneIDi29543.
KEGGirno:29543.
UCSCiRGD:61312. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U14526 mRNA. Translation: AAA21553.1 .
L31884 mRNA. Translation: AAA84581.1 .
S72594 mRNA. Translation: AAC60687.1 .
S82718 mRNA. Translation: AAB49507.1 .
AJ409332 mRNA. Translation: CAC35060.1 .
BC084714 mRNA. Translation: AAH84714.1 .
PIRi S45683.
RefSeqi NP_068824.1. NM_021989.2.
UniGenei Rn.10161.

3D structure databases

ProteinModelPortali P30121.
SMRi P30121. Positions 27-208.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000004290.

Protein family/group databases

MEROPSi I35.002.

Proteomic databases

PaxDbi P30121.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000004290 ; ENSRNOP00000004290 ; ENSRNOG00000003148 .
GeneIDi 29543.
KEGGi rno:29543.
UCSCi RGD:61312. rat.

Organism-specific databases

CTDi 7077.
RGDi 61312. Timp2.

Phylogenomic databases

eggNOGi NOG243625.
GeneTreei ENSGT00390000004555.
HOGENOMi HOG000285981.
HOVERGENi HBG068749.
InParanoidi P30121.
OMAi SAPEECL.
OrthoDBi EOG79GT74.
PhylomeDBi P30121.

Enzyme and pathway databases

Reactomei REACT_198590. Activation of Matrix Metalloproteinases.

Miscellaneous databases

NextBioi 609549.
PROi P30121.

Gene expression databases

Genevestigatori P30121.

Family and domain databases

Gene3Di 3.90.370.10. 1 hit.
InterProi IPR001134. Netrin_domain.
IPR001820. Prot_inh_TIMP.
IPR008993. TIMP-like_OB-fold.
IPR015613. TIMP2.
IPR027465. TIMP_C_dom.
[Graphical view ]
PANTHERi PTHR11844. PTHR11844. 1 hit.
PTHR11844:SF7. PTHR11844:SF7. 1 hit.
Pfami PF00965. TIMP. 1 hit.
[Graphical view ]
SMARTi SM00206. NTR. 1 hit.
[Graphical view ]
SUPFAMi SSF50242. SSF50242. 1 hit.
PROSITEi PS50189. NTR. 1 hit.
PS00288. TIMP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and regulation of rat tissue inhibitor of metalloproteinases-2 in osteoblastic cells."
    Cook T.F., Burke J.S., Bergman K.D., Quinn C.O., Jeffrey J.J., Partridge N.C.
    Arch. Biochem. Biophys. 311:313-320(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Bone.
  2. Gibbons K.L., O'Grady R.L., Piper A.A.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary gland.
  3. "Cloning of the rat tissue inhibitor of metalloproteinases type 2 (TIMP-2) gene: analysis of its expression in normal and transformed thyroid cells."
    Santoro M., Battaglia C., Zhang L., Carlomagno F., Martelli M.L., Salvatore D., Fusco A.
    Exp. Cell Res. 213:398-403(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Purification, cDNA cloning, and developmental changes in the steady-state mRNA level of rat testicular tissue inhibitor of metalloproteases-2 (TIMP-2)."
    Grima J., Calcagno K., Cheng C.Y.
    J. Androl. 17:263-275(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  5. "Cardiac remodeling after long term norepinephrine treatment in rats."
    Briest W., Hoelzl A., Rassler B., Deten A., Leicht M., Baba H.A., Zimmer H.G.
    Cardiovasc. Res. 52:265-273(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Heart.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  7. "Purification and sequence analysis of two rat tissue inhibitors of metalloproteinases."
    Roswit W.T., McCourt D.W., Partridge N.C., Jeffrey J.J.
    Arch. Biochem. Biophys. 292:402-410(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-48.

Entry informationi

Entry nameiTIMP2_RAT
AccessioniPrimary (citable) accession number: P30121
Secondary accession number(s): Q546J4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3