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Protein

Metalloproteinase inhibitor 2

Gene

TIMP2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 bindingi1 – 11Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partnerBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor

Keywords - Ligandi

Metal-binding, Zinc

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194Metalloproteinase inhibitor 2PRO_0000220984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi1 ↔ 72PROSITE-ProRule annotation
Disulfide bondi3 ↔ 101PROSITE-ProRule annotation
Disulfide bondi13 ↔ 126PROSITE-ProRule annotation
Disulfide bondi128 ↔ 175PROSITE-ProRule annotation
Disulfide bondi133 ↔ 138PROSITE-ProRule annotation
Disulfide bondi146 ↔ 167PROSITE-ProRule annotation

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond

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

STRINGi9986.ENSOCUP00000003105.

Structurei

3D structure databases

ProteinModelPortaliQ9TRZ7.
SMRiQ9TRZ7. Positions 1-192.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 126126NTRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 55Involved in metalloproteinase-bindingBy similarity
Regioni69 – 702Involved in metalloproteinase-bindingBy similarity

Sequence similaritiesi

Contains 1 NTR domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG243625.
HOGENOMiHOG000285981.
HOVERGENiHBG068749.
InParanoidiQ9TRZ7.

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.
IPR030490. TIMP_CS.
[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.

Q9TRZ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
CSCSPVHPQQ AFCNADIVIR AKAVNKKEVD SGNDIYGNPI KRIQYEIKQI
60 70 80 90 100
KMFKGPDQDI EFIYTAPSSA VCGVSLDIGG KKEYLIAGKA EGNGNMHITL
110 120 130 140 150
CDFIVPWDTL SATQKKSLNH RYQMGCECKI TRCPMIPCYI SSPDECLWMD
160 170 180 190
WVTEKNINRH QAKFFACIKR SDGSCAWYRG AAPPKQEFLD IEDP
Length:194
Mass (Da):21,849
Last modified:May 1, 2000 - v1
Checksum:iCDC8101A2D38C4A9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171I → V in AAC95005 (PubMed:9837780).Curated
Sequence conflicti25 – 262NK → SE in AAC95005 (PubMed:9837780).Curated
Sequence conflicti58 – 581Q → K in AAC95005 (PubMed:9837780).Curated
Sequence conflicti78 – 781I → V in AAC95005 (PubMed:9837780).Curated
Sequence conflicti93 – 953NGN → DGR in AAC95005 (PubMed:9837780).Curated
Sequence conflicti109 – 1091T → S in AAC95005 (PubMed:9837780).Curated
Sequence conflicti112 – 1121A → S in AAC95005 (PubMed:9837780).Curated
Sequence conflicti131 – 1311T → S in AAC95005 (PubMed:9837780).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069713 mRNA. Translation: AAC95005.1.
UniGeneiOcu.2314.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069713 mRNA. Translation: AAC95005.1.
UniGeneiOcu.2314.

3D structure databases

ProteinModelPortaliQ9TRZ7.
SMRiQ9TRZ7. Positions 1-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000003105.

Protein family/group databases

MEROPSiI35.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG243625.
HOGENOMiHOG000285981.
HOVERGENiHBG068749.
InParanoidiQ9TRZ7.

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.
IPR030490. TIMP_CS.
[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]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and characterization of rabbit TIMP2."
    Wertheimer S.J., Katz S.L.
    Inflamm. Res. 44:S121-S122(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Temporal alterations in mRNA levels for proteinases and inhibitors and their potential regulators in the healing medial collateral ligament."
    Reno C., Boykiw R., Martinez M.L., Hart D.A.
    Biochem. Biophys. Res. Commun. 252:757-763(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-154.
    Strain: New Zealand white.

Entry informationi

Entry nameiTIMP2_RABIT
AccessioniPrimary (citable) accession number: Q9TRZ7
Secondary accession number(s): O97589
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.