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Q9TRZ7 (TIMP2_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metalloproteinase inhibitor 2
Alternative name(s):
Tissue inhibitor of metalloproteinases 2
Short name=TIMP-2
Gene names
Name:TIMP2
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Subunit structure

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

Subcellular location

Secreted.

Post-translational modification

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

Sequence similarities

Belongs to the protease inhibitor I35 (TIMP) family. [View classification]

Contains 1 NTR domain.

Ontologies

Keywords
   Cellular componentSecreted
   LigandMetal-binding
Zinc
   Molecular functionMetalloenzyme inhibitor
Metalloprotease inhibitor
Protease inhibitor
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194Metalloproteinase inhibitor 2
PRO_0000220984

Regions

Domain1 – 126126NTR
Region1 – 55Involved in metalloproteinase-binding By similarity
Region69 – 702Involved in metalloproteinase-binding By similarity

Sites

Metal binding11Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner By similarity

Amino acid modifications

Disulfide bond1 ↔ 72 By similarity
Disulfide bond3 ↔ 101 By similarity
Disulfide bond13 ↔ 126 By similarity
Disulfide bond128 ↔ 175 By similarity
Disulfide bond133 ↔ 138 By similarity
Disulfide bond146 ↔ 167 By similarity

Experimental info

Sequence conflict171I → V in AAC95005. Ref.2
Sequence conflict25 – 262NK → SE in AAC95005. Ref.2
Sequence conflict581Q → K in AAC95005. Ref.2
Sequence conflict781I → V in AAC95005. Ref.2
Sequence conflict93 – 953NGN → DGR in AAC95005. Ref.2
Sequence conflict1091T → S in AAC95005. Ref.2
Sequence conflict1121A → S in AAC95005. Ref.2
Sequence conflict1311T → S in AAC95005. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9TRZ7 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CDC8101A2D38C4A9

FASTA19421,849
        10         20         30         40         50         60 
CSCSPVHPQQ AFCNADIVIR AKAVNKKEVD SGNDIYGNPI KRIQYEIKQI KMFKGPDQDI 

        70         80         90        100        110        120 
EFIYTAPSSA VCGVSLDIGG KKEYLIAGKA EGNGNMHITL CDFIVPWDTL SATQKKSLNH 

       130        140        150        160        170        180 
RYQMGCECKI TRCPMIPCYI SSPDECLWMD WVTEKNINRH QAKFFACIKR SDGSCAWYRG 

       190 
AAPPKQEFLD IEDP 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF069713 mRNA. Translation: AAC95005.1.
UniGeneOcu.2314.

3D structure databases

ProteinModelPortalQ9TRZ7.
SMRQ9TRZ7. Positions 1-192.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSI35.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG243625.
HOGENOMHOG000285981.
HOVERGENHBG068749.

Family and domain databases

Gene3D3.90.370.10. 1 hit.
InterProIPR001134. Netrin_domain.
IPR001820. Prot_inh_TIMP.
IPR008993. TIMP-like_OB-fold.
IPR015613. TIMP2.
IPR027465. TIMP_C_dom.
[Graphical view]
PANTHERPTHR11844. PTHR11844. 1 hit.
PTHR11844:SF7. PTHR11844:SF7. 1 hit.
PfamPF00965. TIMP. 1 hit.
[Graphical view]
SMARTSM00206. NTR. 1 hit.
[Graphical view]
SUPFAMSSF50242. SSF50242. 1 hit.
PROSITEPS50189. NTR. 1 hit.
PS00288. TIMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTIMP2_RABIT
AccessionPrimary (citable) accession number: Q9TRZ7
Secondary accession number(s): O97589
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families