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Q9TRZ7

- TIMP2_RABIT

UniProt

Q9TRZ7 - TIMP2_RABIT

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Protein

Metalloproteinase inhibitor 2

Gene

TIMP2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - 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

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase inhibitor activity Source: UniProtKB-KW
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: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
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

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.
[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 .
UniGenei Ocu.2314.

3D structure databases

ProteinModelPortali Q9TRZ7.
SMRi Q9TRZ7. Positions 1-192.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi I35.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG243625.
HOGENOMi HOG000285981.
HOVERGENi HBG068749.
InParanoidi Q9TRZ7.

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

  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: October 29, 2014
This is version 79 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