Q9WUC6 (TIMP2_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Metalloproteinase inhibitor 2

Alternative name(s):
Tissue inhibitor of metalloproteinases 2
Short name=TIMP-2

Gene names

Name:

TIMP2

Organism

Cavia porcellus (Guinea pig) [Reference proteome]

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Tissue specificity	Predominantly expressed in the lung in alveolar macrophages and epithelial cells. Also found in brain, kidney, intestine, spleen and heart.
Post-translational modification	The activity of TIMP2 is dependent on the presence of disulfide bonds.
Sequence similarities	Belongs to the protease inhibitor I35 (TIMP) family. [View classification] Contains 1 NTR domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Metalloenzyme inhibitor Metalloprotease inhibitor Protease inhibitor
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to organic substance Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara regulation of MAPK cascade Inferred from electronic annotation. Source: Compara regulation of cAMP metabolic process Inferred from electronic annotation. Source: Compara regulation of neuron differentiation Inferred from electronic annotation. Source: Compara
Cellular_component	basement membrane Inferred from electronic annotation. Source: Compara cell surface Inferred from electronic annotation. Source: Compara
Molecular_function	enzyme activator activity Inferred from electronic annotation. Source: Compara metal 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	Potential
	Chain	27 – 220	194	Metalloproteinase inhibitor 2		PRO_0000034333
Regions
	Domain	27 – 152	126	NTR
	Region	27 – 31	5	Involved in metalloproteinase-binding By similarity
	Region	95 – 96	2	Involved in metalloproteinase-binding By similarity
Sites
	Metal binding	27	1	Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner By similarity
Amino acid modifications
	Disulfide bond	27 ↔ 98		By similarity
	Disulfide bond	29 ↔ 127		By similarity
	Disulfide bond	39 ↔ 152		By similarity
	Disulfide bond	154 ↔ 201		By similarity
	Disulfide bond	159 ↔ 164		By similarity
	Disulfide bond	172 ↔ 193		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9WUC6 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 2A2541764755B9AF	FASTA	220	24,318
	10 20 30 40 50 60 MGATARSLRL ALGLLLLGTL PRGADACSCS PVHPQQAFCN ADVVIRAKAV SEKEVDSGND 70 80 90 100 110 120 IYGNPIKRIQ YEIKQIKMFK GPEKDIEFIY TAPSSAVCGV SLDVGGKKEY LIAGKAEGDG 130 140 150 160 170 180 KMHITLCDFI VPWDTLSTTQ KKSLNHRYQM GCECKITRCP MIPCYISSPD ECLWMDWVTE 190 200 210 220 KSINGHQAKF FACIKRSDGS CAWYRGAAPP KQEFLDIEDP

References

[1]	"Cloning and expression of guinea pig TIMP-2. Expression in normal and hyperoxic lung injury." Melendez J., Maldonado V., Selman M., Pardo A. Am. J. Physiol. 278:L737-L743(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Hartley. Tissue: Lung.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF127803 mRNA. Translation: AAD28252.1.
RefSeq	NP_001166495.1. NM_001173024.1.
3D structure databases
ProteinModelPortal	Q9WUC6.
SMR	Q9WUC6. Positions 27-218.
ModBase	Search...
Protein-protein interaction databases
STRING	10141.ENSCPOP00000007780.
Protein family/group databases
MEROPS	I35.002.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSCPOT00000008741; ENSCPOP00000007780; ENSCPOG00000008663.
GeneID	100135629.
Organism-specific databases
CTD	7077.
Phylogenomic databases
eggNOG	NOG243625.
GeneTree	ENSGT00390000004555.
HOGENOM	HOG000285981.
HOVERGEN	HBG068749.
InParanoid	Q9WUC6.
OMA	KMFKGPE.
OrthoDB	EOG4XPQGS.
Family and domain databases
InterPro	IPR001134. Netrin_domain. IPR001820. Prot_inh_TIMP. IPR008993. TIMP-like_OB-fold. IPR015613. TIMP2. [Graphical view]
PANTHER	PTHR11844. PTHR11844. 1 hit. PTHR11844:SF7. PTHR11844:SF7. 1 hit.
Pfam	PF00965. TIMP. 1 hit. [Graphical view]
SMART	SM00206. NTR. 1 hit. [Graphical view]
SUPFAM	SSF50242. TIMP_like. 1 hit.
PROSITE	PS50189. NTR. 1 hit. PS00288. TIMP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TIMP2_CAVPO

Accession

Primary (citable) accession number: Q9WUC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program