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P20414 (TIMP1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 89. 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 1
Alternative name(s):
Embryogenin-1
Short name=EG-1
Tissue inhibitor of metalloproteinases 1
Short name=TIMP-1
Gene names
Name:TIMP1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Secreted.

Post-translational modification

The activity of TIMP1 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
   Biological processErythrocyte maturation
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionMetalloenzyme inhibitor
Metalloprotease inhibitor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processerythrocyte maturation

Inferred from electronic annotation. Source: UniProtKB-KW

   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

Signal peptide1 – 2323 Ref.6
Chain24 – 207184Metalloproteinase inhibitor 1
PRO_0000034320

Regions

Domain24 – 147124NTR
Region24 – 285Involved in metalloproteinase-binding By similarity
Region90 – 912Involved in metalloproteinase-binding By similarity

Sites

Metal binding241Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner By similarity

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation1011N-linked (GlcNAc...) Potential
Disulfide bond24 ↔ 93 By similarity
Disulfide bond26 ↔ 122 By similarity
Disulfide bond36 ↔ 147 By similarity
Disulfide bond150 ↔ 197 By similarity
Disulfide bond155 ↔ 160 By similarity
Disulfide bond168 ↔ 189 By similarity

Sequences

Sequence LengthMass (Da)Tools
P20414 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: E672BEE2E865F3F7

FASTA20723,032
        10         20         30         40         50         60 
MAPFAPMASG ILLLLWLTAP SRACTCVPPH PQTAFCNSDV VIRAKFVGTA EVNETALYQR 

        70         80         90        100        110        120 
YEIKMTKMFK GFSALRDAPD IRFIYTPAME SVCGYFHRSQ NRSEEFLIAG QLSNGHLHIT 

       130        140        150        160        170        180 
TCSFVAPWNS MSSAQRRGFT KTYAAGCEEC TVFPCSSIPC KLQSDTHCLW TDQLLTGSDK 

       190        200 
GFQSRHLACL PREPGLCTWQ SLRAQMA 

« Hide

References

« Hide 'large scale' references
[1]"mRNA of bovine tissue inhibitor of metalloproteinase: sequence and expression in bovine ovarian tissue."
Freudenstein J., Wagner S., Luck R.M., Einspanier R., Scheit K.H.
Biochem. Biophys. Res. Commun. 171:250-256(1990) [PubMed: 2393392] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Tissue inhibitor of metalloproteinases (TIMP-1) produced by granulosa and oviduct cells enhances in vitro development of bovine embryo."
Satoh T., Kobayashi K., Yamashita S., Kikuchi M., Sendai Y., Hoshi H.
Biol. Reprod. 50:835-844(1994) [PubMed: 8199264] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"ACTH induces TIMP-1 expression and inhibits collagenase in adrenal cortex cells."
Reichenstein M., Reich R., Lehoux J.-G., Hanukoglu I.
Mol. Cell. Endocrinol. 215:109-114(2004) [PubMed: 15026182] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adrenal cortex.
[4]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[5]"Involvement of fibroblasts and muscle cells in the expression of an extracellular proteolytic cascade in bovine skeletal muscle."
Balcerzak D., Querengesser L., Dixon W.T., Baracos V.E.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-191.
Tissue: Skeletal muscle.
[6]"Purification and characterization of two related but distinct metalloproteinase inhibitors secreted by bovine aortic endothelial cells."
de Clerck Y.A., Yean T.D., Ratzkin B.J., Lu H.S., Langley K.E.
J. Biol. Chem. 264:17445-17453(1989) [PubMed: 2551903] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 24-69.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60073 mRNA. Translation: AAA30784.1.
S70841 mRNA. Translation: AAB30892.1.
AY295346 mRNA. Translation: AAP44413.1.
BC102489 mRNA. Translation: AAI02490.1.
AF144763 mRNA. Translation: AAD30303.1.
IPIIPI00709084.
PIRA35685.
RefSeqNP_776896.1. NM_174471.3.
UniGeneBt.27976.

3D structure databases

ProteinModelPortalP20414.
SMRP20414. Positions 24-204.
ModBaseSearch...

Protein-protein interaction databases

STRINGP20414.

Proteomic databases

PRIDEP20414.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000006653; ENSBTAP00000006653; ENSBTAG00000005043.
GeneID282092.
KEGGbta:282092.

Organism-specific databases

CTD7076.

Phylogenomic databases

eggNOGmaNOG18103.
HOVERGENHBG068749.
InParanoidP20414.
OMASSIPCKL.
OrthoDBEOG44J2K2.
PhylomeDBP20414.

Family and domain databases

InterProIPR001134. Netrin_domain.
IPR001820. Prot_inh_TIMP.
IPR008993. TIMP-like_OB-fold.
IPR015611. TIMP1.
[Graphical view]
PANTHERPTHR11844. Prot_inh_TIMP. 1 hit.
PTHR11844:SF5. TIMP1. 1 hit.
PfamPF00965. TIMP. 1 hit.
[Graphical view]
SMARTSM00206. NTR. 1 hit.
[Graphical view]
SUPFAMSSF50242. TIMP_like. 1 hit.
PROSITEPS50189. NTR. 1 hit.
PS00288. TIMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTIMP1_BOVIN
AccessionPrimary (citable) accession number: P20414
Secondary accession number(s): Q3T098, Q53ZP2, Q9TVB0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 19, 2011
This is version 89 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