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P39876 (TIMP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 3
Alternative name(s):
Tissue inhibitor of metalloproteinases 3
Short name=TIMP-3
Gene names
Name:Timp3
Synonyms:Sun, Timp-3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. May form part of a tissue-specific acute response to remodeling stimuli.

Subunit structure

Interacts with EFEMP1 By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

Highest levels are found in kidney, lung and brain followed by ovary and uterus. Low levels are found in bone.

Induction

Highly induced by phorbol ester (PMA), EGF and transforming growth factor-beta 1. Also induced by dexamethasone.

Sequence similarities

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

Contains 1 NTR domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 211188Metalloproteinase inhibitor 3
PRO_0000034344

Regions

Domain24 – 143120NTR
Region24 – 285Involved in metalloproteinase-binding By similarity
Region88 – 892Involved in metalloproteinase-binding By similarity
Region105 – 18884Mediates interaction with EFEMP1 By similarity

Sites

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

Amino acid modifications

Disulfide bond24 ↔ 91 By similarity
Disulfide bond26 ↔ 118 By similarity
Disulfide bond36 ↔ 143 By similarity
Disulfide bond145 ↔ 192 By similarity
Disulfide bond150 ↔ 155 By similarity
Disulfide bond163 ↔ 184 By similarity

Experimental info

Sequence conflict311P → S in AAH14713. Ref.7
Sequence conflict531K → T in AAH14713. Ref.7
Sequence conflict1481K → N in AAH14713. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P39876 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 184EDF5B8D69B07B

FASTA21124,182
        10         20         30         40         50         60 
MTPWLGLVVL LSCWSLGHWG AEACTCSPSH PQDAFCNSDI VIRAKVVGKK LVKEGPFGTL 

        70         80         90        100        110        120 
VYTIKQMKMY RGFSKMPHVQ YIHTEASESL CGLKLEVNKY QYLLTGRVYE GKMYTGLCNF 

       130        140        150        160        170        180 
VERWDHLTLS QRKGLNYRYH LGCNCKIKSC YYLPCFVTSK NECLWTDMLS NFGYPGYQSK 

       190        200        210 
HYACIRQKGG YCSWYRGWAP PDKSISNATD P 

« Hide

References

« Hide 'large scale' references
[1]"Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues."
Leco K.J., Khokha R., Pavloff N., Hawkes S.P., Edwards D.R.
J. Biol. Chem. 269:9352-9360(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning of five messenger RNAs differentially expressed in preneoplastic or neoplastic JB6 mouse epidermal cells: one is homologous to human tissue inhibitor of metalloproteinases-3."
Sun Y., Hegamyer G., Colburn N.H.
Cancer Res. 54:1139-1144(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BALB/c.
Tissue: Lung and Skin.
[3]"Gene encoding a novel murine tissue inhibitor of metalloproteinases (TIMP), TIMP-3, is expressed in developing mouse epithelia, cartilage, and muscle, and is located on mouse chromosome 10."
Apte S.S., Hayashi K., Seldin M.F., Mattei M.-G., Hayashi M., Olsen B.R.
Dev. Dyn. 200:177-197(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[4]"Molecular cloning of mouse tissue inhibitor of metalloproteinases-3 and its promoter. Specific lack of expression in neoplastic JB6 cells may reflect altered gene methylation."
Sun Y., Hegamyer G., Kim H., Sithanandam K., Li H., Watts R., Colburn N.H.
J. Biol. Chem. 270:19312-19319(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family."
Apte S.S., Olsen B.R., Murphy G.
J. Biol. Chem. 270:14313-14318(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[6]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Spinal ganglion.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L27424 mRNA. Translation: AAA40447.1.
Z30970 mRNA. Translation: CAA83218.1.
L19622 mRNA. Translation: AAC37669.1.
U26437 expand/collapse EMBL AC list , U26433, U26434, U26435, U26436 Genomic DNA. Translation: AAA85860.1.
AK083905 mRNA. Translation: BAC39055.1.
BC014713 mRNA. Translation: AAH14713.1.
CCDSCCDS24097.1.
PIRA53532.
RefSeqNP_035725.1. NM_011595.2.
UniGeneMm.4871.

3D structure databases

ProteinModelPortalP39876.
SMRP39876. Positions 24-199.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSI35.003.

PTM databases

PhosphoSiteP39876.

Proteomic databases

MaxQBP39876.
PaxDbP39876.
PRIDEP39876.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020234; ENSMUSP00000020234; ENSMUSG00000020044.
GeneID21859.
KEGGmmu:21859.
UCSCuc007gnr.1. mouse.

Organism-specific databases

CTD7078.
MGIMGI:98754. Timp3.

Phylogenomic databases

eggNOGNOG250837.
HOGENOMHOG000285981.
HOVERGENHBG068749.
InParanoidP39876.
KOK16866.
OMAKEGYCSW.
OrthoDBEOG79GT74.
PhylomeDBP39876.
TreeFamTF317409.

Gene expression databases

ArrayExpressP39876.
BgeeP39876.
CleanExMM_TIMP3.
GenevestigatorP39876.

Family and domain databases

Gene3D3.90.370.10. 1 hit.
InterProIPR001134. Netrin_domain.
IPR001820. Prot_inh_TIMP.
IPR008993. TIMP-like_OB-fold.
IPR027465. TIMP_C_dom.
IPR015612. Tissue_inhib_metalloprotease_3.
[Graphical view]
PANTHERPTHR11844. PTHR11844. 1 hit.
PTHR11844:SF6. PTHR11844:SF6. 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...

Other

NextBio301360.
PROP39876.
SOURCESearch...

Entry information

Entry nameTIMP3_MOUSE
AccessionPrimary (citable) accession number: P39876
Secondary accession number(s): Q91WL9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 123 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot