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Protein

Metalloproteinase inhibitor 3

Gene

Timp3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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. May form part of a tissue-specific acute response to remodeling stimuli.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi24 – 241Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partnerBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiI35.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Metalloproteinase inhibitor 3
Alternative name(s):
Tissue inhibitor of metalloproteinases 3
Short name:
TIMP-3
Gene namesi
Name:Timp3
Synonyms:Sun, Timp-3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:98754. Timp3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 211188Metalloproteinase inhibitor 3PRO_0000034344Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 91PROSITE-ProRule annotation
Disulfide bondi26 ↔ 118PROSITE-ProRule annotation
Disulfide bondi36 ↔ 143PROSITE-ProRule annotation
Disulfide bondi145 ↔ 192PROSITE-ProRule annotation
Disulfide bondi150 ↔ 155PROSITE-ProRule annotation
Disulfide bondi163 ↔ 184PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP39876.
PaxDbiP39876.
PRIDEiP39876.

PTM databases

PhosphoSiteiP39876.

Expressioni

Tissue specificityi

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

Inductioni

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

Gene expression databases

BgeeiP39876.
CleanExiMM_TIMP3.
ExpressionAtlasiP39876. baseline and differential.
GenevisibleiP39876. MM.

Interactioni

Subunit structurei

Interacts with EFEMP1.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020234.

Structurei

3D structure databases

ProteinModelPortaliP39876.
SMRiP39876. Positions 24-199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 143120NTRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 285Involved in metalloproteinase-bindingBy similarity
Regioni88 – 892Involved in metalloproteinase-bindingBy similarity
Regioni105 – 18884Mediates interaction with EFEMP1By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 NTR domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG250837.
GeneTreeiENSGT00390000004555.
HOGENOMiHOG000285981.
HOVERGENiHBG068749.
InParanoidiP39876.
KOiK16866.
OMAiKEGYCSW.
OrthoDBiEOG79GT74.
PhylomeDBiP39876.
TreeFamiTF317409.

Family and domain databases

Gene3Di3.90.370.10. 1 hit.
InterProiIPR001134. Netrin_domain.
IPR001820. TIMP.
IPR008993. TIMP-like_OB-fold.
IPR015612. TIMP3.
IPR027465. TIMP_C.
IPR030490. TIMP_CS.
[Graphical view]
PANTHERiPTHR11844. PTHR11844. 1 hit.
PTHR11844:SF6. PTHR11844:SF6. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P39876-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPWLGLVVL LSCWSLGHWG AEACTCSPSH PQDAFCNSDI VIRAKVVGKK
60 70 80 90 100
LVKEGPFGTL VYTIKQMKMY RGFSKMPHVQ YIHTEASESL CGLKLEVNKY
110 120 130 140 150
QYLLTGRVYE GKMYTGLCNF VERWDHLTLS QRKGLNYRYH LGCNCKIKSC
160 170 180 190 200
YYLPCFVTSK NECLWTDMLS NFGYPGYQSK HYACIRQKGG YCSWYRGWAP
210
PDKSISNATD P
Length:211
Mass (Da):24,182
Last modified:February 1, 1995 - v1
Checksum:i184EDF5B8D69B07B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311P → S in AAH14713 (PubMed:15489334).Curated
Sequence conflicti53 – 531K → T in AAH14713 (PubMed:15489334).Curated
Sequence conflicti148 – 1481K → N in AAH14713 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27424 mRNA. Translation: AAA40447.1.
Z30970 mRNA. Translation: CAA83218.1.
L19622 mRNA. Translation: AAC37669.1.
U26437
, U26433, U26434, U26435, U26436 Genomic DNA. Translation: AAA85860.1.
AK083905 mRNA. Translation: BAC39055.1.
BC014713 mRNA. Translation: AAH14713.1.
CCDSiCCDS24097.1.
PIRiA53532.
RefSeqiNP_035725.1. NM_011595.2.
UniGeneiMm.4871.

Genome annotation databases

EnsembliENSMUST00000020234; ENSMUSP00000020234; ENSMUSG00000020044.
GeneIDi21859.
KEGGimmu:21859.
UCSCiuc007gnr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27424 mRNA. Translation: AAA40447.1.
Z30970 mRNA. Translation: CAA83218.1.
L19622 mRNA. Translation: AAC37669.1.
U26437
, U26433, U26434, U26435, U26436 Genomic DNA. Translation: AAA85860.1.
AK083905 mRNA. Translation: BAC39055.1.
BC014713 mRNA. Translation: AAH14713.1.
CCDSiCCDS24097.1.
PIRiA53532.
RefSeqiNP_035725.1. NM_011595.2.
UniGeneiMm.4871.

3D structure databases

ProteinModelPortaliP39876.
SMRiP39876. Positions 24-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020234.

Protein family/group databases

MEROPSiI35.003.

PTM databases

PhosphoSiteiP39876.

Proteomic databases

MaxQBiP39876.
PaxDbiP39876.
PRIDEiP39876.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020234; ENSMUSP00000020234; ENSMUSG00000020044.
GeneIDi21859.
KEGGimmu:21859.
UCSCiuc007gnr.1. mouse.

Organism-specific databases

CTDi7078.
MGIiMGI:98754. Timp3.

Phylogenomic databases

eggNOGiNOG250837.
GeneTreeiENSGT00390000004555.
HOGENOMiHOG000285981.
HOVERGENiHBG068749.
InParanoidiP39876.
KOiK16866.
OMAiKEGYCSW.
OrthoDBiEOG79GT74.
PhylomeDBiP39876.
TreeFamiTF317409.

Miscellaneous databases

NextBioi301360.
PROiP39876.
SOURCEiSearch...

Gene expression databases

BgeeiP39876.
CleanExiMM_TIMP3.
ExpressionAtlasiP39876. baseline and differential.
GenevisibleiP39876. MM.

Family and domain databases

Gene3Di3.90.370.10. 1 hit.
InterProiIPR001134. Netrin_domain.
IPR001820. TIMP.
IPR008993. TIMP-like_OB-fold.
IPR015612. TIMP3.
IPR027465. TIMP_C.
IPR030490. TIMP_CS.
[Graphical view]
PANTHERiPTHR11844. PTHR11844. 1 hit.
PTHR11844:SF6. PTHR11844:SF6. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTIMP3_MOUSE
AccessioniPrimary (citable) accession number: P39876
Secondary accession number(s): Q91WL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 22, 2015
This is version 132 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.