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P39876

- TIMP3_MOUSE

UniProt

P39876 - TIMP3_MOUSE

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Protein

Metalloproteinase inhibitor 3

Gene

Timp3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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

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

GO - Biological processi

  1. cellular response to organic substance Source: MGI
  2. negative regulation of membrane protein ectodomain proteolysis Source: Ensembl
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: Chromosome 10

Organism-specific databases

MGIiMGI:98754. Timp3.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: MGI
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: Ensembl
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.
GenevestigatoriP39876.

Interactioni

Subunit structurei

Interacts with EFEMP1.By similarity

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

Family and domain databases

Gene3Di3.90.370.10. 1 hit.
InterProiIPR001134. Netrin_domain.
IPR001820. Prot_inh_TIMP.
IPR008993. TIMP-like_OB-fold.
IPR027465. TIMP_C_dom.
IPR015612. Tissue_inhib_metalloprotease_3.
[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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS24097.1.
PIRi A53532.
RefSeqi NP_035725.1. NM_011595.2.
UniGenei Mm.4871.

3D structure databases

ProteinModelPortali P39876.
SMRi P39876. Positions 24-199.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi I35.003.

PTM databases

PhosphoSitei P39876.

Proteomic databases

MaxQBi P39876.
PaxDbi P39876.
PRIDEi P39876.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020234 ; ENSMUSP00000020234 ; ENSMUSG00000020044 .
GeneIDi 21859.
KEGGi mmu:21859.
UCSCi uc007gnr.1. mouse.

Organism-specific databases

CTDi 7078.
MGIi MGI:98754. Timp3.

Phylogenomic databases

eggNOGi NOG250837.
HOGENOMi HOG000285981.
HOVERGENi HBG068749.
InParanoidi P39876.
KOi K16866.
OMAi KEGYCSW.
OrthoDBi EOG79GT74.
PhylomeDBi P39876.
TreeFami TF317409.

Miscellaneous databases

NextBioi 301360.
PROi P39876.
SOURCEi Search...

Gene expression databases

Bgeei P39876.
CleanExi MM_TIMP3.
ExpressionAtlasi P39876. baseline and differential.
Genevestigatori P39876.

Family and domain databases

Gene3Di 3.90.370.10. 1 hit.
InterProi IPR001134. Netrin_domain.
IPR001820. Prot_inh_TIMP.
IPR008993. TIMP-like_OB-fold.
IPR027465. TIMP_C_dom.
IPR015612. Tissue_inhib_metalloprotease_3.
[Graphical view ]
PANTHERi PTHR11844. PTHR11844. 1 hit.
PTHR11844:SF6. PTHR11844:SF6. 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

« 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: October 29, 2014
This is version 125 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