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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3875482 [NCBI, ExPASy, EBI, Israel, Japan]
Matrisian L.M.,
Glaichenhaus N.,
Gesnel M.-C.,
Breathnach R.;
"Epidermal growth factor and oncogenes induce transcription of the same cellular mRNA in rat fibroblasts.";
EMBO J. 4:1435-1440(1985).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2431284 [NCBI, ExPASy, EBI, Israel, Japan]
Matrisian L.M.,
Gleroy P.,
Ruhlmann C.,
Gesnel M.-C.,
Breathnach R.;
"Isolation of the oncogene and epidermal growth factor-induced transin gene: complex control in rat fibroblasts.";
Mol. Cell. Biol. 6:1679-1686(1986).
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[3]
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PROTEIN SEQUENCE OF 19-28; 110-119; 309-315 AND 316-325.
PubMed=1963430 [NCBI, ExPASy, EBI, Israel, Japan]
Umenishi F.,
Yasumitsu H.,
Ashida Y.,
Yamauti J.,
Umeda M.,
Miyazaki K.;
"Purification and properties of extracellular matrix-degrading metallo-proteinase overproduced by Rous sarcoma virus-transformed rat liver cell line, and its identification as transin.";
J. Biochem. 108:537-543(1990).
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[4]
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MUTAGENESIS, AND CHARACTERIZATION.
PubMed=2841336 [NCBI, ExPASy, EBI, Israel, Japan]
Sanchez-Lopez R.,
Nicholson R.,
Gesnel M.-C.,
Matrisian L.M.,
Breathnach R.;
"Structure-function relationships in the collagenase family member transin.";
J. Biol. Chem. 263:11892-11899(1988).
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- FUNCTION: Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.
- CATALYTIC ACTIVITY: Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
- COFACTOR: Binds 4 calcium ions per subunit (By similarity).
- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (Probable).
- INDUCTION: By epidermal growth factor and is increased in FR3T3 and RAT-1 fibroblasts transformed by polyoma virus, Rous sarcoma virus, or the human cellular H-Ras oncogene.
- DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
- SIMILARITY: Belongs to the peptidase M10A family [view classification].
- SIMILARITY: Contains 4 hemopexin-like domains.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 475 AA [This is the length of the unprocessed precursor] |
Molecular weight: 53428 Da [This is the MW of the unprocessed precursor] |
CRC64: D81239DC3E26782E [This is a checksum on the sequence] |
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10 20 30 40 50 60
MKGLPVLLWL CTAVCSSYPL HGSEEDAGME VLQKYLENYY GLEKDVKQFT KKKDSSPVVK
70 80 90 100 110 120
KIQEMQKFLG LKMTGKLDSN TMELMHKPRC GVPDVGGFST FPGSPKWRKN HISYRIVNYT
130 140 150 160 170 180
LDLPRESVDS AIERALKVWE EVTPLTFSRI SEGEADIMIS FAVEEHGDFI PFDGPGMVLA
190 200 210 220 230 240
HAYAPGPGTN GDAHFDDDER WTDDVTGTNL FLVAAHELGH SLGLFHSANA EALMYPVYKS
250 260 270 280 290 300
STDLARFHLS QDDVDGIQSL YGPPTESPDV LVVPTKSNSL DPETLPMCSS ALSFDAVSTL
310 320 330 340 350 360
RGEVLFFKDR HFWRKSLRTP EPGFYLISSF WPSLPSNMDA AYEVTNRDTV FILKGNQIWA
370 380 390 400 410 420
IRGHEELAGY PKSIHTLGLP ETVQKIDAAI SLKDQKKTYF FVEDKFWRFD EKKQSMDPEF
430 440 450 460 470
PRKIAENFPG IGTKVDAVFE AFGFLYFFSG SSQLEFDPNA GKVTHILKSN SWFNC
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P03957 in FASTA format |
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ExPASy Home page
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