|
|
|
|
|
|
[1]
|
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Monocytic leukemia;
DOI=10.1016/S0014-5793(99)01065-0; PubMed=10471807 [NCBI, ExPASy, EBI, Israel, Japan]
Kajita M.,
Kinoh H.,
Ito N.,
Takamura A.,
Itoh Y.,
Okada A.,
Sato H.,
Seiki M.;
"Human membrane type-4 matrix metalloproteinase (MT4-MMP) is encoded by a novel major transcript: isolation of complementary DNA clones for human and mouse mt4-mmp transcripts.";
FEBS Lett. 457:353-356(1999).
|
[2]
|
SEQUENCE REVISION TO 44; 47; 205-210; 224 AND 228.
Seiki M.;
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
|
[3]
|
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
TISSUE=Mammary carcinoma;
PubMed=8640782 [NCBI, ExPASy, EBI, Israel, Japan]
Puente X.S.,
Pendas A.M.,
Llano E.,
Velasco G.,
Lopez-Otin C.;
"Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma.";
Cancer Res. 56:944-949(1996).
|
[4]
|
NUCLEOTIDE SEQUENCE [MRNA] OF 129-302, AND CHARACTERIZATION.
DOI=10.1074/jbc.274.46.33043; PubMed=10551873 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Y.,
Johnson A.R.,
Ye Q.-Z.,
Dyer R.D.;
"Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain.";
J. Biol. Chem. 274:33043-33049(1999).
|
[5]
|
GPI-ANCHOR.
DOI=10.1074/jbc.274.48.34260; PubMed=10567400 [NCBI, ExPASy, EBI, Israel, Japan]
Itoh Y.,
Kajita M.,
Kinoh H.,
Mori H.,
Okada A.,
Seiki M.;
"Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase.";
J. Biol. Chem. 274:34260-34266(1999).
|
[6]
|
CHARACTERIZATION.
DOI=10.1515/BC.1999.137; PubMed=10543448 [NCBI, ExPASy, EBI, Israel, Japan]
Kolkenbrock H.,
Essers L.,
Ulbrich N.,
Will H.;
"Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase.";
Biol. Chem. 380:1103-1108(1999).
|
|
|
|
- FUNCTION: Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin.
- CATALYTIC ACTIVITY: Cleaves pro-TNF-alpha at the 74-Ala-|-Gln-75 site.
- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
- COFACTOR: Calcium (By similarity).
- SUBCELLULAR LOCATION: Isoform Long: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Secreted, extracellular space, extracellular matrix.
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
|
| Name | Short |
| Synonyms | Puente |
| Isoform ID | Q9ULZ9-2 |
| Features which should be applied to build the isoform sequence: VSP_005456. |
|
|
- TISSUE SPECIFICITY: Expressed in brain, leukocytes, colon, ovary testis and breast cancer. Expressed also in many transformed and non-transformed cell types.
- 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.
- PTM: The precursor is cleaved by a furin endopeptidase (By similarity).
- SIMILARITY: Belongs to the peptidase M10A family [view classification].
- SIMILARITY: Contains 4 hemopexin-like domains.
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Length: 606 AA [This is the length of the unprocessed precursor] |
Molecular weight: 67006 Da [This is the MW of the unprocessed precursor] |
CRC64: F5D51449118F4BF5 [This is a checksum on the sequence] |
|
10 20 30 40 50 60
MRRRAARGPG PPPPGPGLSR LPLLPLPLLL LLALGTRGGC AAPAPAPRAE DLSLGVEWLS
70 80 90 100 110 120
RFGYLPPADP TTGQLQTQEE LSKAITAMQQ FGGLEATGIL DEATLALMKT PRCSLPDLPV
130 140 150 160 170 180
LTQARRRRQA PAPTKWNKRN LSWRVRTFPR DSPLGHDTVR ALMYYALKVW SDIAPLNFHE
190 200 210 220 230 240
VAGSTADIQI DFSKADHNDG YPFDGPGGTV AHAFFPGHHH TAGDTHFDDD EAWTFRSSDA
250 260 270 280 290 300
HGMDLFAVAV HEFGHAIGLS HVAAAHSIMR PYYQGPVGDP LRYGLPYEDK VRVWQLYGVR
310 320 330 340 350 360
ESVSPTAQPE EPPLLPEPPD NRSSAPPRKD VPHRCSTHFD AVAQIRGEAF FFKGKYFWRL
370 380 390 400 410 420
TRDRHLVSLQ PAQMHRFWRG LPLHLDSVDA VYERTSDHKI VFFKGDRYWV FKDNNVEEGY
430 440 450 460 470 480
PRPVSDFSLP PGGIDAAFSW AHNDRTYFFK DQLYWRYDDH TRHMDPGYPA QSPLWRGVPS
490 500 510 520 530 540
TLDDAMRWSD GASYFFRGQE YWKVLDGELE VAPGYPQSTA RDWLVCGDSQ ADGSVAAGVD
550 560 570 580 590 600
AAEGPRAPPG QHDQSRSEDG YEVCSCTSGA SSPPGAPGPL VAATMLLLLP PLSPGALWTA
AQALTL
|
Q9ULZ9 in FASTA format |
|
ExPASy Home page
SIB Switzerland
