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Matrix metalloproteinase-17 (MMP-17) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 4) (MT-MMP 4) (MTMMP4) (Membrane-type-4 matrix metalloproteinase) (MT4-MMP) (MT4MMP)

 MMP17_HUMAN             Reviewed;         603 AA.
Q9ULZ9; Q14850;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 4.
12-SEP-2018, entry version 179.
RecName: Full=Matrix metalloproteinase-17;
Short=MMP-17;
EC=3.4.24.-;
AltName: Full=Membrane-type matrix metalloproteinase 4;
Short=MT-MMP 4;
Short=MTMMP4;
AltName: Full=Membrane-type-4 matrix metalloproteinase;
Short=MT4-MMP;
Short=MT4MMP;
Flags: Precursor;
Name=MMP17; Synonyms=MT4MMP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Monocytic leukemia;
PubMed=10471807; DOI=10.1016/S0014-5793(99)01065-0;
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 41; 44; 202-207; 221 AND 225.
Seiki M.;
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
TISSUE=Mammary carcinoma;
PubMed=8640782;
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 [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 126-299, AND CHARACTERIZATION.
PubMed=10551873; DOI=10.1074/jbc.274.46.33043;
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).
[6]
GPI-ANCHOR.
PubMed=10567400; DOI=10.1074/jbc.274.48.34260;
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).
[7]
CHARACTERIZATION.
PubMed=10543448; DOI=10.1515/BC.1999.137;
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. Cleaves pro-TNF-alpha at the
'74-Ala-|-Gln-75' site. 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.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Isoform Long: Cell membrane; Lipid-anchor,
GPI-anchor; Extracellular side. Secreted, extracellular space,
extracellular matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q9ULZ9-1; Sequence=Displayed;
Name=Short; Synonyms=Puente;
IsoId=Q9ULZ9-2; 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.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB021225; BAA82707.2; -; mRNA.
EMBL; X89576; CAA61753.1; -; mRNA.
EMBL; AC131009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS31927.1; -. [Q9ULZ9-1]
RefSeq; NP_057239.4; NM_016155.5. [Q9ULZ9-1]
RefSeq; XP_011536657.1; XM_011538355.2. [Q9ULZ9-2]
RefSeq; XP_011536658.1; XM_011538356.2. [Q9ULZ9-2]
RefSeq; XP_011536659.1; XM_011538357.2. [Q9ULZ9-2]
UniGene; Hs.709245; -.
ProteinModelPortal; Q9ULZ9; -.
SMR; Q9ULZ9; -.
BioGrid; 110469; 1.
STRING; 9606.ENSP00000353767; -.
BindingDB; Q9ULZ9; -.
ChEMBL; CHEMBL2937; -.
DrugBank; DB00786; Marimastat.
GuidetoPHARMACOLOGY; 1641; -.
MEROPS; M10.017; -.
iPTMnet; Q9ULZ9; -.
PhosphoSitePlus; Q9ULZ9; -.
BioMuta; MMP17; -.
DMDM; 296439485; -.
PaxDb; Q9ULZ9; -.
PeptideAtlas; Q9ULZ9; -.
PRIDE; Q9ULZ9; -.
ProteomicsDB; 85161; -.
ProteomicsDB; 85162; -. [Q9ULZ9-2]
Ensembl; ENST00000360564; ENSP00000353767; ENSG00000198598. [Q9ULZ9-1]
Ensembl; ENST00000535291; ENSP00000441106; ENSG00000198598. [Q9ULZ9-2]
GeneID; 4326; -.
KEGG; hsa:4326; -.
UCSC; uc001ujc.2; human. [Q9ULZ9-1]
CTD; 4326; -.
DisGeNET; 4326; -.
EuPathDB; HostDB:ENSG00000198598.6; -.
GeneCards; MMP17; -.
H-InvDB; HIX0036662; -.
HGNC; HGNC:7163; MMP17.
MIM; 602285; gene.
neXtProt; NX_Q9ULZ9; -.
OpenTargets; ENSG00000198598; -.
PharmGKB; PA30875; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOVERGEN; HBG052484; -.
InParanoid; Q9ULZ9; -.
KO; K07997; -.
OMA; DRYWVFK; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; Q9ULZ9; -.
TreeFam; TF315428; -.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
GeneWiki; MMP17; -.
GenomeRNAi; 4326; -.
PRO; PR:Q9ULZ9; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000198598; Expressed in 102 organ(s), highest expression level in anterior cingulate cortex.
CleanEx; HS_MMP17; -.
ExpressionAtlas; Q9ULZ9; baseline and differential.
Genevisible; Q9ULZ9; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
GO; GO:0070006; F:metalloaminopeptidase activity; TAS:ParkinsonsUK-UCL.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:ProtInc.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO; GO:0042756; P:drinking behavior; IEA:Ensembl.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; TAS:ParkinsonsUK-UCL.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028726; MMP17.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
PANTHER; PTHR10201:SF21; PTHR10201:SF21; 1.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Extracellular matrix; Glycoprotein; GPI-anchor; Hydrolase;
Lipoprotein; Membrane; Metal-binding; Metalloprotease; Protease;
Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 35 {ECO:0000255}.
PROPEP 36 125 {ECO:0000250}.
/FTId=PRO_0000028818.
CHAIN 126 565 Matrix metalloproteinase-17.
/FTId=PRO_0000028819.
PROPEP 566 603 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000028820.
REPEAT 333 378 Hemopexin 1.
REPEAT 382 427 Hemopexin 2.
REPEAT 428 475 Hemopexin 3.
REPEAT 476 523 Hemopexin 4.
MOTIF 108 115 Cysteine switch. {ECO:0000250}.
COMPBIAS 122 125 Poly-Arg.
ACT_SITE 249 249 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 110 110 Zinc; in inhibited form. {ECO:0000250}.
METAL 248 248 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 252 252 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 258 258 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
LIPID 565 565 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 318 318 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 332 523 {ECO:0000250}.
VAR_SEQ 1 84 Missing (in isoform Short).
{ECO:0000303|PubMed:8640782}.
/FTId=VSP_005456.
CONFLICT 23 23 L -> LLPL (in Ref. 1; BAA82707 and 2;
CAA61753). {ECO:0000305}.
CONFLICT 182 182 A -> T (in Ref. 1; BAA82707 and 2;
CAA61753). {ECO:0000305}.
SEQUENCE 603 AA; 66653 MW; BB297B21973C7A0B CRC64;
MRRRAARGPG PPPPGPGLSR LPLPLLLLLA LGTRGGCAAP APAPRAEDLS LGVEWLSRFG
YLPPADPTTG QLQTQEELSK AITAMQQFGG LEATGILDEA TLALMKTPRC SLPDLPVLTQ
ARRRRQAPAP TKWNKRNLSW RVRTFPRDSP LGHDTVRALM YYALKVWSDI APLNFHEVAG
SAADIQIDFS KADHNDGYPF DGPGGTVAHA FFPGHHHTAG DTHFDDDEAW TFRSSDAHGM
DLFAVAVHEF GHAIGLSHVA AAHSIMRPYY QGPVGDPLRY GLPYEDKVRV WQLYGVRESV
SPTAQPEEPP LLPEPPDNRS SAPPRKDVPH RCSTHFDAVA QIRGEAFFFK GKYFWRLTRD
RHLVSLQPAQ MHRFWRGLPL HLDSVDAVYE RTSDHKIVFF KGDRYWVFKD NNVEEGYPRP
VSDFSLPPGG IDAAFSWAHN DRTYFFKDQL YWRYDDHTRH MDPGYPAQSP LWRGVPSTLD
DAMRWSDGAS YFFRGQEYWK VLDGELEVAP GYPQSTARDW LVCGDSQADG SVAAGVDAAE
GPRAPPGQHD QSRSEDGYEV CSCTSGASSP PGAPGPLVAA TMLLLLPPLS PGALWTAAQA
LTL


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Genprice Inc, Invoices and accounting
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