Human protein: IPI00019242 * 75807 Da * MMP15 Matrix metalloproteinase-15 - Liebel-Lab @ KIT
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>MMP15 Matrix metalloproteinase-15 - Length: 669 AS 
MGSDPSAPGRPGWTGSLLGDREEAARPRLLPLLLVLLGCLGLGVAAEDAEVHAENWLRLYGYLPQPSRHMSTMRSAQILA
SALAEMQRFYGIPVTGVLDEETKEWMKRPRCGVPDQFGVRVKANLRRRRKRYALTGRKWNNHHLTFSIQNYTEKLGWYHS
MEAVRRAFRVWEQATPLVFQEVPYEDIRLRRQKEADIMVLFASGFHGDSSPFDGTGGFLAHAYFPGPGLGGDTHFDADEP
WTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLRGIQQLYGTPDGQPQPTQPLPTVT
PRRPGRPDHRPPRPPQPPPPGGKPERPPKPGPPVQPRATERPDQYGPNICDGDFDTVAMLRGEMFVFKGRWFWRVRHNRV
LDNYPMPIGHFWRGLPGDISAAYERQDGRFVFFKGDRYWLFREANLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFF
FQEDRYWRFNEETQRGDPGYPKPISVWQGIPASPKGAFLSNDAAYTYFYKGTKYWKFDNERLRMEPGYPKSILRDFMGCQ
EHVEPGPRWPDVARPPFNPHGGAEPGADSAEGDVGDGDGDFGAGVNKDGGSRVVVQMEEVARTVNVVMVLVPLLLLLCVL
GLTYALVQMQRKGAPRVLLYCKRSLQEWV
Linkouts to other data resources: BioCompare * Entrez * PolyMeta * GeneCard * imaGenes * GenomeBrowser * Google Scholar * Mitocheck
AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
Diseaselink to OMIM


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
ACTIVATE: SMART analysis
NameBeginEndE-value
signal peptide145-
Pfam:PG_binding_1461101.00e-12
ZnMc1353052.03e-55
HX3744171.70e-08
HX4194631.78e-11
HX4665121.49e-13
HX5145591.02e-11
low complexity586604-
transmembrane624646-

These features and domains are not shown in the diagram, either because their scores are less significant than the required threshold, or because they overlap with some other source of annotation:

NameBeginEndE-valueReason
low complexity2147-overlap
low complexity118137-overlap
Pfam:Peptidase_M101383042.60e-95overlap
low complexity305357-overlap
Pfam:Hemopexin3744171.40e-13overlap
Pfam:Hemopexin4194631.30e-13overlap
Pfam:Hemopexin4665121.40e-17overlap
Pfam:Hemopexin5145592.40e-13overlap
low complexity624647-overlap


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
General information
Entry name MMP15_HUMAN
Accession number P51511, A0A2U6, Q14111
Integrated 01-OCT-1996, UniProtKB/Swiss-Prot.
Sequence update 01-OCT-1996, sequence version 1
Annotation update 25-NOV-2008, entry version 95
UniSave P51511, A0A2U6, Q14111
UniRef100 UniRef100_P51511
UniParc UPI000003DC75
Description and origin of the Protein
Description Recommended
Full=Matrix metalloproteinase-15;
Short=MMP-15;
EC=3.4.24.-;
Synonym
Full=Membrane-type matrix metalloproteinase 2;
Short=MT-MMP 2;
Short=MTMMP2;
Full=Membrane-type-2 matrix metalloproteinase;
Short=MT2-MMP;
Short=MT2MMP;
Full=SMCP-2;
Flags Precursor;
Gene name(s) MMP15
Organism source Homo sapiens (Human).
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
NCBI TaxID 9606
References
[1] Will,H., Hinzmann,B.,
cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment.
(1995) Eur. J. Biochem. 231:602-608
Position NUCLEOTIDE SEQUENCE [MRNA].
Comments TISSUE=Lung;
Medline 95377289
PubMed
7649159 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from WileyInterScience CiteXplore
[2] Livingston,R.J., Rieder,M.J., Shaffer,T., Bertucci,C., Baier,C.N., Rajkumar,N., Willa,H.T., Stanaway,I.B., Nguyen,C.P., Gildersleeve,H., Johnson,E.J., Swanson,J.E., McFarland,I., Park,C., Nickerson,D.A.,
NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).
Submitted SEP-2006 to the EMBL GenBank DDBJ databases
Position NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-200; LEU-350; GLY-596; ARG-609 AND TRP-622.
[3]
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
(2004) Genome Res. 14:2121-2127
Position NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Comments TISSUE=Brain;
DOI 10.1101/gr.2596504;
PubMed
15489334 Free after 6 monthsClick to get it from www.genome.org Free after 6 monthsClick to get it from www.genome.org FreeClick to get it from www.genome.org Subscription requiredClick to get it from DOI Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral CiteXplore
[4] Sato,H., Tanaka,M., Takino,T., Inoue,M., Seiki,M.,
Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15, and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively, by in situ hybridization.
(1997) Genomics 39:412-413
Position NUCLEOTIDE SEQUENCE [MRNA] OF 94-669, AND VARIANT ARG-609.
Medline 97224474
DOI 10.1006/geno.1996.4496;
PubMed
9119382 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from ScienceDirect CiteXplore
[5] Shofuda,K., Yasumitsu,H., Nishihashi,A., Miki,K., Miyazaki,K.,
Submitted MAY-1996 to the EMBL GenBank DDBJ databases
Position NUCLEOTIDE SEQUENCE [MRNA] OF 163-669.
Comments TISSUE=Placenta;
[6] d'Ortho,M.P., Will,H., Atkinson,S., Butler,G., Messent,A., Gavrilovic,J., Smith,B., Timpl,R., Zardi,L., Murphy,G.,
Membrane-type matrix metalloproteinases 1 and 2 exhibit broad- spectrum proteolytic capacities comparable to many matrix metalloproteinases.
(1997) Eur. J. Biochem. 250:751-757
Position FUNCTION.
Medline 98121196
PubMed
9461298 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from WileyInterScience CiteXplore
[7] Sjoeblom,T., Jones,S., Wood,L.D., Parsons,D.W., Lin,J., Barber,T.D., Mandelker,D., Leary,R.J., Ptak,J., Silliman,N., Szabo,S., Buckhaults,P., Farrell,C., Meeh,P., Markowitz,S.D., Willis,J., Dawson,D., Willson,J.K.V., Gazdar,A.F., Hartigan,J., Wu,L., Liu,C., Parmigiani,G., Park,B.H., Bachman,K.E., Papadopoulos,N., Vogelstein,B., Kinzler,K.W., Velculescu,V.E.,
The consensus coding sequences of human breast and colorectal cancers.
(2006) Science 314:268-274
Position VARIANT [LARGE SCALE ANALYSIS] GLY-596.
DOI 10.1126/science.1133427;
PubMed
16959974 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from www.sciencemag.org Subscription requiredClick to get it from www.sciencemag.org FreeClick to get it from www.sciencemag.org Subscription requiredClick to get it from www.sciencemag.org CiteXplore
Comments
FUNCTION Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A.
COFACTOR Binds 1 zinc ion per subunit (By similarity).
COFACTOR Calcium (By similarity).
INTERACTION
P04070:PROC NbExp=2 IntAct=EBI-1383043, EBI-1383018
SUBCELLULAR LOCATION Membrane; Single-pass type I membrane protein; Extracellular side (Potential).
TISSUE SPECIFICITY Appeared to be synthesized preferentially in liver, placenta, testis, colon and intestine. Substantial amounts are also detected in pancreas, kidney, lung, heart and skeletal muscle.
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.
SIMILARITY Contains 4 hemopexin-like domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms Distributed under the Creative Commons Attribution-NoDerivs License
Database cross-references
EMBL
Z48482; CAA88373.1; -; mRNA.
EF032329; ABJ53423.1; -; Genomic_DNA.
BC036495; AAH36495.1; -; mRNA.
BC055428; AAH55428.1; -; mRNA.
D86331; BAA13071.1; ALT_INIT; mRNA.
D85510; BAA22225.1; -; mRNA.
PIR
I38029; I38029.
RefSeq
NP_002419.1; -.
UniGene
Hs.80343; -.
HSSP
P50281; 1BQQ.
SMR
P51511; 134-304.
IntAct
P51511; -.
MEROPS
M10.015; -.
PhosphoSite
P51511; -.
Ensembl
ENSG00000102996; Homo sapiens.
GeneID
4324; -.
KEGG
hsa:4324; -.
NMPDR
fig|9606.3.peg.12328; -.
H-InvDB
HIX0013084; -.
HGNC
HGNC:7161; MMP15.
HPA
CAB002611; -.
MIM
602261; gene.
PharmGKB
PA30873; -.
HOGENOM
P51511; -.
HOVERGEN
P51511; -.
LinkHub
P51511; -.
NextBio
17013; -.
ArrayExpress
P51511; -.
CleanEx
HS_MMP15; -.
GermOnline
ENSG00000102996; Homo sapiens.
GO
GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
GO:0005578; C:proteinaceous extracellular matrix; IEA:InterPro.
GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
GO:0008047; F:enzyme activator activity; TAS:ProtInc.
GO:0004222; F:metalloendopeptidase activity; TAS:ProtInc.
GO:0005515; F:protein binding; IPI:IntAct.
GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO:0006464; P:protein modification process; TAS:ProtInc.
GO:0006508; P:proteolysis; IEA:InterPro.
InterPro
IPR000585; Hemopexin.
IPR001818; Pept_M10A_M12B.
IPR016293; Pept_M10A_matrix.
IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR002477; Peptidoglycan-bd-like.
Gene3D
G3DSA:2.110.10.10; Hemopexin; 1.
Pfam
PF00045; Hemopexin; 4.
PF00413; Peptidase_M10; 1.
PF01471; PG_binding_1; 1.
PIRSF
PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS
PR00138; MATRIXIN.
SMART
SM00120; HX; 4.
SM00235; ZnMc; 1.
PROSITE
PS00546; CYSTEINE_SWITCH; 1.
PS00024; HEMOPEXIN; 1.
PS00142; ZINC_PROTEASE; 1.
Protein Existence
1: Evidence at protein level;
Keywords
Calcium; Cleavage on pair of basic residues; Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; Polymorphism; Protease; Repeat; Signal; Transmembrane; Zinc; Zymogen;
SIGNAL: 1 41, Or 45 (Potential). PROPEP: 42 131, By similarity. /FTId=PRO_0000028808. CHAIN: 132 669, Matrix metalloproteinase-15. /FTId=PRO_0000028809. TOPO_DOM: 132 625, Extracellular (Potential). TOPO_DOM: 647 669, Cytoplasmic (Potential). TRANSMEM: 626 646, Potential. DOMAIN: 374 417, Hemopexin-like 1. DOMAIN: 419 463, Hemopexin-like 2. DOMAIN: 466 512, Hemopexin-like 3. DOMAIN: 514 559, Hemopexin-like 4. MOTIF: 109 116, Cysteine switch (By similarity). COMPBIAS: 331 340, Poly-Pro. ACT_SITE: 260 260, By similarity. METAL: 111 111, Zinc; in inhibited form (By similarity). METAL: 259 259, Zinc; catalytic (By similarity). METAL: 263 263, Zinc; catalytic (By similarity). METAL: 269 269, Zinc; catalytic (By similarity). CARBOHYD: 150 150, N-linked (GlcNAc...) (Potential). DISULFID: 370 559, By similarity. VARIANT: 200 200, L -> P. /FTId=VAR_030523. VARIANT: 350 350, P -> L. /FTId=VAR_030524. VARIANT: 596 596, D -> G. /FTId=VAR_030525. VARIANT: 609 609, G -> R (in dbSNP:rs3743563). /FTId=VAR_020055. VARIANT: 622 622, R -> W (in dbSNP:rs41434246). /FTId=VAR_030526. SIGNAL: 1 41, Or 45 (Potential). PROPEP: 42 131, By similarity. /FTId=PRO_0000028808. CHAIN: 132 669, Matrix metalloproteinase-15. /FTId=PRO_0000028809. TOPO_DOM: 132 625, Extracellular (Potential). TRANSMEM: 626 646, Potential. TOPO_DOM: 647 669, Cytoplasmic (Potential). DOMAIN: 374 417, Hemopexin-like 1. DOMAIN: 419 463, Hemopexin-like 2. DOMAIN: 466 512, Hemopexin-like 3. DOMAIN: 514 559, Hemopexin-like 4. MOTIF: 109 116, Cysteine switch (By similarity). COMPBIAS: 331 340, Poly-Pro. ACT_SITE: 260 260, By similarity. METAL: 111 111, Zinc; in inhibited form (By similarity). METAL: 259 259, Zinc; catalytic (By similarity). METAL: 263 263, Zinc; catalytic (By similarity). METAL: 269 269, Zinc; catalytic (By similarity). CARBOHYD: 150 150, N-linked (GlcNAc...) (Potential). DISULFID: 370 559, By similarity. VARIANT: 200 200, L -> P. /FTId=VAR_030523. VARIANT: 350 350, P -> L. /FTId=VAR_030524. VARIANT: 596 596, D -> G. /FTId=VAR_030525. VARIANT: 609 609, G -> R (in dbSNP:rs3743563). /FTId=VAR_020055. VARIANT: 622 622, R -> W (in dbSNP:rs41434246). /FTId=VAR_030526.
Key Begin End Length Description RESID
  SIGNAL 1 41 41 Or 45 (Potential).
  PROPEP 42 131 90 By similarity. /FTId=PRO_0000028808.
  CHAIN 132 669 538 Matrix metalloproteinase-15. /FTId=PRO_0000028809.
  TOPO_DOM 132 625 494 Extracellular (Potential).
  TRANSMEM 626 646 21 Potential.
  TOPO_DOM 647 669 23 Cytoplasmic (Potential).
  DOMAIN 374 417 44 Hemopexin-like 1.
  DOMAIN 419 463 45 Hemopexin-like 2.
  DOMAIN 466 512 47 Hemopexin-like 3.
  DOMAIN 514 559 46 Hemopexin-like 4.
  MOTIF 109 116 8 Cysteine switch (By similarity).
  COMPBIAS 331 340 10 Poly-Pro.
  ACT_SITE 260 260 1 By similarity. RESID:AA0006
  METAL 111 111 1 Zinc; in inhibited form (By similarity).
  METAL 259 259 1 Zinc; catalytic (By similarity).
  METAL 263 263 1 Zinc; catalytic (By similarity).
  METAL 269 269 1 Zinc; catalytic (By similarity).
  CARBOHYD 150 150 1 N-linked (GlcNAc...) (Potential). RESID:AA0151
  DISULFID 370 559 190 By similarity. RESID:AA0025
  VARIANT 200 200 1 L -> P. /FTId=VAR_030523.
  VARIANT 350 350 1 P -> L. /FTId=VAR_030524.
  VARIANT 596 596 1 D -> G. /FTId=VAR_030525.
  VARIANT 609 609 1 G -> R (in dbSNP:rs3743563). /FTId=VAR_020055.
  VARIANT 622 622 1 R -> W (in dbSNP:rs41434246). /FTId=VAR_030526.


IPI crosslinks:
SP P51511 IPI00019242 Q7KZY0; ENSP00000219271; REVIEWED:NP_002419; HIT000054125; AAH36495;AAH55428;ABJ53423;CAA88373; 7161,MMP15; 4324,MMP15; UPI000003DC75 Hs.80343; CCDS10792.1; GI:4505211; OTTHUMP00000081202;OTTHUMP00000164671;
IPI gene crosslinks:
16 56616783 56638303 1 16q13 ENSG00000102996 7161,MMP15 4324,MMP15 IPI00019242; P51511; Q7KZY0; ENSP00000219271; REVIEWED:NP_002419; HIT000054125; Hs.80343; CCDS10792.1; GI:4505211; OTTHUMG00000073402;OTTHUMG00000133466; OTTHUMP00000081202;OTTHUMP00000164671;