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Q9ULZ9 (MMP17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-17

Short name=MMP-17
EC=3.4.24.-
Alternative name(s):
Membrane-type matrix metalloproteinase 4
Short name=MT-MMP 4
Short name=MTMMP4
Membrane-type-4 matrix metalloproteinase
Short name=MT4-MMP
Short name=MT4MMP
Gene names
Name:MMP17
Synonyms:MT4MMP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Calcium By similarity.

Subcellular location

Isoform Long: Cell membrane; Lipid-anchorGPI-anchor; Extracellular side. Secretedextracellular spaceextracellular matrix Ref.6.

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.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q9ULZ9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: Q9ULZ9-2)

Also known as: Puente;

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Propeptide36 – 12590 By similarity
PRO_0000028818
Chain126 – 565440Matrix metalloproteinase-17
PRO_0000028819
Propeptide566 – 60338Removed in mature form Potential
PRO_0000028820

Regions

Repeat333 – 37846Hemopexin 1
Repeat382 – 42746Hemopexin 2
Repeat428 – 47548Hemopexin 3
Repeat476 – 52348Hemopexin 4
Motif108 – 1158Cysteine switch By similarity
Compositional bias122 – 1254Poly-Arg

Sites

Active site2491 By similarity
Metal binding1101Zinc; in inhibited form By similarity
Metal binding2481Zinc; catalytic By similarity
Metal binding2521Zinc; catalytic By similarity
Metal binding2581Zinc; catalytic By similarity

Amino acid modifications

Lipidation5651GPI-anchor amidated serine Potential
Glycosylation1371N-linked (GlcNAc...) Potential
Glycosylation3181N-linked (GlcNAc...) Potential
Disulfide bond332 ↔ 523 By similarity

Natural variations

Alternative sequence1 – 8484Missing in isoform Short.
VSP_005456

Experimental info

Sequence conflict231L → LLPL in BAA82707. Ref.1
Sequence conflict231L → LLPL in CAA61753. Ref.2
Sequence conflict1821A → T in BAA82707. Ref.1
Sequence conflict1821A → T in CAA61753. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified May 18, 2010. Version 4.
Checksum: BB297B21973C7A0B

FASTA60366,653
        10         20         30         40         50         60 
MRRRAARGPG PPPPGPGLSR LPLPLLLLLA LGTRGGCAAP APAPRAEDLS LGVEWLSRFG 

        70         80         90        100        110        120 
YLPPADPTTG QLQTQEELSK AITAMQQFGG LEATGILDEA TLALMKTPRC SLPDLPVLTQ 

       130        140        150        160        170        180 
ARRRRQAPAP TKWNKRNLSW RVRTFPRDSP LGHDTVRALM YYALKVWSDI APLNFHEVAG 

       190        200        210        220        230        240 
SAADIQIDFS KADHNDGYPF DGPGGTVAHA FFPGHHHTAG DTHFDDDEAW TFRSSDAHGM 

       250        260        270        280        290        300 
DLFAVAVHEF GHAIGLSHVA AAHSIMRPYY QGPVGDPLRY GLPYEDKVRV WQLYGVRESV 

       310        320        330        340        350        360 
SPTAQPEEPP LLPEPPDNRS SAPPRKDVPH RCSTHFDAVA QIRGEAFFFK GKYFWRLTRD 

       370        380        390        400        410        420 
RHLVSLQPAQ MHRFWRGLPL HLDSVDAVYE RTSDHKIVFF KGDRYWVFKD NNVEEGYPRP 

       430        440        450        460        470        480 
VSDFSLPPGG IDAAFSWAHN DRTYFFKDQL YWRYDDHTRH MDPGYPAQSP LWRGVPSTLD 

       490        500        510        520        530        540 
DAMRWSDGAS YFFRGQEYWK VLDGELEVAP GYPQSTARDW LVCGDSQADG SVAAGVDAAE 

       550        560        570        580        590        600 
GPRAPPGQHD QSRSEDGYEV CSCTSGASSP PGAPGPLVAA TMLLLLPPLS PGALWTAAQA 


LTL 

« Hide

Isoform Short (Puente) [UniParc].

Checksum: EB74B32E8A7619C3
Show »

FASTA51957,938

References

« Hide 'large scale' references
[1]"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."
Kajita M., Kinoh H., Ito N., Takamura A., Itoh Y., Okada A., Sato H., Seiki M.
FEBS Lett. 457:353-356(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: Monocytic leukemia.
[2]Seiki M.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 41; 44; 202-207; 221 AND 225.
[3]"Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma."
Puente X.S., Pendas A.M., Llano E., Velasco G., Lopez-Otin C.
Cancer Res. 56:944-949(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Tissue: Mammary carcinoma.
[4]"The finished DNA sequence of human chromosome 12."
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. expand/collapse author list , 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.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain."
Wang Y., Johnson A.R., Ye Q.-Z., Dyer R.D.
J. Biol. Chem. 274:33043-33049(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 126-299, CHARACTERIZATION.
[6]"Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase."
Itoh Y., Kajita M., Kinoh H., Mori H., Okada A., Seiki M.
J. Biol. Chem. 274:34260-34266(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR.
[7]"Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase."
Kolkenbrock H., Essers L., Ulbrich N., Will H.
Biol. Chem. 380:1103-1108(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB021225 mRNA. Translation: BAA82707.2.
X89576 mRNA. Translation: CAA61753.1.
AC131009 Genomic DNA. No translation available.
CCDSCCDS31927.1. [Q9ULZ9-1]
RefSeqNP_057239.4. NM_016155.4. [Q9ULZ9-1]
UniGeneHs.709245.

3D structure databases

ProteinModelPortalQ9ULZ9.
SMRQ9ULZ9. Positions 39-523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110469. 1 interaction.
STRING9606.ENSP00000353767.

Chemistry

ChEMBLCHEMBL2937.

Protein family/group databases

MEROPSM10.017.

PTM databases

PhosphoSiteQ9ULZ9.

Polymorphism databases

DMDM296439485.

Proteomic databases

PaxDbQ9ULZ9.
PRIDEQ9ULZ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360564; ENSP00000353767; ENSG00000198598. [Q9ULZ9-1]
ENST00000535291; ENSP00000441106; ENSG00000198598. [Q9ULZ9-2]
GeneID4326.
KEGGhsa:4326.
UCSCuc001ujc.1. human. [Q9ULZ9-1]

Organism-specific databases

CTD4326.
GeneCardsGC12P132312.
H-InvDBHIX0036662.
HGNCHGNC:7163. MMP17.
MIM602285. gene.
neXtProtNX_Q9ULZ9.
PharmGKBPA30875.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295915.
HOVERGENHBG052484.
InParanoidQ9ULZ9.
KOK07997.
OMAAHNDRTY.
OrthoDBEOG7XPZ57.
PhylomeDBQ9ULZ9.
TreeFamTF315428.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ9ULZ9.
BgeeQ9ULZ9.
CleanExHS_MMP17.
GenevestigatorQ9ULZ9.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR028726. MMP17.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERPTHR10201:SF118. PTHR10201:SF118. 1 hit.
PfamPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMMP17.
GenomeRNAi4326.
NextBio17023.
PROQ9ULZ9.
SOURCESearch...

Entry information

Entry nameMMP17_HUMAN
AccessionPrimary (citable) accession number: Q9ULZ9
Secondary accession number(s): Q14850
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 141 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM