P24347 (MMP11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Stromelysin-3
Short name=SL-3
Short name=ST3
EC=3.4.24.-

Alternative name(s):
Matrix metalloproteinase-11
Short name=MMP-11

Gene names

Name:	MMP11
Synonyms:	STMY3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play an important role in the progression of epithelial malignancies.
Cofactor	Binds 1 calcium ion per subunit By similarity. Binds 2 zinc ions per subunit By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix Probable.
Tissue specificity	Specifically expressed in stromal cells of breast carcinomas.
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-like domains.

Ontologies

Keywords
Biological process	Collagen degradation
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW extracellular matrix disassembly Traceable author statement. Source: Reactome multicellular organismal development Traceable author statement Ref.6. Source: ProtInc proteolysis Traceable author statement Ref.1. Source: ProtInc
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome proteinaceous extracellular matrix Traceable author statement Ref.1. Source: ProtInc
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro metalloendopeptidase activity Traceable author statement Ref.6. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Potential
	Propeptide	32 – 97	66	Activation peptide By similarity		PRO_0000028770
	Chain	98 – 488	391	Stromelysin-3		PRO_0000028771
Regions
	Domain	298 – 341	44	Hemopexin-like 1
	Domain	343 – 384	42	Hemopexin-like 2
	Domain	387 – 434	48	Hemopexin-like 3
	Domain	436 – 480	45	Hemopexin-like 4
	Motif	78 – 85	8	Cysteine switch By similarity
Sites
	Active site	216	1	By similarity
	Metal binding	80	1	Zinc 2; in inhibited form By similarity
	Metal binding	166	1	Zinc 1 By similarity
	Metal binding	171	1	Calcium By similarity
	Metal binding	172	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	174	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	176	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	179	1	Zinc 1 By similarity
	Metal binding	192	1	Zinc 1 By similarity
	Metal binding	215	1	Zinc 2; catalytic By similarity
	Metal binding	219	1	Zinc 2; catalytic By similarity
	Metal binding	225	1	Zinc 2; catalytic By similarity
Amino acid modifications
	Disulfide bond	294 ↔ 480		By similarity
Natural variations
	Natural variant	38	1	A → V. Ref.1 Ref.2 Corresponds to variant rs738792 [ dbSNP | Ensembl ].		VAR_022181
	Natural variant	44	1	E → K. Ref.2 Corresponds to variant rs28363646 [ dbSNP | Ensembl ].		VAR_022182
	Natural variant	61	1	P → L. Ref.2 Corresponds to variant rs28363647 [ dbSNP | Ensembl ].		VAR_022183
	Natural variant	86	1	S → P. Ref.2 Corresponds to variant rs28363648 [ dbSNP | Ensembl ].		VAR_022184
	Natural variant	166	1	D → N in a colorectal cancer sample; somatic mutation. Ref.7		VAR_036140
	Natural variant	182	1	F → S. Ref.4 Corresponds to variant rs17854940 [ dbSNP | Ensembl ].		VAR_029659

Sequences

	Sequence		Length	Mass (Da)
	P24347 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: F03C537EE76706A9	FASTA	488	54,590
	10 20 30 40 50 60 MAPAAWLRSA AARALLPPML LLLLQPPPLL ARALPPDAHH LHAERRGPQP WHAALPSSPA 70 80 90 100 110 120 PAPATQEAPR PASSLRPPRC GVPDPSDGLS ARNRQKRFVL SGGRWEKTDL TYRILRFPWQ 130 140 150 160 170 180 LVQEQVRQTM AEALKVWSDV TPLTFTEVHE GRADIMIDFA RYWHGDDLPF DGPGGILAHA 190 200 210 220 230 240 FFPKTHREGD VHFDYDETWT IGDDQGTDLL QVAAHEFGHV LGLQHTTAAK ALMSAFYTFR 250 260 270 280 290 300 YPLSLSPDDC RGVQHLYGQP WPTVTSRTPA LGPQAGIDTN EIAPLEPDAP PDACEASFDA 310 320 330 340 350 360 VSTIRGELFF FKAGFVWRLR GGQLQPGYPA LASRHWQGLP SPVDAAFEDA QGHIWFFQGA 370 380 390 400 410 420 QYWVYDGEKP VLGPAPLTEL GLVRFPVHAA LVWGPEKNKI YFFRGRDYWR FHPSTRRVDS 430 440 450 460 470 480 PVPRRATDWR GVPSEIDAAF QDADGYAYFL RGRLYWKFDP VKVKALEGFP RLVGPDFFGC AEPANTFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas." Basset P., Bellocq J.-P., Wolf C., Stoll I., Hutin P., Limacher J.-M., Podhajcer O.L., Chenard M.P., Rio M.C., Chambon P. Nature 348:699-704(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-38.
[2]	NIEHS SNPs program Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-38; LYS-44; LEU-61 AND PRO-86.
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-182. Tissue: Placenta.
[5]	"Structure and promoter characterization of the human stromelysin-3 gene." Anglard P., Melot T., Guerin E., Thomas G., Basset P. J. Biol. Chem. 270:20337-20344(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
[6]	"Furin-dependent intracellular activation of the human stromelysin-3 zymogen." Pei D., Weiss S.J. Nature 375:244-247(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 81-101.
[7]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-166.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	X57766 mRNA. Translation: CAA40918.1. AY899208 Genomic DNA. Translation: AAW65373.1. AP000349 Genomic DNA. No translation available. BC057788 mRNA. Translation: AAH57788.1. X84664 Genomic DNA. Translation: CAA59150.1.
IPI	IPI00306778.
PIR	S13423.
RefSeq	NP_005931.2. NM_005940.3.
UniGene	Hs.143751.
3D structure databases
ProteinModelPortal	P24347.
SMR	P24347. Positions 75-460.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000215743.
Protein family/group databases
MEROPS	M10.007.
PTM databases
PhosphoSite	P24347.
Polymorphism databases
DMDM	62906884.
Proteomic databases
PaxDb	P24347.
PRIDE	P24347.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000215743; ENSP00000215743; ENSG00000099953.
GeneID	4320.
KEGG	hsa:4320.
UCSC	uc002zxx.3. human.
Organism-specific databases
CTD	4320.
GeneCards	GC22P024110.
H-InvDB	HIX0203187.
HGNC	HGNC:7157. MMP11.
HPA	CAB002593.
MIM	185261. gene.
neXtProt	NX_P24347.
PharmGKB	PA30869.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG236137.
HOGENOM	HOG000217927.
HOVERGEN	HBG052484.
InParanoid	P24347.
KO	K07993.
OMA	VDTNEIA.
OrthoDB	EOG4CC41D.
PhylomeDB	P24347.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	P24347.
Bgee	P24347.
CleanEx	HS_MMP11.
Genevestigator	P24347.
GermOnline	ENSG00000099953. Homo sapiens.
Family and domain databases
Gene3D	2.110.10.10. 1 hit. 3.40.390.10. 1 hit.
InterPro	IPR000585. Hemopexin-like_dom. IPR018487. Hemopexin-like_repeat. IPR018486. Hemopexin_CS. IPR024079. MetalloPept_cat_dom. IPR001818. Pept_M10_metallopeptidase. IPR021190. Pept_M10A. IPR016293. Pept_M10A_Metazoans. IPR021158. Pept_M10A_Zn_BS. IPR006026. Peptidase_Metallo. [Graphical view]
Pfam	PF00045. Hemopexin. 4 hits. PF00413. Peptidase_M10. 1 hit. [Graphical view]
PIRSF	PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTS	PR00138. MATRIXIN.
SMART	SM00120. HX. 4 hits. SM00235. ZnMc. 1 hit. [Graphical view]
SUPFAM	SSF50923. Hemopexin. 1 hit.
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P24347.
ChEMBL	CHEMBL2867.
GenomeRNAi	4320.
NextBio	16997.
SOURCE	Search...

Entry information

Entry name

MMP11_HUMAN

Accession

Primary (citable) accession number: P24347
Secondary accession number(s): Q5FX24, Q6PEZ6, Q9UC26

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 137 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.