Q9H306 (MMP27_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Matrix metalloproteinase-27
Short name=MMP-27
EC=3.4.24.-

Gene names

Name:	MMP27
ORF Names:	UNQ2503/PRO5992

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

General annotation (Comments)

Function	Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens By similarity.
Cofactor	Binds 4 calcium ions per subunit By similarity. Binds 2 zinc ions per subunit By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Expressed in B-cells. Ref.4
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.
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	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro 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 – 17	17	Potential
	Propeptide	18 – 98	81	Activation peptide By similarity		PRO_0000287561
	Chain	99 – 513	415	Matrix metalloproteinase-27		PRO_0000287562
Regions
	Domain	285 – 327	43	Hemopexin-like 1
	Domain	329 – 371	43	Hemopexin-like 2
	Domain	376 – 423	48	Hemopexin-like 3
	Domain	425 – 465	41	Hemopexin-like 4
	Motif	89 – 96	8	Cysteine switch By similarity
Sites
	Active site	217	1	By similarity
	Metal binding	91	1	Zinc 2; in inhibited form By similarity
	Metal binding	121	1	Calcium 1 By similarity
	Metal binding	155	1	Calcium 2 By similarity
	Metal binding	165	1	Zinc 1 By similarity
	Metal binding	173	1	Calcium 3 By similarity
	Metal binding	174	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	178	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	181	1	Zinc 1 By similarity
	Metal binding	188	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	192	1	Calcium 2 By similarity
	Metal binding	194	1	Zinc 1 By similarity
	Metal binding	196	1	Calcium 3 By similarity
	Metal binding	199	1	Calcium 1 By similarity
	Metal binding	199	1	Calcium 3 By similarity
	Metal binding	216	1	Zinc 2; catalytic By similarity
	Metal binding	220	1	Zinc 2; catalytic By similarity
	Metal binding	226	1	Zinc 2; catalytic By similarity
	Metal binding	286	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	377	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	426	1	Calcium 4; via carbonyl oxygen By similarity
Amino acid modifications
	Glycosylation	110	1	N-linked (GlcNAc...) Potential
	Disulfide bond	279 ↔ 465		By similarity
Natural variations
	Natural variant	22	1	R → W. Corresponds to variant rs12099177 [ dbSNP | Ensembl ].		VAR_032326
	Natural variant	24	1	T → M. Ref.1 Corresponds to variant rs1939015 [ dbSNP | Ensembl ].		VAR_032327
	Natural variant	30	1	M → V. Ref.1 Corresponds to variant rs2846707 [ dbSNP | Ensembl ].		VAR_032328
	Natural variant	266	1	E → V. Ref.2 Corresponds to variant rs1276286 [ dbSNP | Ensembl ].		VAR_032329
	Natural variant	304	1	W → L. Corresponds to variant rs35616217 [ dbSNP | Ensembl ].		VAR_032330
	Natural variant	447	1	D → N. Ref.2 Corresponds to variant rs2509010 [ dbSNP | Ensembl ].		VAR_032331
	Natural variant	477	1	I → V. Corresponds to variant rs35822551 [ dbSNP | Ensembl ].		VAR_032332

Sequences

	Sequence		Length	Mass (Da)
	Q9H306 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 941D5B8DA55BD32A	FASTA	513	59,026
	10 20 30 40 50 60 MKRLLLLFLF FITFSSAFPL VRMTENEENM QLAQAYLNQF YSLEIEGNHL VQSKNRSLID 70 80 90 100 110 120 DKIREMQAFF GLTVTGKLDS NTLEIMKTPR CGVPDVGQYG YTLPGWRKYN LTYRIINYTP 130 140 150 160 170 180 DMARAAVDEA IQEGLEVWSK VTPLKFTKIS KGIADIMIAF RTRVHGRCPR YFDGPLGVLG 190 200 210 220 230 240 HAFPPGPGLG GDTHFDEDEN WTKDGAGFNL FLVAAHEFGH ALGLSHSNDQ TALMFPNYVS 250 260 270 280 290 300 LDPRKYPLSQ DDINGIQSIY GGLPKEPAKP KEPTIPHACD PDLTFDAITT FRREVMFFKG 310 320 330 340 350 360 RHLWRIYYDI TDVEFELIAS FWPSLPADLQ AAYENPRDKI LVFKDENFWM IRGYAVLPDY 370 380 390 400 410 420 PKSIHTLGFP GRVKKIDAAV CDKTTRKTYF FVGIWCWRFD EMTQTMDKGF PQRVVKHFPG 430 440 450 460 470 480 ISIRVDAAFQ YKGFFFFSRG SKQFEYDIKT KNITRIMRTN TWFQCKEPKN SSFGFDINKE 490 500 510 KAHSGGIKIL YHKSLSLFIF GIVHLLKNTS IYQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a novel matrix metalloproteinase homologous to stromelysins." Benoit de Coignac A., Elson G., Magistrelli G., Jeannin P., Delneste Y., Aubry J.-P., Berthier O., Bonnefoy J.-Y., Gauchat J.-F. Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MET-24 AND VAL-30.
[2]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-266 AND ASN-447.
[3]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis." Bar-Or A., Nuttall R.K., Duddy M., Alter A., Kim H.J., Ifergan I., Pennington C.J., Bourgoin P., Edwards D.R., Yong V.W. Brain 126:2738-2749(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF195192 mRNA. Translation: AAG28453.1. AY358752 mRNA. Translation: AAQ89112.1. AP000647 Genomic DNA. No translation available. AP000851 Genomic DNA. No translation available.
IPI	IPI00005471.
RefSeq	NP_071405.2. NM_022122.2.
UniGene	Hs.534479.
3D structure databases
HSSP	HSSP built from PDB template 1Q3A based on UniProtKB P09238.
ProteinModelPortal	Q9H306.
SMR	Q9H306. Positions 30-465.
ModBase	Search...
Protein family/group databases
MEROPS	M10.027.
PTM databases
PhosphoSite	Q9H306.
Polymorphism databases
DMDM	296437372.
Proteomic databases
PaxDb	Q9H306.
PRIDE	Q9H306.
Protocols and materials databases
DNASU	64066.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000260229; ENSP00000260229; ENSG00000137675.
GeneID	64066.
KEGG	hsa:64066.
UCSC	uc001phd.1. human.
Organism-specific databases
CTD	64066.
GeneCards	GC11M102596.
H-InvDB	HIX0201706.
HGNC	HGNC:14250. MMP27.
neXtProt	NX_Q9H306.
PharmGKB	PA30884.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG260291.
HOGENOM	HOG000217927.
HOVERGEN	HBG052484.
InParanoid	Q9H306.
KO	K08005.
OMA	HACDPDL.
OrthoDB	EOG42BX8B.
PhylomeDB	Q9H306.
Gene expression databases
Bgee	Q9H306.
CleanEx	HS_MMP27.
Genevestigator	Q9H306.
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. IPR002477. Peptidoglycan-bd-like. [Graphical view]
Pfam	PF00045. Hemopexin. 3 hits. PF00413. Peptidase_M10. 1 hit. PF01471. PG_binding_1. 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. SSF47090. PGBD_like. 1 hit.
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	64066.
NextBio	65838.

Entry information

Entry name

MMP27_HUMAN

Accession

Primary (citable) accession number: Q9H306
Secondary accession number(s): Q6UWK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 93 of the entry and version 2 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.