Reviewed, UniProtKB/Swiss-Prot O75900 (MMP23_HUMAN)

Names and origin

Protein names

Recommended name:
    Matrix metalloproteinase-23
      Short name=MMP-23
    EC=3.4.24.-
Alternative name(s):
    Matrix metallopeptidase 21
      Short name=MMP-21
    Matrix metalloprotease 22
      Short name=MMP-22
    Femalysin
    MIFR-1
Cleaved into the following chain:
    1- Recommended name:
            Matrix metalloproteinase-23, soluble form

Gene names

Name:	MMP23A
Synonyms:	MMP21
AND
Name:	MMP23B
Synonyms:	MMP21, MMP22

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	390 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	Protease.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Enzyme regulation	Inhibited by TIMP2 By similarity.
Subcellular location	Membrane; Single-pass type II membrane protein. Cytoplasm › perinuclear region. Note= A secreted form produced by proteolytic cleavage seems also to exist Probable.
Tissue specificity	Predominantly expressed in ovary, testis and prostate.
Post-translational modification	N-glycosylated. Proteolytic cleavage might yield an active form By similarity.
Sequence similarities	Belongs to the peptidase M10A family. Contains 1 Ig-like C2-type (immunoglobulin-like) domain.
Sequence caution	The sequence CAM12836.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Signal-anchor Transmembrane
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	proteolysis Ref.2 Inferred from direct assay. Source: UniProtKB reproduction Ref.2 Inferred from expression pattern. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW proteinaceous extracellular matrix Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	metalloendopeptidase activity Ref.1 Ref.2 Inferred from direct assay. Source: UniProtKB zinc ion binding Ref.2 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75900-1)

Also known as: MMP21/22A;

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 2 (identifier: O75900-2)

Also known as: MMP21/22B;

The sequence of this isoform differs from the canonical sequence as follows:
     199-199: G → GDRPGSSWRPLLCSTVGCRGRALGQTAGGTFRGGGCHWSLAG

Isoform 3 (identifier: O75900-3)

Also known as: MMP21/22C;

The sequence of this isoform differs from the canonical sequence as follows:
     254-254: G → GESLCRAGGRGPGGPEPGVLPTLPIG

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 390	390	Matrix metalloproteinase-23		PRO_0000259513
	Propeptide	1 – 78	78	Potential		PRO_0000259514
	Chain	79 – 390	312	Matrix metalloproteinase-23, soluble form		PRO_0000259515
Regions
	Topological domain	1 – 19	19	Cytoplasmic Potential
	Transmembrane	20 – 40	21	Signal-anchor for type II membrane protein Potential
	Topological domain	41 – 390	350	Extracellular Potential
	Domain	295 – 380	86	Ig-like C2-type
Sites
	Active site	212	1	By similarity
	Metal binding	211	1	Zinc; catalytic By similarity
	Metal binding	215	1	Zinc; catalytic By similarity
	Metal binding	221	1	Zinc; catalytic By similarity
	Site	78 – 79	2	Cleavage; by furin-like protease Potential
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	148	1	N-linked (GlcNAc...) Potential
	Glycosylation	232	1	N-linked (GlcNAc...) Potential
	Glycosylation	316	1	N-linked (GlcNAc...) Potential
	Disulfide bond	321 ↔ 370		By similarity
Natural variations
	Alternative sequence	199	1	G → GDRPGSSWRPLLCSTVGCRG RALGQTAGGTFRGGGCHWSL AG in isoform 2.		VSP_021411
	Alternative sequence	254	1	G → GESLCRAGGRGPGGPEPGVL PTLPIG in isoform 3.		VSP_021412
	Natural variant	91	1	F → L: dbSNP rs1139033.		VAR_028948
Experimental info
	Mutagenesis	78	1	R → G: Abolishes processing of soluble form

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (MMP21/22A) [UniParc]. Last modified October 31, 2006. Version 2. Checksum: 5D78E4B4F2053D15	FASTA	390	43,935
	10 20 30 40 50 60 MGRGARVPSE APGAGVERRW LGAALVALCL LPALVLLARL GAPAVPAWSA AQGDVAALGL 70 80 90 100 110 120 SAVPPTRVPG PLAPRRRRYT LTPARLRWDH FNLTYRILSF PRNLLSPRET RRALAAAFRM 130 140 150 160 170 180 WSDVSPFSFR EVAPEQPSDL RIGFYPINHT DCLVSALHHC FDGPTGELAH AFFPPHGGIH 190 200 210 220 230 240 FDDSEYWVLG PTRYSWKKGV WLTDLVHVAA HEIGHALGLM HSQHGRALMH LNATLRGWKA 250 260 270 280 290 300 LSQDELWGLH RLYGCLDRLF VCASWARRGF CDARRRLMKR LCPSSCDFCY EFPFPTVATT 310 320 330 340 350 360 PPPPRTKTRL VPEGRNVTFR CGQKILHKKG KVYWYKDQEP LEFSYPGYLA LGEAHLSIIA 370 380 390 NAVNEGTYTC VVRRQQRVLT TYSWRVRVRG
	Isoform 2 (MMP21/22B) [UniParc]. Checksum: 807BA712BA201EF1		431	48,107
	10 20 30 40 50 60 MGRGARVPSE APGAGVERRW LGAALVALCL LPALVLLARL GAPAVPAWSA AQGDVAALGL 70 80 90 100 110 120 SAVPPTRVPG PLAPRRRRYT LTPARLRWDH FNLTYRILSF PRNLLSPRET RRALAAAFRM 130 140 150 160 170 180 WSDVSPFSFR EVAPEQPSDL RIGFYPINHT DCLVSALHHC FDGPTGELAH AFFPPHGGIH 190 200 210 220 230 240 FDDSEYWVLG PTRYSWKKGD RPGSSWRPLL CSTVGCRGRA LGQTAGGTFR GGGCHWSLAG 250 260 270 280 290 300 VWLTDLVHVA AHEIGHALGL MHSQHGRALM HLNATLRGWK ALSQDELWGL HRLYGCLDRL 310 320 330 340 350 360 FVCASWARRG FCDARRRLMK RLCPSSCDFC YEFPFPTVAT TPPPPRTKTR LVPEGRNVTF 370 380 390 400 410 420 RCGQKILHKK GKVYWYKDQE PLEFSYPGYL ALGEAHLSII ANAVNEGTYT CVVRRQQRVL 430 TTYSWRVRVR G
	Isoform 3 (MMP21/22C) [UniParc]. Checksum: CD428F3F07F226EB		415	46,305
	10 20 30 40 50 60 MGRGARVPSE APGAGVERRW LGAALVALCL LPALVLLARL GAPAVPAWSA AQGDVAALGL 70 80 90 100 110 120 SAVPPTRVPG PLAPRRRRYT LTPARLRWDH FNLTYRILSF PRNLLSPRET RRALAAAFRM 130 140 150 160 170 180 WSDVSPFSFR EVAPEQPSDL RIGFYPINHT DCLVSALHHC FDGPTGELAH AFFPPHGGIH 190 200 210 220 230 240 FDDSEYWVLG PTRYSWKKGV WLTDLVHVAA HEIGHALGLM HSQHGRALMH LNATLRGWKA 250 260 270 280 290 300 LSQDELWGLH RLYGESLCRA GGRGPGGPEP GVLPTLPIGC LDRLFVCASW ARRGFCDARR 310 320 330 340 350 360 RLMKRLCPSS CDFCYEFPFP TVATTPPPPR TKTRLVPEGR NVTFRCGQKI LHKKGKVYWY 370 380 390 400 410 KDQEPLEFSY PGYLALGEAH LSIIANAVNE GTYTCVVRRQ QRVLTTYSWR VRVRG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of two novel metalloproteinase genes linked to the Cdc2L locus on human chromosome 1p36.3." Gururajan R., Grenet J., Lahti J.M., Kidd V.J. Genomics 52:101-106(1998) [PubMed: 9740677] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), VARIANT LEU-91.
[2]	"Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members." Velasco G., Pendas A.M., Fueyo A., Knaueper V., Murphy G., Lopez-Otin C. J. Biol. Chem. 274:4570-4576(1999) [PubMed: 9988691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Ovary.
[3]	"Cloning and characterization of a rat ortholog of MMP-23 (matrix metalloproteinase-23), a unique type of membrane-anchored matrix metalloproteinase and conditioned switching of its expression during the ovarian follicular development." Ohnishi J., Ohnishi E., Jin M., Hirano W., Nakane D., Matsui H., Kimura A., Sawa H., Nakayama K., Shibuya H., Nagashima K., Takahashi T. Mol. Endocrinol. 15:747-764(2001) [PubMed: 11328856] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), GLYCOSYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-78. Tissue: Uterus.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Pancreas.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF055334 Genomic DNA. Translation: AAC63527.1. AF055334 Genomic DNA. Translation: AAC63528.1. AF055334 Genomic DNA. Translation: AAC63529.1. AF056200 mRNA. Translation: AAC62616.1. AF057061 mRNA. Translation: AAC62617.1. AF057062 mRNA. Translation: AAC62618.1. AJ005256 mRNA. Translation: CAB38176.1. AB031068 Genomic DNA. Translation: BAA92769.1. AB010961 mRNA. Translation: BAA24833.1. AL691432 Genomic DNA. Translation: CAM12835.1. AL691432 Genomic DNA. Translation: CAM12836.1. Sequence problems. BC025719 mRNA. Translation: AAH25719.1.
RefSeq	NP_008914.1.
UniGene	Hs.192316 Hs.671760
3D structure databases
HSSP	HSSP built from PDB template 1HV5 based on UniProtKB Q02853.
ModBase	Search...
Protein family/group databases
MEROPS	M10.022.
PTM databases
PhosphoSite	O75900.
Genome annotation databases
Ensembl	ENSG00000189409. Homo sapiens. [Contig view]
GeneID	8510.
KEGG	hsa:8510.
Organism-specific databases
HGNC	HGNC:7170. MMP23A. HGNC:7171. MMP23B.
HPA	CAB002768.
MIM	603320. gene. 603321. gene.
PharmGKB	PA30879.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOVERGEN	O75900.
Gene expression databases
CleanEx	HS_MMP21.
GermOnline	ENSG00000189409. Homo sapiens.
Family and domain databases
InterPro	IPR007110. Ig-like. IPR003599. Ig_sub. IPR001818. Pept_M10A_M12B. IPR006025. Pept_M_Zn_BS. IPR006026. Peptidase_M. IPR003582. ShK_toxin. [Graphical view]
Pfam	PF00413. Peptidase_M10. 1 hit. PF01549. ShK. 1 hit. [Graphical view]
PRINTS	PR00138. MATRIXIN.
SMART	SM00409. IG. 1 hit. SM00254. ShKT. 1 hit. SM00235. ZnMc. 1 hit. [Graphical view]
PROSITE	PS50835. IG_LIKE. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	31851.
SOURCE	Search...

Entry information

Entry name

MMP23_HUMAN

Accession

Primary (citable) accession number: O75900
Secondary accession number(s): A2AGN0 , A2AGN1, O75894, O75895, Q5QPQ8, Q76P96, Q7LDM6, Q7LDM7, Q9UBR9, Q9UJK8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	November 25, 2008
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)