Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot O75900 (MMP23_HUMAN)

Last modified November 25, 2008. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Cytoplasmperinuclear 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 390390Matrix metalloproteinase-23
PRO_0000259513
Propeptide1 – 7878 Potential
PRO_0000259514
Chain79 – 390312Matrix metalloproteinase-23, soluble form
PRO_0000259515

Regions

Topological domain1 – 1919Cytoplasmic Potential
Transmembrane20 – 4021Signal-anchor for type II membrane protein Potential
Topological domain41 – 390350Extracellular Potential
Domain295 – 38086Ig-like C2-type

Sites

Active site2121 By similarity
Metal binding2111Zinc; catalytic By similarity
Metal binding2151Zinc; catalytic By similarity
Metal binding2211Zinc; catalytic By similarity
Site78 – 792Cleavage; by furin-like protease Potential

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1481N-linked (GlcNAc...) Potential
Glycosylation2321N-linked (GlcNAc...) Potential
Glycosylation3161N-linked (GlcNAc...) Potential
Disulfide bond321 ↔ 370 By similarity

Natural variations

Alternative sequence1991G → GDRPGSSWRPLLCSTVGCRG RALGQTAGGTFRGGGCHWSL AG in isoform 2.
VSP_021411
Alternative sequence2541G → GESLCRAGGRGPGGPEPGVL PTLPIG in isoform 3.
VSP_021412
Natural variant911F → L: dbSNP rs1139033.
VAR_028948

Experimental info

Mutagenesis781R → G: Abolishes processing of soluble form

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (MMP21/22A) [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: 5D78E4B4F2053D15

FASTA39043,935
        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 

« Hide

Isoform 2 (MMP21/22B) [UniParc].

Checksum: 807BA712BA201EF1
Show »

43148,107
Isoform 3 (MMP21/22C) [UniParc].

Checksum: CD428F3F07F226EB
Show »

41546,305

References

« Hide '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. expand/collapse author list , 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

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.
RefSeqNP_008914.1.
UniGeneHs.192316
Hs.671760

3D structure databases

HSSPHSSP built from PDB template 1HV5 based on UniProtKB Q02853.
ModBaseSearch...

Protein family/group databases

MEROPSM10.022.

PTM databases

PhosphoSiteO75900.

Genome annotation databases

EnsemblENSG00000189409. Homo sapiens. [Contig view]
GeneID8510.
KEGGhsa:8510.

Organism-specific databases

HGNCHGNC:7170. MMP23A.
HGNC:7171. MMP23B.
HPACAB002768.
MIM603320. gene.
603321. gene.
PharmGKBPA30879.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENO75900.

Gene expression databases

CleanExHS_MMP21.
GermOnlineENSG00000189409. Homo sapiens.

Family and domain databases

InterProIPR007110. Ig-like.
IPR003599. Ig_sub.
IPR001818. Pept_M10A_M12B.
IPR006025. Pept_M_Zn_BS.
IPR006026. Peptidase_M.
IPR003582. ShK_toxin.
[Graphical view]
PfamPF00413. Peptidase_M10. 1 hit.
PF01549. ShK. 1 hit.
[Graphical view]
PRINTSPR00138. MATRIXIN.
SMARTSM00409. IG. 1 hit.
SM00254. ShKT. 1 hit.
SM00235. ZnMc. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio31851.
SOURCESearch...

Entry information

Entry nameMMP23_HUMAN
AccessionPrimary (citable) accession number: O75900
Secondary accession number(s): A2AGN0 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents