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O75900 (MMP23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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-23

Short name=MMP-23
EC=3.4.24.-
Alternative name(s):
Femalysin
MIFR-1
Matrix metalloproteinase-21
Short name=MMP-21
Matrix metalloproteinase-22
Short name=MMP-22

Cleaved into the following chain:

  1. Matrix metalloproteinase-23, soluble form
Gene names
Name:MMP23A
Synonyms:MMP21
AND
Name:MMP23B
Synonyms:MMP21, MMP22
OrganismHomo sapiens (Human) [Reference proteome]
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. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum By similarity.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by TIMP2 By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity. Membrane; Single-pass type II membrane protein. Note: A secreted form produced by proteolytic cleavage may also exist Probable. Ref.3

Tissue specificity

Predominantly expressed in ovary, testis and prostate. Ref.2

Domain

The ShKT domain associates with, and blocks several potassium channels in the nanomolar to low micromolar range. The relative affinity is Kv1.6 > Kv1.3 > Kv1.1 = Kv3.2 > Kv1.4 By similarity.

Post-translational modification

N-glycosylated. Ref.3

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.

Contains 1 ShKT domain.

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 – 4021Helical; Signal-anchor for type II membrane protein; Potential
Topological domain41 – 390350Lumenal Potential
Domain255 – 28935ShKT
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 bond255 ↔ 289 By similarity
Disulfide bond262 ↔ 282 By similarity
Disulfide bond271 ↔ 286 By similarity
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. Ref.1
Corresponds to variant rs1139033 [ dbSNP | Ensembl ].
VAR_028948

Experimental info

Mutagenesis781R → G: Abolishes processing of soluble form. Ref.3

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 »

FASTA43148,107
Isoform 3 (MMP21/22C) [UniParc].

Checksum: CD428F3F07F226EB
Show »

FASTA41546,305

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Pancreas.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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. No translation available.
BC025719 mRNA. Translation: AAH25719.1.
CCDSCCDS30559.1. [O75900-1]
RefSeqNP_008914.1. NM_006983.1. [O75900-1]
UniGeneHs.192316.
Hs.671760.

3D structure databases

ProteinModelPortalO75900.
SMRO75900. Positions 87-289.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114082. 1 interaction.
IntActO75900. 1 interaction.

Protein family/group databases

MEROPSM10.022.

PTM databases

PhosphoSiteO75900.

Proteomic databases

PaxDbO75900.
PRIDEO75900.

Protocols and materials databases

DNASU8510.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356026; ENSP00000348308; ENSG00000189409. [O75900-1]
GeneID8510.
KEGGhsa:8510.
UCSCuc001agp.3. human. [O75900-1]

Organism-specific databases

CTD8510.
GeneCardsGC01P001559.
GC01P001619.
H-InvDBHIX0178039.
HGNCHGNC:7170. MMP23A.
HGNC:7171. MMP23B.
HPACAB002768.
MIM603320. gene.
603321. gene.
neXtProtNX_O75900.
PharmGKBPA30880.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG245056.
HOVERGENHBG053177.
InParanoidO75900.
KOK08001.
OMAGFYPVNH.
OrthoDBEOG7KSX8P.
PhylomeDBO75900.
TreeFamTF315428.

Gene expression databases

BgeeO75900.
CleanExHS_MMP21.
GenevestigatorO75900.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR024079. MetalloPept_cat_dom.
IPR028687. MMP23.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR006026. Peptidase_Metallo.
IPR003582. ShKT_dom.
[Graphical view]
PANTHERPTHR10201:SF7. PTHR10201:SF7. 1 hit.
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.
PS51670. SHKT. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMMP23B.
GenomeRNAi8510.
NextBio31851.
PROO75900.
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: July 9, 2014
This is version 116 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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