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O75900

- MMP23_HUMAN

UniProt

O75900 - MMP23_HUMAN

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Protein

Matrix metalloproteinase-23

Gene

MMP23A

more
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity).By similarity

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Inhibited by TIMP2.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei78 – 792Cleavage; by furin-like proteaseSequence Analysis
Metal bindingi211 – 2111Zinc; catalyticPROSITE-ProRule annotation
Active sitei212 – 2121PROSITE-ProRule annotation
Metal bindingi215 – 2151Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi221 – 2211Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. metalloendopeptidase activity Source: UniProtKB
  2. metallopeptidase activity Source: UniProtKB
  3. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. proteolysis Source: UniProtKB
  2. reproduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.022.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-23 (EC:3.4.24.-)
Short name:
MMP-23
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:
Gene namesi
Name:MMP23A
Synonyms:MMP21
AND
Name:MMP23B
Synonyms:MMP21, MMP22
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:7170. MMP23A.
HGNC:7171. MMP23B.

Subcellular locationi

Endoplasmic reticulum membrane By similarity; Single-pass type II membrane protein By similarity. Membrane 1 Publication; Single-pass type II membrane protein 1 Publication
Note: A secreted form produced by proteolytic cleavage may also exist.Curated

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei20 – 4021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini41 – 390350LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. intracellular Source: UniProtKB
  4. proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi78 – 781R → G: Abolishes processing of soluble form. 1 Publication

Organism-specific databases

PharmGKBiPA30880.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Matrix metalloproteinase-23PRO_0000259513Add
BLAST
Propeptidei1 – 7878Sequence AnalysisPRO_0000259514Add
BLAST
Chaini79 – 390312Matrix metalloproteinase-23, soluble formPRO_0000259515Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi255 ↔ 289By similarity
Disulfide bondi262 ↔ 282By similarity
Disulfide bondi271 ↔ 286By similarity
Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi321 ↔ 370By similarity

Post-translational modificationi

N-glycosylated.1 Publication
Proteolytic cleavage might yield an active form.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiO75900.
PRIDEiO75900.

PTM databases

PhosphoSiteiO75900.

Expressioni

Tissue specificityi

Predominantly expressed in ovary, testis and prostate.1 Publication

Gene expression databases

BgeeiO75900.
CleanExiHS_MMP21.
ExpressionAtlasiO75900. baseline.
GenevestigatoriO75900.

Organism-specific databases

HPAiCAB002768.

Interactioni

Protein-protein interaction databases

BioGridi114082. 1 interaction.
IntActiO75900. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliO75900.
SMRiO75900. Positions 58-289, 307-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini255 – 28935ShKTPROSITE-ProRule annotationAdd
BLAST
Domaini295 – 38086Ig-like C2-typeAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 1 ShKT domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG245056.
GeneTreeiENSGT00760000119132.
HOVERGENiHBG053177.
InParanoidiO75900.
KOiK08001.
OMAiGFYPVNH.
OrthoDBiEOG7KSX8P.
PhylomeDBiO75900.
TreeFamiTF315428.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR007110. 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]
PANTHERiPTHR10201:SF7. PTHR10201:SF7. 1 hit.
PfamiPF00413. Peptidase_M10. 1 hit.
PF01549. ShK. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00409. IG. 1 hit.
SM00254. ShKT. 1 hit.
SM00235. ZnMc. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51670. SHKT. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75900-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGRGARVPSE APGAGVERRW LGAALVALCL LPALVLLARL GAPAVPAWSA
60 70 80 90 100
AQGDVAALGL SAVPPTRVPG PLAPRRRRYT LTPARLRWDH FNLTYRILSF
110 120 130 140 150
PRNLLSPRET RRALAAAFRM WSDVSPFSFR EVAPEQPSDL RIGFYPINHT
160 170 180 190 200
DCLVSALHHC FDGPTGELAH AFFPPHGGIH FDDSEYWVLG PTRYSWKKGV
210 220 230 240 250
WLTDLVHVAA HEIGHALGLM HSQHGRALMH LNATLRGWKA LSQDELWGLH
260 270 280 290 300
RLYGCLDRLF VCASWARRGF CDARRRLMKR LCPSSCDFCY EFPFPTVATT
310 320 330 340 350
PPPPRTKTRL VPEGRNVTFR CGQKILHKKG KVYWYKDQEP LEFSYPGYLA
360 370 380 390
LGEAHLSIIA NAVNEGTYTC VVRRQQRVLT TYSWRVRVRG
Length:390
Mass (Da):43,935
Last modified:October 31, 2006 - v2
Checksum:i5D78E4B4F2053D15
GO
Isoform 2 (identifier: O75900-2) [UniParc]FASTAAdd to Basket

Also known as: MMP21/22B

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

Show »
Length:431
Mass (Da):48,107
Checksum:i807BA712BA201EF1
GO
Isoform 3 (identifier: O75900-3) [UniParc]FASTAAdd to Basket

Also known as: MMP21/22C

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

Show »
Length:415
Mass (Da):46,305
Checksum:iCD428F3F07F226EB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti91 – 911F → L.1 Publication
Corresponds to variant rs1139033 [ dbSNP | Ensembl ].
VAR_028948

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei199 – 1991G → GDRPGSSWRPLLCSTVGCRG RALGQTAGGTFRGGGCHWSL AG in isoform 2. 1 PublicationVSP_021411
Alternative sequencei254 – 2541G → GESLCRAGGRGPGGPEPGVL PTLPIG in isoform 3. 1 PublicationVSP_021412

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30559.1. [O75900-1]
RefSeqiNP_008914.1. NM_006983.1. [O75900-1]
UniGeneiHs.192316.
Hs.671760.

Genome annotation databases

EnsembliENST00000356026; ENSP00000348308; ENSG00000189409. [O75900-1]
ENST00000412810; ENSP00000482367; ENSG00000189409. [O75900-1]
GeneIDi8510.
KEGGihsa:8510.
UCSCiuc001agp.3. human. [O75900-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS30559.1. [O75900-1 ]
RefSeqi NP_008914.1. NM_006983.1. [O75900-1 ]
UniGenei Hs.192316.
Hs.671760.

3D structure databases

ProteinModelPortali O75900.
SMRi O75900. Positions 58-289, 307-375.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114082. 1 interaction.
IntActi O75900. 1 interaction.

Chemistry

DrugBanki DB00786. Marimastat.

Protein family/group databases

MEROPSi M10.022.

PTM databases

PhosphoSitei O75900.

Proteomic databases

PaxDbi O75900.
PRIDEi O75900.

Protocols and materials databases

DNASUi 8510.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356026 ; ENSP00000348308 ; ENSG00000189409 . [O75900-1 ]
ENST00000412810 ; ENSP00000482367 ; ENSG00000189409 . [O75900-1 ]
GeneIDi 8510.
KEGGi hsa:8510.
UCSCi uc001agp.3. human. [O75900-1 ]

Organism-specific databases

CTDi 8510.
GeneCardsi GC01P001567.
GC01P001619.
H-InvDB HIX0178039.
HGNCi HGNC:7170. MMP23A.
HGNC:7171. MMP23B.
HPAi CAB002768.
MIMi 603320. gene.
603321. gene.
neXtProti NX_O75900.
PharmGKBi PA30880.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG245056.
GeneTreei ENSGT00760000119132.
HOVERGENi HBG053177.
InParanoidi O75900.
KOi K08001.
OMAi GFYPVNH.
OrthoDBi EOG7KSX8P.
PhylomeDBi O75900.
TreeFami TF315428.

Miscellaneous databases

GeneWikii MMP23B.
GenomeRNAii 8510.
NextBioi 31851.
PROi O75900.
SOURCEi Search...

Gene expression databases

Bgeei O75900.
CleanExi HS_MMP21.
ExpressionAtlasi O75900. baseline.
Genevestigatori O75900.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR007110. 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 ]
PANTHERi PTHR10201:SF7. PTHR10201:SF7. 1 hit.
Pfami PF00413. Peptidase_M10. 1 hit.
PF01549. ShK. 1 hit.
[Graphical view ]
PRINTSi PR00138. MATRIXIN.
SMARTi SM00409. IG. 1 hit.
SM00254. ShKT. 1 hit.
SM00235. ZnMc. 1 hit.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 1 hit.
PS51670. SHKT. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiMMP23_HUMAN
AccessioniPrimary (citable) accession number: O75900
Secondary accession number(s): A2AGN0
, A2AGN1, O75894, O75895, Q5QPQ8, Q76P96, Q7LDM6, Q7LDM7, Q9UBR9, Q9UJK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: November 26, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3