Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O75900

- MMP23_HUMAN

UniProt

O75900 - MMP23_HUMAN

Protein

Matrix metalloproteinase-23

Gene

MMP23A

more
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (31 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    Cofactori

    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

    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

    GO - Cellular componenti

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

    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.
    GenevestigatoriO75900.

    Organism-specific databases

    HPAiCAB002768.

    Interactioni

    Protein-protein interaction databases

    BioGridi114082. 1 interaction.
    IntActiO75900. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliO75900.
    SMRiO75900. Positions 87-289.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini41 – 390350LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei20 – 4021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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.
    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

    MGRGARVPSE APGAGVERRW LGAALVALCL LPALVLLARL GAPAVPAWSA    50
    AQGDVAALGL SAVPPTRVPG PLAPRRRRYT LTPARLRWDH FNLTYRILSF 100
    PRNLLSPRET RRALAAAFRM WSDVSPFSFR EVAPEQPSDL RIGFYPINHT 150
    DCLVSALHHC FDGPTGELAH AFFPPHGGIH FDDSEYWVLG PTRYSWKKGV 200
    WLTDLVHVAA HEIGHALGLM HSQHGRALMH LNATLRGWKA LSQDELWGLH 250
    RLYGCLDRLF VCASWARRGF CDARRRLMKR LCPSSCDFCY EFPFPTVATT 300
    PPPPRTKTRL VPEGRNVTFR CGQKILHKKG KVYWYKDQEP LEFSYPGYLA 350
    LGEAHLSIIA NAVNEGTYTC VVRRQQRVLT TYSWRVRVRG 390
    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:
    EMBL
    GenBank
    DDBJ
    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]
    GeneIDi8510.
    KEGGihsa:8510.
    UCSCiuc001agp.3. human. [O75900-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 87-289.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

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

    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 ]
    GeneIDi 8510.
    KEGGi hsa:8510.
    UCSCi uc001agp.3. human. [O75900-1 ]

    Organism-specific databases

    CTDi 8510.
    GeneCardsi GC01P001559.
    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.
    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.
    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

    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: October 1, 2014
    This is version 117 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