MMP23_HUMAN
ID MMP23_HUMAN Reviewed; 390 AA.
AC O75900; A2AGN0; A2AGN1; O75894; O75895; Q5QPQ8; Q76P96; Q7LDM6; Q7LDM7;
AC Q9UBR9; Q9UJK8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Matrix metalloproteinase-23;
DE Short=MMP-23;
DE EC=3.4.24.-;
DE AltName: Full=Femalysin;
DE AltName: Full=MIFR-1;
DE AltName: Full=Matrix metalloproteinase-21;
DE Short=MMP-21;
DE AltName: Full=Matrix metalloproteinase-22;
DE Short=MMP-22;
DE Contains:
DE RecName: Full=Matrix metalloproteinase-23, soluble form;
DE Flags: Precursor;
GN Name=MMP23B; Synonyms=MMP21, MMP22;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP LEU-91.
RX PubMed=9740677; DOI=10.1006/geno.1998.5401;
RA Gururajan R., Grenet J., Lahti J.M., Kidd V.J.;
RT "Isolation and characterization of two novel metalloproteinase genes linked
RT to the Cdc2L locus on human chromosome 1p36.3.";
RL Genomics 52:101-106(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=9988691; DOI=10.1074/jbc.274.8.4570;
RA Velasco G., Pendas A.M., Fueyo A., Knaueper V., Murphy G., Lopez-Otin C.;
RT "Cloning and characterization of human MMP-23, a new matrix
RT metalloproteinase predominantly expressed in reproductive tissues and
RT lacking conserved domains in other family members.";
RL J. Biol. Chem. 274:4570-4576(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), GLYCOSYLATION,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-78.
RC TISSUE=Uterus;
RX PubMed=11328856; DOI=10.1210/mend.15.5.0638;
RA Ohnishi J., Ohnishi E., Jin M., Hirano W., Nakane D., Matsui H., Kimura A.,
RA Sawa H., Nakayama K., Shibuya H., Nagashima K., Takahashi T.;
RT "Cloning and characterization of a rat ortholog of MMP-23 (matrix
RT metalloproteinase-23), a unique type of membrane-anchored matrix
RT metalloproteinase and conditioned switching of its expression during the
RT ovarian follicular development.";
RL Mol. Endocrinol. 15:747-764(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Protease. May regulate the surface expression of some
CC potassium channels by retaining them in the endoplasmic reticulum (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by TIMP2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}. Membrane
CC {ECO:0000269|PubMed:11328856}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:11328856}. Note=A secreted form produced by
CC proteolytic cleavage may also exist. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=MMP21/22A;
CC IsoId=O75900-1; Sequence=Displayed;
CC Name=2; Synonyms=MMP21/22B;
CC IsoId=O75900-2; Sequence=VSP_021411;
CC Name=3; Synonyms=MMP21/22C;
CC IsoId=O75900-3; Sequence=VSP_021412;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in ovary, testis and
CC prostate. {ECO:0000269|PubMed:9988691}.
CC -!- DOMAIN: The ShKT domain associates with, and blocks several potassium
CC channels in the nanomolar to low micromolar range. The relative
CC affinity is Kv1.6 > Kv1.3 > Kv1.1 = Kv3.2 > Kv1.4 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11328856}.
CC -!- PTM: Proteolytic cleavage might yield an active form. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF055334; AAC63527.1; -; Genomic_DNA.
DR EMBL; AF055334; AAC63528.1; -; Genomic_DNA.
DR EMBL; AF055334; AAC63529.1; -; Genomic_DNA.
DR EMBL; AF056200; AAC62616.1; -; mRNA.
DR EMBL; AF057061; AAC62617.1; -; mRNA.
DR EMBL; AF057062; AAC62618.1; -; mRNA.
DR EMBL; AJ005256; CAB38176.1; -; mRNA.
DR EMBL; AB031068; BAA92769.1; -; Genomic_DNA.
DR EMBL; AB010961; BAA24833.1; -; mRNA.
DR EMBL; AL691432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025719; AAH25719.1; -; mRNA.
DR CCDS; CCDS30559.1; -. [O75900-1]
DR RefSeq; NP_008914.1; NM_006983.1. [O75900-1]
DR AlphaFoldDB; O75900; -.
DR BMRB; O75900; -.
DR SMR; O75900; -.
DR BioGRID; 114082; 2.
DR IntAct; O75900; 1.
DR STRING; 9606.ENSP00000348308; -.
DR DrugBank; DB00786; Marimastat.
DR MEROPS; M10.022; -.
DR TCDB; 8.B.14.2.2; the sea anemone peptide toxin, class 1 (bgk) family.
DR GlyGen; O75900; 4 sites.
DR iPTMnet; O75900; -.
DR PhosphoSitePlus; O75900; -.
DR BioMuta; HGNC:7170; -.
DR CPTAC; CPTAC-2612; -.
DR jPOST; O75900; -.
DR MassIVE; O75900; -.
DR PaxDb; O75900; -.
DR PeptideAtlas; O75900; -.
DR PRIDE; O75900; -.
DR Antibodypedia; 3453; 373 antibodies from 32 providers.
DR DNASU; 8510; -.
DR Ensembl; ENST00000356026.10; ENSP00000348308.5; ENSG00000189409.14. [O75900-1]
DR GeneID; 8510; -.
DR KEGG; hsa:8510; -.
DR MANE-Select; ENST00000356026.10; ENSP00000348308.5; NM_006983.2; NP_008914.1.
DR UCSC; uc001agp.4; human. [O75900-1]
DR CTD; 8510; -.
DR DisGeNET; 8510; -.
DR GeneCards; MMP23B; -.
DR HGNC; HGNC:7171; MMP23B.
DR HPA; ENSG00000189409; Tissue enhanced (ovary).
DR MIM; 603320; gene.
DR MIM; 603321; gene.
DR neXtProt; NX_O75900; -.
DR OpenTargets; ENSG00000189409; -.
DR Orphanet; 1606; 1p36 deletion syndrome.
DR PharmGKB; PA30880; -.
DR VEuPathDB; HostDB:ENSG00000189409; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000161187; -.
DR HOGENOM; CLU_015489_2_1_1; -.
DR InParanoid; O75900; -.
DR OMA; HLHHCFD; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; O75900; -.
DR TreeFam; TF315428; -.
DR PathwayCommons; O75900; -.
DR SignaLink; O75900; -.
DR BioGRID-ORCS; 8510; 16 hits in 1062 CRISPR screens.
DR GeneWiki; MMP23B; -.
DR GenomeRNAi; 8510; -.
DR Pharos; O75900; Tbio.
DR PRO; PR:O75900; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75900; protein.
DR Bgee; ENSG00000189409; Expressed in apex of heart and 94 other tissues.
DR ExpressionAtlas; O75900; baseline and differential.
DR Genevisible; O75900; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0000003; P:reproduction; IEP:UniProtKB.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR028687; MMP23.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR10201:SF7; PTHR10201:SF7; 1.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01549; ShK; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00409; IG; 1.
DR SMART; SM00254; ShKT; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51670; SHKT; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Immunoglobulin domain;
KW Membrane; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT CHAIN 1..390
FT /note="Matrix metalloproteinase-23"
FT /id="PRO_0000259513"
FT PROPEP 1..78
FT /evidence="ECO:0000255"
FT /id="PRO_0000259514"
FT CHAIN 79..390
FT /note="Matrix metalloproteinase-23, soluble form"
FT /id="PRO_0000259515"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..390
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 255..289
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DOMAIN 295..380
FT /note="Ig-like C2-type"
FT ACT_SITE 212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 78..79
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 255..289
FT /evidence="ECO:0000250"
FT DISULFID 262..282
FT /evidence="ECO:0000250"
FT DISULFID 271..286
FT /evidence="ECO:0000250"
FT DISULFID 321..370
FT /evidence="ECO:0000250"
FT VAR_SEQ 199
FT /note="G -> GDRPGSSWRPLLCSTVGCRGRALGQTAGGTFRGGGCHWSLAG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:9740677"
FT /id="VSP_021411"
FT VAR_SEQ 254
FT /note="G -> GESLCRAGGRGPGGPEPGVLPTLPIG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9740677"
FT /id="VSP_021412"
FT VARIANT 91
FT /note="F -> L"
FT /evidence="ECO:0000269|PubMed:9740677"
FT /id="VAR_028948"
FT MUTAGEN 78
FT /note="R->G: Abolishes processing of soluble form."
FT /evidence="ECO:0000269|PubMed:11328856"
SQ SEQUENCE 390 AA; 43935 MW; 5D78E4B4F2053D15 CRC64;
MGRGARVPSE APGAGVERRW LGAALVALCL LPALVLLARL GAPAVPAWSA AQGDVAALGL
SAVPPTRVPG PLAPRRRRYT LTPARLRWDH FNLTYRILSF PRNLLSPRET RRALAAAFRM
WSDVSPFSFR EVAPEQPSDL RIGFYPINHT DCLVSALHHC FDGPTGELAH AFFPPHGGIH
FDDSEYWVLG PTRYSWKKGV WLTDLVHVAA HEIGHALGLM HSQHGRALMH LNATLRGWKA
LSQDELWGLH RLYGCLDRLF VCASWARRGF CDARRRLMKR LCPSSCDFCY EFPFPTVATT
PPPPRTKTRL VPEGRNVTFR CGQKILHKKG KVYWYKDQEP LEFSYPGYLA LGEAHLSIIA
NAVNEGTYTC VVRRQQRVLT TYSWRVRVRG
