MMP23_RAT
ID MMP23_RAT Reviewed; 391 AA.
AC O88272;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Matrix metalloproteinase-23;
DE Short=MMP-23;
DE EC=3.4.24.-;
DE AltName: Full=metalloprotease in the female reproductive tract;
DE Short=MIFR;
DE Contains:
DE RecName: Full=Matrix metalloproteinase-23, soluble form;
DE Flags: Precursor;
GN Name=Mmp23; Synonyms=Mifr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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).
RN [3]
RP STRUCTURE BY NMR OF 254-290, FUNCTION, SUBCELLULAR LOCATION, TOXIN-LIKE
RP DOMAIN, AND DISULFIDE BONDS.
RX PubMed=19965868; DOI=10.1074/jbc.m109.071266;
RA Rangaraju S., Khoo K.K., Feng Z.P., Crossley G., Nugent D., Khaytin I.,
RA Chi V., Pham C., Calabresi P., Pennington M.W., Norton R.S., Chandy K.G.;
RT "Potassium channel modulation by a toxin domain in matrix metalloprotease
RT 23.";
RL J. Biol. Chem. 285:9124-9136(2010).
CC -!- FUNCTION: Protease. May regulate the surface expression of some
CC potassium channels by retaining them in the endoplasmic reticulum.
CC {ECO:0000269|PubMed:19965868}.
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: Membrane; Single-pass type II membrane protein.
CC Endoplasmic reticulum membrane; Single-pass type II membrane protein.
CC Note=A secreted form produced by proteolytic cleavage may also exist.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at the highest levels in ovary and
CC uterus. In ovary expression is strictly confined to granulosa cells of
CC preantral and small antral follicles. Detected also in testis and
CC prostate. {ECO:0000269|PubMed:11328856}.
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.
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}.
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DR EMBL; AB010960; BAA24832.1; -; mRNA.
DR EMBL; BC086586; AAH86586.1; -; mRNA.
DR RefSeq; NP_446058.1; NM_053606.2.
DR PDB; 2K72; NMR; -; A=254-290.
DR PDBsum; 2K72; -.
DR AlphaFoldDB; O88272; -.
DR BMRB; O88272; -.
DR SMR; O88272; -.
DR BioGRID; 250194; 2.
DR STRING; 10116.ENSRNOP00000061528; -.
DR MEROPS; M10.022; -.
DR GlyGen; O88272; 4 sites.
DR PaxDb; O88272; -.
DR Ensembl; ENSRNOT00000066880; ENSRNOP00000061528; ENSRNOG00000017477.
DR GeneID; 94339; -.
DR KEGG; rno:94339; -.
DR CTD; 26561; -.
DR RGD; 620201; Mmp23.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000161187; -.
DR HOGENOM; CLU_015489_2_1_1; -.
DR InParanoid; O88272; -.
DR OMA; HLHHCFD; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; O88272; -.
DR EvolutionaryTrace; O88272; -.
DR PRO; PR:O88272; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000017477; Expressed in ovary and 19 other tissues.
DR Genevisible; O88272; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
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; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; ISS:UniProtKB.
DR GO; GO:0000003; P:reproduction; ISS: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; 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; 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 3D-structure; 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..391
FT /note="Matrix metalloproteinase-23"
FT /id="PRO_0000259918"
FT PROPEP 1..79
FT /evidence="ECO:0000255"
FT /id="PRO_0000259919"
FT CHAIN 80..391
FT /note="Matrix metalloproteinase-23, soluble form"
FT /id="PRO_0000259920"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..391
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 256..290
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DOMAIN 296..381
FT /note="Ig-like C2-type"
FT ACT_SITE 213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 79..80
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 256..290
FT /evidence="ECO:0000269|PubMed:19965868"
FT DISULFID 263..283
FT /evidence="ECO:0000269|PubMed:19965868"
FT DISULFID 272..287
FT /evidence="ECO:0000269|PubMed:19965868"
FT DISULFID 322..371
FT /evidence="ECO:0000250"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:2K72"
FT TURN 268..273
FT /evidence="ECO:0007829|PDB:2K72"
FT HELIX 276..282
FT /evidence="ECO:0007829|PDB:2K72"
FT TURN 284..288
FT /evidence="ECO:0007829|PDB:2K72"
SQ SEQUENCE 391 AA; 44618 MW; F980FD50BDDB6A10 CRC64;
MGWRACLRPE ASGAVQGRWL GAVLSGLCLL SALAFLEWLG SPTETAWNAA QGNVDAPDVG
GSTPQVPSLL SMLVTRRRRY TLTPARLRWD HFNLTYRILS FPRNLLSPEE TRRGLAAAFR
MWSDVSPFSF REVAPERPSD LKIGFYPVNH TDCLVSALHH CFDGPTGELA HAFFPPHGGI
HFDDSEYWVL GPTRYSWKKG VWLTDLVHVA AHEIGHALGL MHSQQDQALM HLNATLRGWK
ALSQDELWGL HRLYGCLDRI FVCTSWARKG FCDVRQRLMK RLCPRSCDFC YEFPFPTVAT
TTSPTRTKTR FVREGRNMTF HCGQKILHKK GKVYWYKDQE PLEFSYPGYL ALGEARLSII
ANAVNEGTYT CVVRHRQRVL TTYSWRVRVR S
