MMP23_BOVIN
ID MMP23_BOVIN Reviewed; 393 AA.
AC Q2TBM7;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Matrix metalloproteinase-23;
DE Short=MMP-23;
DE EC=3.4.24.-;
DE AltName: Full=Matrix metallopeptidase 23B;
DE Contains:
DE RecName: Full=Matrix metalloproteinase-23, soluble form;
DE Flags: Precursor;
GN Name=MMP23; Synonyms=MMP23B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC Note=A secreted form produced by proteolytic cleavage may also exist.
CC {ECO:0000250}.
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. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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; BC109902; AAI09903.1; -; mRNA.
DR RefSeq; NP_001033645.1; NM_001038556.2.
DR AlphaFoldDB; Q2TBM7; -.
DR SMR; Q2TBM7; -.
DR STRING; 9913.ENSBTAP00000014210; -.
DR MEROPS; M10.022; -.
DR PaxDb; Q2TBM7; -.
DR PRIDE; Q2TBM7; -.
DR GeneID; 527590; -.
DR KEGG; bta:527590; -.
DR CTD; 26561; -.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; Q2TBM7; -.
DR OrthoDB; 1075463at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; IBA:GO_Central.
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; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT CHAIN 1..393
FT /note="Matrix metalloproteinase-23"
FT /id="PRO_0000259912"
FT PROPEP 1..81
FT /evidence="ECO:0000255"
FT /id="PRO_0000259913"
FT CHAIN 82..393
FT /note="Matrix metalloproteinase-23, soluble form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000259914"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..393
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 258..292
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DOMAIN 298..383
FT /note="Ig-like C2-type"
FT REGION 60..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 81..82
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 258..292
FT /evidence="ECO:0000250"
FT DISULFID 265..285
FT /evidence="ECO:0000250"
FT DISULFID 274..289
FT /evidence="ECO:0000250"
FT DISULFID 324..373
FT /evidence="ECO:0000250"
SQ SEQUENCE 393 AA; 43964 MW; AF5A4C5FC3AA9F32 CRC64;
MGRGACVPSA ASGAGDRARQ LGAVLGALCL FPALVLLAWP GTPANGAGAR VAQGDAAPQT
SGVLASGSLG PPHPPVPRRR RYTLTPARLR WEHFNLTYKI LSFPRNLLSP SETRRGLAAA
FRMWSDVSPF SFREVAPEQP SDLRIGFYPV NHTDCLVSPL HHCFDGPTGE LAHAFFPPHG
GIHFDDSEYW VLGRTRYSWK KGVWLTDLVH VAAHEIGHAL GLMHSQHGRA LMHLNATLRG
WKALSQDELW GLHRLYGCLD RLFVCASWAR RGFCDTRRRL MKRLCPSSCD FCYEFPFPTV
AATPPPPRTK TKLVPEGRNV TFRCGQKILH KKGKVYWYKD QEPLEFSYPG YLALGEAHLS
IIANAINEGT YTCVVRRRQR VLSTYSWRIR VRS
