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Matrix metalloproteinase-23 (MMP-23) (EC 3.4.24.-) (metalloprotease in the female reproductive tract) (MIFR) [Cleaved into: Matrix metalloproteinase-23, soluble form]

 MMP23_RAT               Reviewed;         391 AA.
O88272;
14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
05-DEC-2018, entry version 127.
RecName: Full=Matrix metalloproteinase-23;
Short=MMP-23;
EC=3.4.24.-;
AltName: Full=metalloprotease in the female reproductive tract;
Short=MIFR;
Contains:
RecName: Full=Matrix metalloproteinase-23, soluble form;
Flags: Precursor;
Name=Mmp23; Synonyms=Mifr;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, AND
SUBCELLULAR LOCATION.
STRAIN=Sprague-Dawley; TISSUE=Ovary;
PubMed=11328856; DOI=10.1210/mend.15.5.0638;
Ohnishi J., Ohnishi E., Jin M., Hirano W., Nakane D., Matsui H.,
Kimura A., Sawa H., Nakayama K., Shibuya H., Nagashima K.,
Takahashi T.;
"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.";
Mol. Endocrinol. 15:747-764(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
STRUCTURE BY NMR OF 254-290, FUNCTION, SUBCELLULAR LOCATION,
TOXIN-LIKE DOMAIN, AND DISULFIDE BONDS.
PubMed=19965868; DOI=10.1074/jbc.M109.071266;
Rangaraju S., Khoo K.K., Feng Z.P., Crossley G., Nugent D.,
Khaytin I., Chi V., Pham C., Calabresi P., Pennington M.W.,
Norton R.S., Chandy K.G.;
"Potassium channel modulation by a toxin domain in matrix
metalloprotease 23.";
J. Biol. Chem. 285:9124-9136(2010).
-!- FUNCTION: Protease. May regulate the surface expression of some
potassium channels by retaining them in the endoplasmic reticulum.
{ECO:0000269|PubMed:19965868}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- ACTIVITY REGULATION: Inhibited by TIMP2. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
protein. Endoplasmic reticulum membrane; Single-pass type II
membrane protein. Note=A secreted form produced by proteolytic
cleavage may also exist. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed at the highest levels in ovary and
uterus. In ovary expression is strictly confined to granulosa
cells of preantral and small antral follicles. Detected also in
testis and prostate. {ECO:0000269|PubMed:11328856}.
-!- DOMAIN: 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.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:11328856}.
-!- PTM: Proteolytic cleavage might yield an active form.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AB010960; BAA24832.1; -; mRNA.
EMBL; BC086586; AAH86586.1; -; mRNA.
RefSeq; NP_446058.1; NM_053606.2.
UniGene; Rn.22562; -.
PDB; 2K72; NMR; -; A=254-290.
PDBsum; 2K72; -.
ProteinModelPortal; O88272; -.
SMR; O88272; -.
BioGrid; 250194; 2.
STRING; 10116.ENSRNOP00000061528; -.
MEROPS; M10.022; -.
PaxDb; O88272; -.
PRIDE; O88272; -.
Ensembl; ENSRNOT00000066880; ENSRNOP00000061528; ENSRNOG00000017477.
GeneID; 94339; -.
KEGG; rno:94339; -.
CTD; 26561; -.
RGD; 620201; Mmp23.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00940000161187; -.
HOGENOM; HOG000231157; -.
HOVERGEN; HBG053177; -.
InParanoid; O88272; -.
KO; K08001; -.
OMA; DEVWGLH; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; O88272; -.
EvolutionaryTrace; O88272; -.
PRO; PR:O88272; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000017477; Expressed in 9 organ(s), highest expression level in spleen.
Genevisible; O88272; RN.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
GO; GO:0000003; P:reproduction; ISS:UniProtKB.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028687; MMP23.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR003582; ShKT_dom.
PANTHER; PTHR10201:SF7; PTHR10201:SF7; 1.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01549; ShK; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00254; ShKT; 1.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51670; SHKT; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues; Complete proteome;
Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
Immunoglobulin domain; Membrane; Metal-binding; Metalloprotease;
Protease; Reference proteome; Signal-anchor; Transmembrane;
Transmembrane helix; Zinc; Zymogen.
CHAIN 1 391 Matrix metalloproteinase-23.
/FTId=PRO_0000259918.
PROPEP 1 79 {ECO:0000255}.
/FTId=PRO_0000259919.
CHAIN 80 391 Matrix metalloproteinase-23, soluble
form.
/FTId=PRO_0000259920.
TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.
TRANSMEM 20 38 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 39 391 Lumenal. {ECO:0000255}.
DOMAIN 256 290 ShKT. {ECO:0000255|PROSITE-
ProRule:PRU01005}.
DOMAIN 296 381 Ig-like C2-type.
COMPBIAS 76 79 Poly-Arg.
ACT_SITE 213 213 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 212 212 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 216 216 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 222 222 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
SITE 79 80 Cleavage; by furin-like protease.
{ECO:0000255}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 149 149 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 233 233 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 256 290 {ECO:0000269|PubMed:19965868}.
DISULFID 263 283 {ECO:0000269|PubMed:19965868}.
DISULFID 272 287 {ECO:0000269|PubMed:19965868}.
DISULFID 322 371 {ECO:0000250}.
HELIX 263 267 {ECO:0000244|PDB:2K72}.
TURN 268 273 {ECO:0000244|PDB:2K72}.
HELIX 276 282 {ECO:0000244|PDB:2K72}.
TURN 284 288 {ECO:0000244|PDB:2K72}.
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


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