ID   MMP23_MOUSE             Reviewed;         391 AA.
AC   O88676; Q3KNC0;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=Matrix metalloproteinase-23;
DE            Short=MMP-23;
DE            EC=3.4.24.-;
DE   AltName: Full=Cysteine array matrix metalloproteinase;
DE            Short=CA-MMP;
DE            Short=CAMP metalloproteinase;
DE   Contains:
DE     RecName: Full=Matrix metalloproteinase-23, soluble form;
DE   Flags: Precursor;
GN   Name=Mmp23; Synonyms=Cammp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, DEVELOPMENTAL
RP   STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Spleen;
RX   PubMed=10471791; DOI=10.1016/s0014-5793(99)01046-7;
RA   Pei D.;
RT   "CA-MMP: a matrix metalloproteinase with a novel cysteine array, but
RT   without the classic cysteine switch.";
RL   FEBS Lett. 457:262-270(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type II membrane protein {ECO:0000250}. Membrane
CC       {ECO:0000269|PubMed:10471791}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:10471791}. Note=A secreted form produced by
CC       proteolytic cleavage may also exist. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O88676-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88676-2; Sequence=VSP_021561;
CC   -!- TISSUE SPECIFICITY: Expressed at relatively high level in heart, lung
CC       and spleen. Not detected in brain, liver, skeletal muscle, kidney and
CC       testis. {ECO:0000269|PubMed:10471791}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at relatively high level at 7 days old
CC       embryo compared to those at stadges day 11, 15 and 17.
CC       {ECO:0000269|PubMed:10471791}.
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:0000250}.
CC   -!- PTM: Proteolytic cleavage might yield an active form.
CC   -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR   EMBL; AF085742; AAC34886.1; -; mRNA.
DR   EMBL; AK146510; BAE27223.1; -; mRNA.
DR   EMBL; BC107357; AAI07358.1; -; mRNA.
DR   EMBL; BC107358; AAI07359.1; -; mRNA.
DR   CCDS; CCDS19034.1; -. [O88676-1]
DR   RefSeq; NP_001307164.1; NM_001320235.1. [O88676-2]
DR   RefSeq; NP_036115.1; NM_011985.3. [O88676-1]
DR   RefSeq; XP_006538945.1; XM_006538882.3. [O88676-1]
DR   AlphaFoldDB; O88676; -.
DR   BMRB; O88676; -.
DR   SMR; O88676; -.
DR   STRING; 10090.ENSMUSP00000030937; -.
DR   MEROPS; M10.022; -.
DR   TCDB; 8.B.14.2.1; the sea anemone peptide toxin, class 1 (bgk) family.
DR   GlyCosmos; O88676; 4 sites, No reported glycans.
DR   GlyGen; O88676; 4 sites.
DR   iPTMnet; O88676; -.
DR   PhosphoSitePlus; O88676; -.
DR   MaxQB; O88676; -.
DR   PaxDb; 10090-ENSMUSP00000030937; -.
DR   ProteomicsDB; 295688; -. [O88676-1]
DR   ProteomicsDB; 295689; -. [O88676-2]
DR   Antibodypedia; 3453; 404 antibodies from 32 providers.
DR   DNASU; 26561; -.
DR   Ensembl; ENSMUST00000030937.2; ENSMUSP00000030937.2; ENSMUSG00000029061.3. [O88676-1]
DR   GeneID; 26561; -.
DR   KEGG; mmu:26561; -.
DR   UCSC; uc008wed.1; mouse. [O88676-1]
DR   UCSC; uc012dqs.1; mouse. [O88676-2]
DR   AGR; MGI:1347361; -.
DR   CTD; 26561; -.
DR   MGI; MGI:1347361; Mmp23.
DR   VEuPathDB; HostDB:ENSMUSG00000029061; -.
DR   eggNOG; KOG1565; Eukaryota.
DR   GeneTree; ENSGT00940000161187; -.
DR   HOGENOM; CLU_015489_2_1_1; -.
DR   InParanoid; O88676; -.
DR   OMA; HLHHCFD; -.
DR   OrthoDB; 3012491at2759; -.
DR   PhylomeDB; O88676; -.
DR   TreeFam; TF315428; -.
DR   BioGRID-ORCS; 26561; 4 hits in 77 CRISPR screens.
DR   PRO; PR:O88676; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; O88676; Protein.
DR   Bgee; ENSMUSG00000029061; Expressed in ascending aorta and 170 other cell types or tissues.
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: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; cd00096; Ig; 1.
DR   CDD; cd04278; ZnMc_MMP; 1.
DR   Gene3D; 1.10.10.1940; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR001818; Pept_M10_metallopeptidase.
DR   InterPro; IPR021190; Pept_M10A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR003582; ShKT_dom.
DR   PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR   PANTHER; PTHR10201:SF7; MATRIX METALLOPROTEINASE-23; 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; Immunoglobulin; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51670; SHKT; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; O88676; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW   Endoplasmic reticulum; Glycoprotein; Hydrolase; Immunoglobulin domain;
KW   Membrane; Metal-binding; Protease; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT   CHAIN           1..391
FT                   /note="Matrix metalloproteinase-23"
FT                   /id="PRO_0000259915"
FT   PROPEP          1..79
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000259916"
FT   CHAIN           80..391
FT                   /note="Matrix metalloproteinase-23, soluble form"
FT                   /id="PRO_0000259917"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..391
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          256..290
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DOMAIN          298..383
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:0000250"
FT   DISULFID        263..283
FT                   /evidence="ECO:0000250"
FT   DISULFID        272..287
FT                   /evidence="ECO:0000250"
FT   DISULFID        322..371
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         144..157
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021561"
SQ   SEQUENCE   391 AA;  44451 MW;  8C9675020F02F632 CRC64;
     MGCRACLRPE ASGAVQGRWL GAALSGLCLL SALALLEWLG APTETAWRAA QGNVDAPNVG
     SSTAQVPRLL TMSVTRRRRY TLTPARLRWD HFNLTYRVLS FPRNLLSPEE TRRGLAAAFR
     MWSDVSPFSF REVAPERPSD LKIGFYPVNH TDCLVSAVHH CFDGPTGELA HAFFPPHGGI
     HFDDSEYWVL GPTRYSWKKG VWLTNLVHVA AHEIGHALGL MHSQQDQALM HLNATLRGWK
     ALSQDELWGL HRLYGCLDRI FVCASWARKG FCDVRQRLMK RLCPRSCDFC YEFPFPTVAT
     TTSPTRTKTR LVREGRNMTF HCGQKILHKK GKVYWYKDQE PLEFSYPGYL ALGEAQLSII
     ANAVNEGTYT CVVRRHQRVL STYSWRVRVR N
//