MMP23_MOUSE
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 03-AUG-2022, entry version 158.
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 GlyGen; O88676; 4 sites.
DR iPTMnet; O88676; -.
DR PhosphoSitePlus; O88676; -.
DR MaxQB; O88676; -.
DR PaxDb; O88676; -.
DR PRIDE; O88676; -.
DR ProteomicsDB; 295688; -. [O88676-1]
DR ProteomicsDB; 295689; -. [O88676-2]
DR Antibodypedia; 3453; 373 antibodies from 32 providers.
DR DNASU; 26561; -.
DR Ensembl; ENSMUST00000030937; ENSMUSP00000030937; ENSMUSG00000029061. [O88676-1]
DR GeneID; 26561; -.
DR KEGG; mmu:26561; -.
DR UCSC; uc008wed.1; mouse. [O88676-1]
DR UCSC; uc012dqs.1; mouse. [O88676-2]
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; 1075463at2759; -.
DR PhylomeDB; O88676; -.
DR TreeFam; TF315428; -.
DR BioGRID-ORCS; 26561; 4 hits in 72 CRISPR screens.
DR PRO; PR:O88676; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O88676; protein.
DR Bgee; ENSMUSG00000029061; Expressed in ascending aorta and 167 other tissues.
DR Genevisible; O88676; MM.
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 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
