ADA23_MOUSE
ID ADA23_MOUSE Reviewed; 829 AA.
AC Q9R1V7; Q6QDY9; Q6QDZ0; Q8CC33;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 23;
DE Short=ADAM 23;
DE AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 3;
DE Short=MDC-3;
DE Flags: Precursor;
GN Name=Adam23; Synonyms=Mdc3;
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 ALPHA), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10433968; DOI=10.1016/s0378-1119(99)00253-x;
RA Sagane K., Yamazaki K., Mizui Y., Tanaka I.;
RT "Cloning and chromosomal mapping of mouse ADAM11, ADAM22 and ADAM23.";
RL Gene 236:79-86(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 666-829 (ISOFORMS ALPHA; BETA AND GAMMA), AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=14697522; DOI=10.1016/j.gene.2003.10.012;
RA Sun Y.P., Deng K.J., Wang F., Zhang J., Huang X., Qiao S., Zhao S.;
RT "Two novel isoforms of Adam23 expressed in the developmental process of
RT mouse and human brains.";
RL Gene 325:171-178(2004).
RN [5]
RP INTERACTION WITH LGI1 AND LGI4.
RX PubMed=18974846; DOI=10.7150/ijbs.4.387;
RA Sagane K., Ishihama Y., Sugimoto H.;
RT "LGI1 and LGI4 bind to ADAM22, ADAM23 and ADAM11.";
RL Int. J. Biol. Sci. 4:387-396(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in cell-cell and cell-matrix interactions.
CC This is a non-catalytic metalloprotease-like protein (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Can bind to LGI1 and LGI4.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform Gamma]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Alpha;
CC IsoId=Q9R1V7-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9R1V7-2; Sequence=VSP_012050;
CC Name=Gamma;
CC IsoId=Q9R1V7-3; Sequence=VSP_012049;
CC Name=Delta;
CC IsoId=Q9R1V7-4; Sequence=VSP_012047, VSP_012048;
CC -!- TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:10433968}.
CC -!- DEVELOPMENTAL STAGE: On 15 dpc embryo the level of isoform Gamma
CC exceeded that of isoform Alpha and isoform Beta and decreased after
CC birth. On P10 post neonatal, the level of isoform Gamma is undetectable
CC and isoform Alpha and isoform Beta are expressed again.
CC {ECO:0000269|PubMed:14697522}.
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DR EMBL; AB009673; BAA83381.1; -; mRNA.
DR EMBL; AK034022; BAC28550.1; -; mRNA.
DR EMBL; AL645534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL683801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY545640; AAS49900.1; -; mRNA.
DR EMBL; AY545641; AAS49901.1; -; mRNA.
DR CCDS; CCDS14999.1; -. [Q9R1V7-1]
DR RefSeq; NP_035910.1; NM_011780.3. [Q9R1V7-1]
DR RefSeq; XP_006496032.1; XM_006495969.3. [Q9R1V7-2]
DR RefSeq; XP_006496033.1; XM_006495970.3. [Q9R1V7-3]
DR AlphaFoldDB; Q9R1V7; -.
DR SMR; Q9R1V7; -.
DR BioGRID; 204715; 14.
DR IntAct; Q9R1V7; 2.
DR MINT; Q9R1V7; -.
DR STRING; 10090.ENSMUSP00000138362; -.
DR MEROPS; M12.979; -.
DR GlyConnect; 2259; 5 N-Linked glycans (3 sites).
DR GlyGen; Q9R1V7; 8 sites, 5 N-linked glycans (3 sites).
DR iPTMnet; Q9R1V7; -.
DR PhosphoSitePlus; Q9R1V7; -.
DR SwissPalm; Q9R1V7; -.
DR MaxQB; Q9R1V7; -.
DR PaxDb; Q9R1V7; -.
DR PeptideAtlas; Q9R1V7; -.
DR PRIDE; Q9R1V7; -.
DR ProteomicsDB; 285881; -. [Q9R1V7-1]
DR ProteomicsDB; 285882; -. [Q9R1V7-2]
DR ProteomicsDB; 285883; -. [Q9R1V7-3]
DR ProteomicsDB; 285884; -. [Q9R1V7-4]
DR Antibodypedia; 34180; 244 antibodies from 29 providers.
DR DNASU; 23792; -.
DR Ensembl; ENSMUST00000087374; ENSMUSP00000084633; ENSMUSG00000025964. [Q9R1V7-1]
DR Ensembl; ENSMUST00000114103; ENSMUSP00000139862; ENSMUSG00000025964. [Q9R1V7-3]
DR Ensembl; ENSMUST00000114107; ENSMUSP00000109742; ENSMUSG00000025964. [Q9R1V7-2]
DR GeneID; 23792; -.
DR KEGG; mmu:23792; -.
DR UCSC; uc007bge.1; mouse. [Q9R1V7-4]
DR UCSC; uc007bgg.1; mouse. [Q9R1V7-1]
DR CTD; 8745; -.
DR MGI; MGI:1345162; Adam23.
DR VEuPathDB; HostDB:ENSMUSG00000025964; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000158781; -.
DR HOGENOM; CLU_012714_5_2_1; -.
DR InParanoid; Q9R1V7; -.
DR OMA; ECDCTES; -.
DR OrthoDB; 162519at2759; -.
DR Reactome; R-MMU-5682910; LGI-ADAM interactions.
DR BioGRID-ORCS; 23792; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q9R1V7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9R1V7; protein.
DR Bgee; ENSMUSG00000025964; Expressed in facial nucleus and 216 other tissues.
DR Genevisible; Q9R1V7; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..55
FT /evidence="ECO:0000255"
FT PROPEP 56..283
FT /evidence="ECO:0000255"
FT /id="PRO_0000029120"
FT CHAIN 284..829
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 23"
FT /id="PRO_0000029121"
FT TOPO_DOM 284..789
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..810
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 811..829
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 296..493
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 499..585
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 729..766
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 405..488
FT /evidence="ECO:0000250"
FT DISULFID 447..472
FT /evidence="ECO:0000250"
FT DISULFID 449..456
FT /evidence="ECO:0000250"
FT DISULFID 557..577
FT /evidence="ECO:0000250"
FT DISULFID 733..748
FT /evidence="ECO:0000250"
FT DISULFID 742..754
FT /evidence="ECO:0000250"
FT DISULFID 756..765
FT /evidence="ECO:0000250"
FT VAR_SEQ 690
FT /note="S -> R (in isoform Delta)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012047"
FT VAR_SEQ 691..829
FT /note="Missing (in isoform Delta)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012048"
FT VAR_SEQ 784..829
FT /note="GPSATNLIIGSIAGAILVAAIVLGGTGWGFKNVKKRRFDPTQQGPI -> ET
FT SRRGDSIPLSKAPSESSALEECHLALLGSGNDMFSAMLPELLSL (in isoform
FT Gamma)"
FT /evidence="ECO:0000305"
FT /id="VSP_012049"
FT VAR_SEQ 784..814
FT /note="GPSATNLIIGSIAGAILVAAIVLGGTGWGFK -> VNMATSRLIGAVAGTVL
FT ALGVIFGGTGWGIE (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_012050"
FT CONFLICT 6
FT /note="S -> I (in Ref. 2; BAC28550)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="P -> S (in Ref. 2; BAC28550)"
FT /evidence="ECO:0000305"
FT CONFLICT 19..22
FT /note="PGAS -> SGTF (in Ref. 2; BAC28550)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="A -> S (in Ref. 2; BAC28550)"
FT /evidence="ECO:0000305"
FT CONFLICT 33..35
FT /note="VPA -> EPV (in Ref. 2; BAC28550)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 829 AA; 91548 MW; F6EBCD69DD50F53A CRC64;
MKPPGSISRR PTLTGCSLPG ASCGPGRCPA GPVPARAPPC RLLLVLLLLP ALATSSRPRA
RGAAAPSAPH WNETAEKTLG VLADEDNTLQ QNSSSRNTSY SSAVQKEITL PSRLVYYINQ
DSESPYHVLD TKARHQQKHN KAVHLAQASF QIEAFGSKFI LDLTLNNGLL SSDYVEIHYE
DGKQMYSKGG EHCYYHGSIR GVKDSRVALS TCNGLHGMFE DDTFVYMIEP LELTDDEKST
GRPHIIQKTL AGQYSKQMKN LSTDGSDQWP LLPELQWLRR RKRAVNPSRG VFEEMKYLEL
MIVNDHKTYK KHRSSHAHTN NFAKSVVNLV DSIYKEQLNT RVVLVAVETW TEKDHIDITI
NPVQMLHDFS KYRQRIKQHA DAVHLISRVT FHYKRSSLSY FGGVCSRIRG VGVNEYGLPM
AVAQVLSQSL AQNLGIQWEP SSRKPKCECI ESWGGCIMEE TGVSHSRKFS KCSILEYRDF
LQRGGGACLF NRPTKLFEPT ECGNGYVEAG EECDCGFHVE CYGVCCKKCS LSNGAHCSDG
PCCNNTSCLF QSRGYECRDA VNSCDITEYC TGDSGQCPPN LHKQDGYSCN QNQGRCYNGE
CKTRDNQCQY IWGTKAAGSD KFCYEKLNTE GTEKGNCGKD GDRWIPCSKH DVFCGFLLCT
NLTRAPRIGQ LQGEIIPTSF YHQGRVIDCS GAHVVLDDDT DVGYVEDGTP CGPSMMCLDR
KCLQIQALNM SSCPLDSRGK VCSGHGVCSN EATCICDFTW AGTDCSIRDP VRNPNPPKDE
GPKGPSATNL IIGSIAGAIL VAAIVLGGTG WGFKNVKKRR FDPTQQGPI
