GenomeNet

Database: UniProt
Entry: Q9R1V7
LinkDB: Q9R1V7
Original site: Q9R1V7 
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   10-APR-2019, entry version 142.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   of 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May play a role in cell-cell and cell-matrix
CC       interactions. This is a non-catalytic metalloprotease-like protein
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Can bind to LGI1 and LGI4.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
CC       type I 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         Note=No experimental confirmation available.;
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
CC       after birth. On P10 post neonatal, the level of isoform Gamma is
CC       undetectable and isoform Alpha and isoform Beta are expressed
CC       again. {ECO:0000269|PubMed:14697522}.
DR   EMBL; AB009673; BAA83381.1; -; mRNA.
DR   EMBL; AK034022; BAC28550.1; -; mRNA.
DR   EMBL; AL645534; CAI25281.1; -; Genomic_DNA.
DR   EMBL; AL645534; CAI25282.1; -; Genomic_DNA.
DR   EMBL; AL645637; CAI25282.1; JOINED; Genomic_DNA.
DR   EMBL; AL645534; CAI25284.1; -; Genomic_DNA.
DR   EMBL; AL645637; CAI25284.1; JOINED; Genomic_DNA.
DR   EMBL; AL645637; CAI25456.1; -; Genomic_DNA.
DR   EMBL; AL645534; CAI25456.1; JOINED; Genomic_DNA.
DR   EMBL; AL645637; CAI25458.1; -; Genomic_DNA.
DR   EMBL; AL645534; CAI25458.1; JOINED; Genomic_DNA.
DR   EMBL; AL683801; CAI26241.1; -; 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   UniGene; Mm.124892; -.
DR   ProteinModelPortal; Q9R1V7; -.
DR   SMR; Q9R1V7; -.
DR   BioGrid; 204715; 1.
DR   IntAct; Q9R1V7; 3.
DR   MINT; Q9R1V7; -.
DR   STRING; 10090.ENSMUSP00000138362; -.
DR   MEROPS; M12.979; -.
DR   iPTMnet; Q9R1V7; -.
DR   PhosphoSitePlus; Q9R1V7; -.
DR   SwissPalm; Q9R1V7; -.
DR   PaxDb; Q9R1V7; -.
DR   PeptideAtlas; Q9R1V7; -.
DR   PRIDE; Q9R1V7; -.
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   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000158781; -.
DR   HOGENOM; HOG000231962; -.
DR   HOVERGEN; HBG050456; -.
DR   InParanoid; Q9R1V7; -.
DR   KO; K06837; -.
DR   OMA; SSDQWPF; -.
DR   OrthoDB; 162519at2759; -.
DR   Reactome; R-MMU-5682910; LGI-ADAM interactions.
DR   PRO; PR:Q9R1V7; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000025964; Expressed in 225 organ(s), highest expression level in substantia nigra.
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   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; IPR013032; EGF-like_CS.
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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Reference proteome; Secreted;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     55       {ECO:0000255}.
FT   PROPEP       56    283       {ECO:0000255}.
FT                                /FTId=PRO_0000029120.
FT   CHAIN       284    829       Disintegrin and metalloproteinase domain-
FT                                containing protein 23.
FT                                /FTId=PRO_0000029121.
FT   TOPO_DOM    284    789       Extracellular. {ECO:0000255}.
FT   TRANSMEM    790    810       Helical. {ECO:0000255}.
FT   TOPO_DOM    811    829       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      296    493       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      499    585       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      729    766       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    586    608       Cys-rich.
FT   CARBOHYD     72     72       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     92     92       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     97     97       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    260    260       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    544    544       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    545    545       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    661    661       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    729    729       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    405    488       {ECO:0000250}.
FT   DISULFID    447    472       {ECO:0000250}.
FT   DISULFID    449    456       {ECO:0000250}.
FT   DISULFID    557    577       {ECO:0000250}.
FT   DISULFID    733    748       {ECO:0000250}.
FT   DISULFID    742    754       {ECO:0000250}.
FT   DISULFID    756    765       {ECO:0000250}.
FT   VAR_SEQ     690    690       S -> R (in isoform Delta).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_012047.
FT   VAR_SEQ     691    829       Missing (in isoform Delta).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_012048.
FT   VAR_SEQ     784    829       GPSATNLIIGSIAGAILVAAIVLGGTGWGFKNVKKRRFDPT
FT                                QQGPI -> ETSRRGDSIPLSKAPSESSALEECHLALLGSG
FT                                NDMFSAMLPELLSL (in isoform Gamma).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_012049.
FT   VAR_SEQ     784    814       GPSATNLIIGSIAGAILVAAIVLGGTGWGFK -> VNMATS
FT                                RLIGAVAGTVLALGVIFGGTGWGIE (in isoform
FT                                Beta). {ECO:0000305}.
FT                                /FTId=VSP_012050.
FT   CONFLICT      6      6       S -> I (in Ref. 2; BAC28550).
FT                                {ECO:0000305}.
FT   CONFLICT     11     11       P -> S (in Ref. 2; BAC28550).
FT                                {ECO:0000305}.
FT   CONFLICT     19     22       PGAS -> SGTF (in Ref. 2; BAC28550).
FT                                {ECO:0000305}.
FT   CONFLICT     30     30       A -> S (in Ref. 2; BAC28550).
FT                                {ECO:0000305}.
FT   CONFLICT     33     35       VPA -> EPV (in Ref. 2; BAC28550).
FT                                {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
//
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