ID ADA23_HUMAN Reviewed; 832 AA. AC O75077; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 28-JUL-2009, entry version 68. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA). RC TISSUE=Brain; RX MEDLINE=98359734; PubMed=9693107; RA Sagane K., Ohya Y., Hasegawa Y., Tanaka I.; RT "Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 RT and MDC3: novel human cellular disintegrins highly expressed in the RT brain."; RL Biochem. J. 334:93-98(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), INTERACTION WITH INTEGRIN RP ALPHA-V/BETA-3, AND MUTAGENESIS OF GLU-566. RC TISSUE=Brain; RX MEDLINE=20214833; PubMed=10749942; RA Cal S., Freije J.M.P., Lopez J.M., Takada Y., Lopez-Otin C.; RT "ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via RT interaction with the alpha v beta 3 integrin through an RGD- RT independent mechanism."; RL Mol. Biol. Cell 11:1457-1469(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA), AND RP TISSUE SPECIFICITY. RC TISSUE=Fetal 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-707, AND MASS RP SPECTROMETRY. RC TISSUE=T-cell; RX PubMed=16094384; DOI=10.1038/nmeth776; RA Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., RA Bodenmiller B., Watts J.D., Hood L., Aebersold R.; RT "Quantitative phosphoproteome analysis using a dendrimer conjugation RT chemistry and tandem mass spectrometry."; RL Nat. Methods 2:591-598(2005). CC -!- FUNCTION: May play a role in cell-cell and cell-matrix CC interactions. This is a non-catalytic metalloprotease-like CC protein. CC -!- SUBUNIT: Ligand for integrin alpha-V/beta-3. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein (Potential). CC -!- SUBCELLULAR LOCATION: Isoform Gamma: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Alpha; CC IsoId=O75077-1; Sequence=Displayed; CC Name=Beta; CC IsoId=O75077-2; Sequence=VSP_012046; CC Name=Gamma; CC IsoId=O75077-3; Sequence=VSP_012045; CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and weakly CC expressed in the heart. In the brain, expressed prominently in the CC amygdala, caudate nucleus, hypothalamus, thalamus, cerebral cortex CC and occipital pole. CC -!- DEVELOPMENTAL STAGE: Highly expressed in the fetal brain. CC -!- DOMAIN: A conserved motif AVN[ED]CD within the disintegrin-like CC domain could be involved in the binding to the integrin receptor. CC -!- SIMILARITY: Contains 1 disintegrin domain. CC -!- SIMILARITY: Contains 1 EGF-like domain. CC -!- SIMILARITY: Contains 1 peptidase M12B domain. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/ADAM23ID44041ch2q33.html"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB009672; BAA32351.1; -; mRNA. DR EMBL; AJ005580; CAC20565.1; -; mRNA. DR IPI; IPI00021903; -. DR IPI; IPI00477723; -. DR IPI; IPI00478084; -. DR RefSeq; NP_003803.1; -. DR UniGene; Hs.591643; -. DR HSSP; P18619; 1FVL. DR PhosphoSite; O75077; -. DR PRIDE; O75077; -. DR Ensembl; ENST00000264377; ENSP00000264377; ENSG00000114948; Homo sapiens. DR Ensembl; ENST00000374416; ENSP00000363537; ENSG00000114948; Homo sapiens. DR GeneID; 8745; -. DR KEGG; hsa:8745; -. DR UCSC; uc002vbq.1; human. DR GeneCards; GC02P207018; -. DR H-InvDB; HIX0002773; -. DR H-InvDB; HIX0030166; -. DR HGNC; HGNC:202; ADAM23. DR MIM; 603710; gene. DR PharmGKB; PA24519; -. DR HOGENOM; O75077; -. DR HOVERGEN; O75077; -. DR OMA; O75077; NTSCLFQ. DR NextBio; 32813; -. DR ArrayExpress; O75077; -. DR Bgee; O75077; -. DR CleanEx; HS_ADAM23; -. DR GermOnline; ENSG00000114948; Homo sapiens. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0005178; F:integrin binding; TAS:ProtInc. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR001762; Blood-coag_inhib_Disintegrin. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR006210; EGF-like. DR InterPro; IPR013032; EGF-like_reg_CS. DR InterPro; IPR000742; EGF_3. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Gene3D; G3DSA:4.10.70.10; Blood-coag_inhib_Disintegrin; 1. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR ProDom; PD000664; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SMART; SM00181; EGF; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; FALSE_NEG. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; FALSE_NEG. 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; Phosphoprotein; Secreted; KW Signal; Transmembrane. FT SIGNAL 1 59 Potential. FT PROPEP 60 286 Potential. FT /FTId=PRO_0000029118. FT CHAIN 287 832 Disintegrin and metalloproteinase domain- FT containing protein 23. FT /FTId=PRO_0000029119. FT TOPO_DOM 287 792 Extracellular (Potential). FT TRANSMEM 793 813 Potential. FT TOPO_DOM 814 832 Cytoplasmic (Potential). FT DOMAIN 299 496 Peptidase M12B. FT DOMAIN 502 588 Disintegrin. FT DOMAIN 732 769 EGF-like. FT REGION 563 568 May bind the integrin receptor. FT COMPBIAS 589 611 Cys-rich. FT MOD_RES 707 707 Phosphotyrosine. FT CARBOHYD 76 76 N-linked (GlcNAc...) (Potential). FT CARBOHYD 96 96 N-linked (GlcNAc...) (Potential). FT CARBOHYD 100 100 N-linked (GlcNAc...) (Potential). FT CARBOHYD 263 263 N-linked (GlcNAc...) (Potential). FT CARBOHYD 547 547 N-linked (GlcNAc...) (Potential). FT CARBOHYD 548 548 N-linked (GlcNAc...) (Potential). FT CARBOHYD 664 664 N-linked (GlcNAc...) (Potential). FT CARBOHYD 732 732 N-linked (GlcNAc...) (Potential). FT DISULFID 408 491 By similarity. FT DISULFID 450 475 By similarity. FT DISULFID 452 459 By similarity. FT DISULFID 560 580 By similarity. FT DISULFID 736 751 By similarity. FT DISULFID 745 757 By similarity. FT DISULFID 759 768 By similarity. FT VAR_SEQ 787 832 GPSATNLIIGSIAGAILVAAIVLGGTGWGFKNVKKRRFDPT FT QQGPI -> EMSRREGSILLSKAPSESAALDGHRLALLDSG FT YDILAAVLLELLSL (in isoform Gamma). FT /FTId=VSP_012045. FT VAR_SEQ 787 817 GPSATNLIIGSIAGAILVAAIVLGGTGWGFK -> VNMATS FT RLIGAVAGTLLALGVIFGGTGWGIE (in isoform FT Beta). FT /FTId=VSP_012046. FT MUTAGEN 566 566 E->A: Significantly lower of adhesion- FT promoting activity. SQ SEQUENCE 832 AA; 91926 MW; 7841A9670E1C24EF CRC64; MKPPGSSSRQ PPLAGCSLAG ASCGPQRGPA GSVPASAPAR TPPCRLLLVL LLLPPLAASS RPRAWGAAAP SAPHWNETAE KNLGVLADED NTLQQNSSSN ISYSNAMQKE ITLPSRLIYY INQDSESPYH VLDTKARHQQ KHNKAVHLAQ ASFQIEAFGS KFILDLILNN GLLSSDYVEI HYENGKPQYS KGGEHCYYHG SIRGVKDSKV ALSTCNGLHG MFEDDTFVYM IEPLELVHDE KSTGRPHIIQ KTLAGQYSKQ MKNLTMERGD QWPFLSELQW LKRRKRAVNP SRGIFEEMKY LELMIVNDHK TYKKHRSSHA HTNNFAKSVV NLVDSIYKEQ LNTRVVLVAV ETWTEKDQID ITTNPVQMLH EFSKYRQRIK QHADAVHLIS RVTFHYKRSS LSYFGGVCSR TRGVGVNEYG LPMAVAQVLS QSLAQNLGIQ WEPSSRKPKC DCTESWGGCI MEETGVSHSR KFSKCSILEY RDFLQRGGGA CLFNRPTKLF EPTECGNGYV EAGEECDCGF HVECYGLCCK KCSLSNGAHC SDGPCCNNTS CLFQPRGYEC RDAVNECDIT EYCTGDSGQC PPNLHKQDGY ACNQNQGRCY NGECKTRDNQ CQYIWGTKAA GSDKFCYEKL NTEGTEKGNC GKDGDRWIQC SKHDVFCGFL LCTNLTRAPR IGQLQGEIIP TSFYHQGRVI DCSGAHVVLD DDTDVGYVED GTPCGPSMMC LDRKCLQIQA LNMSSCPLDS KGKVCSGHGV CSNEATCICD FTWAGTDCSI RDPVRNLHPP KDEGPKGPSA TNLIIGSIAG AILVAAIVLG GTGWGFKNVK KRRFDPTQQG PI //