ID ADNP_MOUSE Reviewed; 828 AA. AC Q9Z103; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-OCT-2009, entry version 75. DE RecName: Full=Activity-dependent neuroprotector homeobox protein; DE AltName: Full=Activity-dependent neuroprotective protein; GN Name=Adnp; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND SYNTHESIS OF 74-81. RC TISSUE=Brain; RX MEDLINE=99155106; PubMed=10037502; RX DOI=10.1046/j.1471-4159.1999.0721283.x; RA Bassan M., Zamostiano R., Davidson A., Pinhasov A., Giladi E., RA Perl O., Bassan H., Blat C., Gibney G., Glazner G., Brenneman D.E., RA Gozes I.; RT "Complete sequence of a novel protein containing a femtomolar- RT activity-dependent neuroprotective peptide."; RL J. Neurochem. 72:1283-1293(1999). CC -!- FUNCTION: Potential transcription factor. May mediate some of the CC neuroprotective peptide VIP-associated effects involving normal CC growth and cancer proliferation. CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- TISSUE SPECIFICITY: Expressed in the brain, with a higher CC expression in cerebellum and hippocampus. Weakly expressed in CC lung, kidney and intestine, and expressed at intermediate level in CC testis. CC -!- INDUCTION: By the neuroprotective peptide VIP. CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By CC similarity). CC -!- MISCELLANEOUS: When isolated from the sequence, the CC neuroprotective peptide provides neuroprotection at subfemtomolar CC concentrations against toxicity associated with tetrodoxin CC (electrical blockade), the beta-amyloid peptide (the Alzheimer CC disease neurotoxin), N-methyl-aspartate (excitotoxicity), and the CC human immunideficiency virus (HIV) envelope protein. CC -!- SIMILARITY: Contains 5 C2H2-type zinc fingers. CC -!- SIMILARITY: Contains 1 homeobox DNA-binding domain. 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; AF068198; AAD19843.1; -; mRNA. DR IPI; IPI00672180; -. DR UniGene; Mm.201322; -. DR STRING; Q9Z103; -. DR PhosphoSite; Q9Z103; -. DR PRIDE; Q9Z103; -. DR Ensembl; ENSMUST00000057793; ENSMUSP00000056809; ENSMUSG00000051149; Mus musculus. DR Ensembl; ENSMUST00000088001; ENSMUSP00000085316; ENSMUSG00000051149; Mus musculus. DR Ensembl; ENSMUST00000109196; ENSMUSP00000104819; ENSMUSG00000051149; Mus musculus. DR MGI; MGI:1338758; Adnp. DR HOVERGEN; Q9Z103; -. DR ArrayExpress; Q9Z103; -. DR Bgee; Q9Z103; -. DR CleanEx; MM_ADNP; -. DR Genevestigator; Q9Z103; -. DR GermOnline; ENSMUSG00000051149; Mus musculus. DR GO; GO:0005615; C:extracellular space; IDA:MGI. DR GO; GO:0005634; C:nucleus; IC:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0005515; F:protein binding; IPI:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0043524; P:negative regulation of neuron apoptosis; IDA:MGI. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR007087; Znf_C2H2. DR InterPro; IPR015880; Znf_C2H2-like. DR Pfam; PF00046; Homeobox; 1. DR Pfam; PF00096; zf-C2H2; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00355; ZnF_C2H2; 4. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. PE 2: Evidence at transcript level; KW Acetylation; DNA-binding; Homeobox; Metal-binding; Nucleus; KW Phosphoprotein; Repeat; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1 828 Activity-dependent neuroprotector FT homeobox protein. FT /FTId=PRO_0000048808. FT ZN_FING 166 188 C2H2-type 1; atypical. FT ZN_FING 208 229 C2H2-type 2. FT ZN_FING 231 254 C2H2-type 3. FT ZN_FING 341 366 C2H2-type 4; atypical. FT ZN_FING 381 405 C2H2-type 5; atypical. FT DNA_BIND 473 533 Homeobox. FT REGION 74 81 Neuroprotective peptide. FT COMPBIAS 599 670 Glu-rich. FT MOD_RES 128 128 Phosphoserine (By similarity). FT MOD_RES 132 132 Phosphoserine (By similarity). FT MOD_RES 428 428 Phosphoserine (By similarity). FT MOD_RES 595 595 Phosphoserine (By similarity). FT MOD_RES 597 597 Phosphoserine (By similarity). FT MOD_RES 679 679 Phosphoserine (By similarity). FT MOD_RES 681 681 Phosphoserine (By similarity). FT MOD_RES 761 761 N6-acetyllysine (By similarity). FT MOD_RES 768 768 N6-acetyllysine (By similarity). SQ SEQUENCE 828 AA; 92063 MW; 9DFE669C506E8606 CRC64; MGLPPRISSL ASGNVRSLPS QQMVNRLSIP KPNLNSTGVN MMSNVHLQQN NYGVKSVGQS YGVGQSVRLG LGGNAPVSIP QQSQSVKQLL PSGNGRSFGL GAEQRPPAAA RYSLQTANTS LPPGQVKSPS VSQSQASRVL GQSSSKPPPA ATGPPPSNHC ATQKWKICTI CNELFPENVY SVHFEKEHKA EKVPAVANYI MKIHNFTSKC LYCNRYLPTD TLLNHMLIHG LSCPYCRSTF NDVEKMAAHM RMVHIDEEMG PKTDSTLSFD LTLQQGSHTN IHLLVTTYNL RDAPAESVAY HAQNNAPVPP KPQPKVQEKA DVPVKSSPQA AVPYKKDVGK TLCPLCFSIL KGPISDALAH HLRERHQVIQ TVHPVEKKLT YKCIHCLGVY TSNMTASTIT LHLVHCRGVG KTQNGQDKTN APSRLNQSPG LAPVKRTYEQ MEFPLLKKRK LEEDADSPSC FEEKPEEPVV LALDPKGHED DSYEARKSFL TKYFNKQPYP TRREIEKLAA SLWLWKSDIA SHFSNKRKKC VRDCEKYKPG VLLGFNMKEL NKVKHEMDFD AEWLFENHDE KDSRVNASKT VDKKHNLGKE DDSFSDSFEH LEEESNGSGS PFDPVFEVEP KIPSDNLEEP VPKVIPEGAL ESEKLDQKEE EEEEEEEDGS KYETIHLTEE PAKLMHDASD SEVDQDDVVE WKDGASPSES GPGSQQISDF EDNTCEMKPG TWSDESSQSE DARSSKPAAK KKATVQDDTE QLKWKNSSYG KVEGFWSKDQ SQWENASENA ERLPNPQIEW QNSTIDSEDG EQFDSMTDGV ADPMHGSLTG VKLSSQQA //