ID ADNP_MOUSE Reviewed; 1108 AA. AC Q9Z103; A2BDX0; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2015, sequence version 2. DT 08-JUN-2016, entry version 132. 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; Mus. OX NCBI_TaxID=10090; RN [1] 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 281-1108, AND SYNTHESIS OF 354-361. RC TISSUE=Brain; RX PubMed=10037502; 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). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-959, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-708; SER-737; SER-888; RP SER-904; SER-959 AND SER-1077, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis; 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: 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 {ECO:0000255|PROSITE- CC ProRule:PRU00108}. 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 -!- 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 9 C2H2-type zinc fingers. CC {ECO:0000255|PROSITE-ProRule:PRU00042}. CC -!- SIMILARITY: Contains 1 homeobox DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00108}. 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; BX005039; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF068198; AAD19843.1; -; mRNA. DR CCDS; CCDS38342.1; -. DR RefSeq; NP_001297015.1; NM_001310086.1. DR RefSeq; NP_033758.2; NM_009628.3. DR UniGene; Mm.201322; -. DR ProteinModelPortal; Q9Z103; -. DR IntAct; Q9Z103; 1. DR MINT; MINT-4087285; -. DR STRING; 10090.ENSMUSP00000056809; -. DR iPTMnet; Q9Z103; -. DR PhosphoSite; Q9Z103; -. DR EPD; Q9Z103; -. DR MaxQB; Q9Z103; -. DR PaxDb; Q9Z103; -. DR PRIDE; Q9Z103; -. DR DNASU; 11538; -. DR Ensembl; ENSMUST00000057793; ENSMUSP00000056809; ENSMUSG00000051149. DR Ensembl; ENSMUST00000088001; ENSMUSP00000085316; ENSMUSG00000051149. DR GeneID; 11538; -. DR KEGG; mmu:11538; -. DR UCSC; uc008oaq.1; mouse. DR CTD; 23394; -. DR MGI; MGI:1338758; Adnp. DR eggNOG; ENOG410IIIX; Eukaryota. DR eggNOG; ENOG410XYDF; LUCA. DR GeneTree; ENSGT00530000063631; -. DR HOGENOM; HOG000232088; -. DR HOVERGEN; HBG024319; -. DR InParanoid; Q9Z103; -. DR OMA; STGVNMM; -. DR OrthoDB; EOG7GJ6C7; -. DR PhylomeDB; Q9Z103; -. DR TreeFam; TF328818; -. DR ChiTaRS; Adnp; mouse. DR PRO; PR:Q9Z103; -. DR Proteomes; UP000000589; Chromosome 2. DR Bgee; Q9Z103; -. DR CleanEx; MM_ADNP; -. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0005615; C:extracellular space; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IC:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0005507; F:copper ion binding; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0042277; F:peptide binding; IEA:Ensembl. DR GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl. DR GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl. DR GO; GO:0044849; P:estrous cycle; IEA:Ensembl. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI. DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl. DR GO; GO:0050805; P:negative regulation of synaptic transmission; IEA:Ensembl. DR GO; GO:0033484; P:nitric oxide homeostasis; IEA:Ensembl. DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl. DR GO; GO:0030828; P:positive regulation of cGMP biosynthetic process; IEA:Ensembl. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl. DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl. DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; IEA:Ensembl. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0009743; P:response to carbohydrate; IEA:Ensembl. DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl. DR GO; GO:0007614; P:short-term memory; IEA:Ensembl. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR001356; Homeobox_dom. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR007087; Znf_C2H2. DR InterPro; IPR015880; Znf_C2H2-like. DR Pfam; PF00046; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00355; ZnF_C2H2; 8. DR SUPFAM; SSF46689; SSF46689; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; DNA-binding; Homeobox; KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1 1108 Activity-dependent neuroprotector FT homeobox protein. FT /FTId=PRO_0000048808. FT ZN_FING 74 97 C2H2-type 1; degenerate. FT {ECO:0000255|PROSITE-ProRule:PRU00042}. FT ZN_FING 107 129 C2H2-type 2; degenerate. FT {ECO:0000255|PROSITE-ProRule:PRU00042}. FT ZN_FING 165 188 C2H2-type 3; degenerate. FT {ECO:0000255|PROSITE-ProRule:PRU00042}. FT ZN_FING 221 244 C2H2-type 4; degenerate. FT {ECO:0000255|PROSITE-ProRule:PRU00042}. FT ZN_FING 446 468 C2H2-type 5; atypical. FT {ECO:0000255|PROSITE-ProRule:PRU00042}. FT ZN_FING 488 509 C2H2-type 6. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 511 534 C2H2-type 7. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 621 646 C2H2-type 8; atypical. FT {ECO:0000255|PROSITE-ProRule:PRU00042}. FT ZN_FING 661 685 C2H2-type 9; atypical. FT {ECO:0000255|PROSITE-ProRule:PRU00042}. FT DNA_BIND 753 813 Homeobox. {ECO:0000255|PROSITE- FT ProRule:PRU00108}. FT REGION 354 361 Neuroprotective peptide. FT {ECO:0000269|PubMed:10037502}. FT COMPBIAS 879 950 Glu-rich. FT MOD_RES 98 98 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9H2P0}. FT MOD_RES 408 408 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9H2P0}. FT MOD_RES 412 412 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9H2P0}. FT MOD_RES 708 708 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 737 737 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 804 804 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9H2P0}. FT MOD_RES 875 875 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9H2P0}. FT MOD_RES 877 877 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9H2P0}. FT MOD_RES 885 885 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9JKL8}. FT MOD_RES 888 888 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 904 904 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 959 959 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 961 961 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9H2P0}. FT MOD_RES 1041 1041 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:Q9H2P0}. FT MOD_RES 1048 1048 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9H2P0}. FT MOD_RES 1077 1077 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT CROSSLNK 144 144 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q9H2P0}. FT CROSSLNK 266 266 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q9H2P0}. FT CROSSLNK 279 279 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q9H2P0}. FT CROSSLNK 367 367 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q9H2P0}. FT CROSSLNK 407 407 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q9H2P0}. FT CROSSLNK 426 426 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q9H2P0}. FT CROSSLNK 599 599 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q9H2P0}. FT CROSSLNK 605 605 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q9H2P0}. FT CROSSLNK 620 620 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q9H2P0}. FT CROSSLNK 715 715 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q9H2P0}. FT CROSSLNK 730 730 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q9H2P0}. FT CROSSLNK 928 928 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q9H2P0}. FT CROSSLNK 1041 1041 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. FT {ECO:0000250|UniProtKB:Q9H2P0}. SQ SEQUENCE 1108 AA; 124308 MW; C69498C5DFC9150B CRC64; MFQLPVNNLG SLRKARKTVK KILSDIGLEY CKEHIEDFKQ FEPNDFYLKN TTWEDVGLWD PSLTKNQDYR TKPFCCSACP FSSKFFSAYK SHFRNVHSED FENRILLNCP YCTFNADKKT LETHIKIFHA PNSSAPSSSL STFKDKNKND GLKPKQADNV EQAVYYCKKC TYRDPLYEIV RKHIYREHFQ HVAAPYIAKA GEKSLNGAVS LGTNAREECN IHCKRCLFMP KSYEALVQHV IEDHERIGYQ VTAMIGHTNV VVPRAKPLML IAPKPQDKKG 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 //