ADNP2_MOUSE
ID ADNP2_MOUSE Reviewed; 1165 AA.
AC Q8CHC8; Q6P294; Q80VS0; Q811H5; Q8R1A2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Activity-dependent neuroprotector homeobox protein 2;
DE Short=ADNP homeobox protein 2;
DE AltName: Full=Zinc finger protein 508;
GN Name=Adnp2; Synonyms=Kiaa0863, Zfp508, Znf508;
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 [LARGE SCALE MRNA].
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Eye, Mammary tumor, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24969.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH44898.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC41452.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AB093268; BAC41452.1; ALT_INIT; mRNA.
DR EMBL; BC024969; AAH24969.1; ALT_INIT; mRNA.
DR EMBL; BC044898; AAH44898.1; ALT_INIT; mRNA.
DR EMBL; BC044904; AAH44904.1; -; mRNA.
DR EMBL; BC064672; AAH64672.1; -; mRNA.
DR CCDS; CCDS50332.1; -.
DR RefSeq; NP_778193.1; NM_175028.1.
DR RefSeq; XP_006526529.1; XM_006526466.2.
DR AlphaFoldDB; Q8CHC8; -.
DR BioGRID; 232200; 2.
DR STRING; 10090.ENSMUSP00000068560; -.
DR iPTMnet; Q8CHC8; -.
DR PhosphoSitePlus; Q8CHC8; -.
DR EPD; Q8CHC8; -.
DR MaxQB; Q8CHC8; -.
DR PaxDb; Q8CHC8; -.
DR PeptideAtlas; Q8CHC8; -.
DR PRIDE; Q8CHC8; -.
DR ProteomicsDB; 285554; -.
DR Antibodypedia; 1760; 66 antibodies from 17 providers.
DR Ensembl; ENSMUST00000066743; ENSMUSP00000068560; ENSMUSG00000053950.
DR GeneID; 240442; -.
DR KEGG; mmu:240442; -.
DR UCSC; uc008fsk.1; mouse.
DR CTD; 22850; -.
DR MGI; MGI:2448562; Adnp2.
DR VEuPathDB; HostDB:ENSMUSG00000053950; -.
DR eggNOG; ENOG502QU0M; Eukaryota.
DR GeneTree; ENSGT00530000063631; -.
DR HOGENOM; CLU_009119_1_0_1; -.
DR InParanoid; Q8CHC8; -.
DR OMA; NLDQMLH; -.
DR OrthoDB; 135860at2759; -.
DR PhylomeDB; Q8CHC8; -.
DR TreeFam; TF328818; -.
DR BioGRID-ORCS; 240442; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Adnp2; mouse.
DR PRO; PR:Q8CHC8; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8CHC8; protein.
DR Bgee; ENSMUSG00000053950; Expressed in ascending aorta and 210 other tissues.
DR Genevisible; Q8CHC8; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IDA:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR038861; ADNP/ADNP2.
DR InterPro; IPR045762; ADNP_Znf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15740; PTHR15740; 3.
DR Pfam; PF19627; ADNP_N; 3.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Homeobox; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1165
FT /note="Activity-dependent neuroprotector homeobox protein
FT 2"
FT /id="PRO_0000280417"
FT ZN_FING 73..96
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 106..128
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 155..178
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 215..240
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 696..718
FT /note="C2H2-type 5; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 724..746
FT /note="C2H2-type 6; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 777..798
FT /note="C2H2-type 7; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 800..823
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 905..935
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 1073..1132
FT /note="Homeobox"
FT REGION 303..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ32"
FT CROSSLNK 1009
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ32"
FT CROSSLNK 1048
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ32"
SQ SEQUENCE 1165 AA; 126768 MW; 6965AEF434A6FDDA CRC64;
MFQIPVQNLD NIRKVRKRVK GILVDIGLDS CKELMKDLKS FDPGEKYFYN TSWGDVSPWE
PSGKKARYRT KPYCCSLCRY STKVLTSLKN HLHRYHEDEA DQELMIPCPN CPFSSQPRVV
GKHFRMFHAP ARKVQSYTVN ILGETKTSRS DVISFTCLKC NFSNTLYYSM KKHVLVAHFN
YLINSYFGLR TEETGEQPKA SDPVSVDKIL PFDKYYCKKC SAIASSQDAL MYHILTSDAH
RDLENKLRSV ISEHIKRTGF LKQMHIAPKP VTHLALPPNS SAPSIAAPPP CFQLALPQNS
QSSGTVQSVT VTPGTSGSLT HSPPTTAQSH VALVSSSLPV CQSSLSLQQS APPPVFLSHS
VALNQPVNTA VLPLTQPVGP VNKSVGTSIL PVNQAMCSVN QAVRPGLLPL TKPMGPMNRP
VGPAVLPMGP SVNSGVLQAT SPGVISVGRA VPSGVLPAGQ VTPAGVIPGQ TATSGVLPTG
QVVQSSTLPV GQTAPSRGLP PGQTVPLRVL PAGQVVPSGL LSSNQTVPSG VVPVNQGVNS
GVLQLGQPVT PGVLPVGPPV RPGVLQLSPS VSTSILPMSQ PVRAGTSQNT TFFTSGSILR
QLIPTGKQVN GIPTYTLAPV SVTLPVPSGG GLAAVGPPPQ VPVQFLPSGS GTQMGSSLPS
LPSPQVLVSP APSVFVQATP PLADANQALK QAKQWKTCPV CNELFPSNVY QVHMEVAHKQ
SEAQLCQVCN ELFPANVYQV HMEVAHKQSE SKSSEKLEPE KLAACAPFLK WMREKTVRCL
SCKCLVSQEE LMHHLLMHGL GCLFCPCTFH DVRGLVEHSR TKHLGKKRLS MDYSNRGFQL
DLDANGNLLF PHLDFITILP REKLGEREVY LAILAGIHSK SLVPVYVKVR PQPEVAPKIP
NKQKLTCPFC LSTFMTADAY ELHLKERHHV MPTVHTMLRS PAFKCIHCCG VYTGNMTLGA
IAVHLLRCRS APKDSSSDLQ VQPGFIESSE LLMVNGDVIP ESTFPVKRKL PEGHLGPEDQ
RDGEEPQLTL DADASSGSEK GLGAVPLKRQ KSEIRTEGSG PSEDSLQALA LDPSKYEGRS
YEEKKQFLRD YFHRRPYPSR KEVELLSSLL WVWKIDVASF FGKRRYICMK AIKTHKPSVL
LGFDMSELKN VKHRLNFGEC ESQKL