ID Q3KN55_DROME Unreviewed; 697 AA. AC Q3KN55; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 02-SEP-2026, entry version 156. DE SubName: Full=RE55168p {ECO:0000313|EMBL:ABA81818.1}; GN Name=Ank2 {ECO:0000313|EMBL:ABA81818.1, GN ECO:0000313|FlyBase:FBgn0261788}; GN ORFNames=CG42734 {ECO:0000313|FlyBase:FBgn0261788}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida; OC Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota; OC Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:ABA81818.1}; RN [1] {ECO:0000313|EMBL:ABA81818.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Berkeley {ECO:0000313|EMBL:ABA81818.1}; RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J., RA Park S., Wan K., Yu C., Celniker S.; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- INTERACTION: CC Q3KN55; P17789: ttk; NbExp=4; IntAct=EBI-15122666, EBI-6173284; 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; BT023884; ABA81818.1; -; mRNA. DR RefSeq; NP_001097534.1; NM_001104064.2. DR AlphaFoldDB; Q3KN55; -. DR SMR; Q3KN55; -. DR IntAct; Q3KN55; 21. DR PeptideAtlas; Q3KN55; -. DR DNASU; 38863; -. DR GeneID; 38863; -. DR UCSC; CG34416-RE; d. melanogaster. DR AGR; FB:FBgn0261788; -. DR CTD; 287; -. DR FlyBase; FBgn0261788; Ank2. DR VEuPathDB; VectorBase:FBgn0261788; -. DR OrthoDB; 20872at2759; -. DR BioGRID-ORCS; 38863; 0 hits in 3 CRISPR screens. DR Bgee; FBgn0261788; Expressed in multidendritic neuron (Drosophila) in post-embryonic organism and 244 other cell types or tissues. DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase. DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase. DR GO; GO:0042734; C:presynaptic membrane; IDA:FlyBase. DR GO; GO:0036062; C:presynaptic periactive zone; IDA:FlyBase. DR GO; GO:0043195; C:terminal bouton; IDA:FlyBase. DR GO; GO:0048675; P:axon extension; IMP:FlyBase. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:FlyBase. DR GO; GO:1900074; P:negative regulation of neuromuscular synaptic transmission; IMP:FlyBase. DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase. DR GO; GO:0070050; P:neuron cellular homeostasis; IGI:FlyBase. DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase. DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase. DR GO; GO:0007614; P:short-term memory; IMP:FlyBase. DR FunFam; 1.25.40.20:FF:000095; Ankyrin 2, isoform J; 1. DR FunFam; 1.25.40.20:FF:000001; Ankyrin-2 isoform 2; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR PANTHER; PTHR24198; ANKYRIN REPEAT AND PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR24198:SF165; ANKYRIN REPEAT-CONTAINING PROTEIN-RELATED; 1. DR Pfam; PF00023; Ank; 1. DR Pfam; PF12796; Ank_2; 5. DR Pfam; PF13637; Ank_4; 1. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 16. DR SUPFAM; SSF48403; Ankyrin repeat; 3. DR PROSITE; PS50297; ANK_REP_REGION; 13. DR PROSITE; PS50088; ANK_REPEAT; 13. PE 1: Evidence at protein level; KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE- KW ProRule:PRU00023}; Repeat {ECO:0000256|ARBA:ARBA00022737}. FT REPEAT 193..225 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 226..258 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 259..291 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 292..314 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 354..386 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 387..419 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 420..452 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 453..485 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 486..518 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 519..551 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 552..584 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 585..617 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 618..650 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REGION 17..112 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 131..163 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 49..60 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 73..103 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 154..163 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 697 AA; 75677 MW; D01DE5A266177F1A CRC64; MAQFVTHIQP TLMEASQGHV PHHHGHQVGV QHSSHLPHSG HNMPSPPTHN HHHAHGHGHH TSSGGHHGGA GGHSQKQAAH HSTTSGHAAK GQHHSPPSRI HSPPTEHHPD HVGHYEYFQH QHEQIFHHEG ANGGASHKQQ THHHPNKHEH CPTGHQSAGD GNTSFLRAAR AGNLERVLEH LKNNIDINTS NANGLNALHL ASKDGHIHVV SELLRRGAIV DSATKKGNTA LHIASLAGQE EVVKLLLEHN ASVNVQSQNG FTPLYMAAQE NHDAVVRLLL SNGANQSLAT EDGFTPLAVA MQQGHDKVVA VLLESDTRGK VRLPALHIAA KKDDVKAATL LLDNDHNPDV TSKSGFTPLH IASHYGNQNI ANLLIQKGAD VNYSAKHNIS PLHVAAKWGK TNMVSLLLEK GGNIEAKTRD GLTPLHCAAR SGHEQVVDML LERGAPISAK TKNGLAPLHM AAQGEHVDAA RILLYHRAPV DEVTVDYLTA LHVAAHCGHV RVAKLLLDRN ADANARALNG FTPLHIACKK NRLKVVELLL RHGASISATT ESGLTPLHVA AFMGCMNIVI YLLQHDASPD VPTVRGETPL HLAARANQTD IIRILLRNGA QVDARAREQQ TPLHIASRLG NVDIVMLLLQ HGAQVDATTK DMYTALHIAA KEGQDEVKDL IAKKITDHID TVYLMQLFWI RHQEFFI //