ID Q7KAJ2_DROME Unreviewed; 2285 AA. AC Q7KAJ2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 02-OCT-2024, entry version 127. DE SubName: Full=Kakapo {ECO:0000313|EMBL:CAA09870.1}; DE Flags: Fragment; GN Name=shot {ECO:0000313|FlyBase:FBgn0013733}; GN Synonyms=kak {ECO:0000313|EMBL:CAA09870.1}; GN ORFNames=CG18076 {ECO:0000313|FlyBase:FBgn0013733}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAA09870.1}; RN [1] {ECO:0000313|EMBL:CAA09870.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Embryonic and imaginal disc {ECO:0000313|EMBL:CAA09870.1}; RX PubMed=9832555; DOI=10.1083/jcb.143.5.1271; RA Gregory S.L., Brown N.H.; RT "kakapo, a gene required for adhesion between and within cell layers in RT Drosophila, encodes a large cytoskeletal linker protein related to plectin RT and dystrophin."; RL J. Cell Biol. 143:1271-1282(1998). 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; AJ011925; CAA09870.1; -; mRNA. DR PeptideAtlas; Q7KAJ2; -. DR AGR; FB:FBgn0013733; -. DR FlyBase; FBgn0013733; shot. DR VEuPathDB; VectorBase:FBgn0013733; -. DR ChiTaRS; shot; fly. DR ExpressionAtlas; Q7KAJ2; baseline and differential. DR GO; GO:0005912; C:adherens junction; IDA:FlyBase. DR GO; GO:0000235; C:astral microtubule; IDA:FlyBase. DR GO; GO:0044295; C:axonal growth cone; IDA:FlyBase. DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase. DR GO; GO:0005856; C:cytoskeleton; NAS:FlyBase. DR GO; GO:0030175; C:filopodium; IDA:FlyBase. DR GO; GO:0045169; C:fusome; IDA:FlyBase. DR GO; GO:0030426; C:growth cone; IDA:FlyBase. DR GO; GO:0030056; C:hemidesmosome; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; IDA:FlyBase. DR GO; GO:0035371; C:microtubule plus-end; IDA:FlyBase. DR GO; GO:0005927; C:muscle tendon junction; IDA:FlyBase. DR GO; GO:0003779; F:actin binding; TAS:FlyBase. DR GO; GO:0008017; F:microtubule binding; TAS:FlyBase. DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central. DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:FlyBase. DR GO; GO:0016199; P:axon midline choice point recognition; IMP:FlyBase. DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase. DR GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase. DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central. DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase. DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IBA:GO_Central. DR GO; GO:0035149; P:lumen formation, open tracheal system; IMP:FlyBase. DR GO; GO:0001578; P:microtubule bundle formation; IMP:FlyBase. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:FlyBase. DR GO; GO:0007017; P:microtubule-based process; NAS:FlyBase. DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase. DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:FlyBase. DR GO; GO:0030716; P:oocyte fate determination; IMP:FlyBase. DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase. DR GO; GO:0045773; P:positive regulation of axon extension; IMP:FlyBase. DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:FlyBase. DR GO; GO:0030516; P:regulation of axon extension; IMP:FlyBase. DR GO; GO:0042060; P:wound healing; IBA:GO_Central. DR CDD; cd21188; CH_PLEC-like_rpt1; 1. DR CDD; cd21189; CH_PLEC-like_rpt2; 1. DR CDD; cd00176; SPEC; 4. DR Gene3D; 1.20.58.60; -; 11. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR Gene3D; 3.90.1290.10; Plakin repeat; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR041615; Desmoplakin_SH3. DR InterPro; IPR049538; PCN-like_spectrin-like_rpt. DR InterPro; IPR043197; Plakin. DR InterPro; IPR035915; Plakin_repeat_sf. DR InterPro; IPR001101; Plectin_repeat. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR002017; Spectrin_repeat. DR PANTHER; PTHR23169; ENVOPLAKIN; 1. DR PANTHER; PTHR23169:SF23; SHORT STOP, ISOFORM H; 1. DR Pfam; PF00307; CH; 2. DR Pfam; PF17902; SH3_10; 1. DR Pfam; PF00435; Spectrin; 3. DR Pfam; PF21019; Spectrin_3; 1. DR Pfam; PF21020; Spectrin_4; 1. DR SMART; SM00033; CH; 2. DR SMART; SM00250; PLEC; 2. DR SMART; SM00150; SPEC; 14. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF75399; Plakin repeat; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR SUPFAM; SSF46966; Spectrin repeat; 13. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS50021; CH; 2. DR PROSITE; PS50002; SH3; 1. PE 2: Evidence at transcript level; KW Actin-binding {ECO:0000256|ARBA:ARBA00023203}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Microtubule {ECO:0000256|ARBA:ARBA00022701}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}. FT DOMAIN 37..140 FT /note="Calponin-homology (CH)" FT /evidence="ECO:0000259|PROSITE:PS50021" FT DOMAIN 152..257 FT /note="Calponin-homology (CH)" FT /evidence="ECO:0000259|PROSITE:PS50021" FT DOMAIN 803..861 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT REGION 2176..2240 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 368..452 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 943..970 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1855..1882 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1994..2021 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 2212..2240 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 2285 FT /evidence="ECO:0000313|EMBL:CAA09870.1" SQ SEQUENCE 2285 AA; 262581 MW; 9803A2D0EE51B264 CRC64; MMDRESLSEW AKDKPLSILQ LDPADRAVLR IADERDAIQK KTFTKWVNKH LKKANRRVVD LFEDLRDGHN LLSLLEVLSG EHLPREKGKM RFHMLQNAQM ALDFLRYKKI KLVNIRAEDI VDGNPKLTLG LIWTIILHFQ ISDIVVGKED NVSAREALLR WARRSTARYP GVRVNDFTSS WRDGLAFSAL VHRNRPDLLD WRKARNDRPR ERLETAFHIV EKEYGVTRLL DPEDVDTNEP DEKSLITYIS SLYDVFPEPP SIHPLFDMES QRRVHEYRDL AQQFIYWCHE KTAYLQERSF PPTLIEMKRL LSDLQRFRSD EVSARKREKS KLIQIYKELE RYFETVGEVD VEAELRPDAI EKAWYRMNTA LQDREVILQQ EIERLERLQR LADKVQREIK HVDQKLTDLE ARIGEEGRRI ERLHPVDAKS IVEALETEIR HLEEPIQDMN QDCHVLNEGR YPHVSELHKK VNKLHQRWAQ LRTNFHTNLV QKLSGLKYPV HETTVTRQTR MVVESRQIDT NPHFRDLQEH IEWCQNKLKQ LLAADYGSDL PSVKEELDRQ QHEHKIIDQF HTKILNDERQ QTKFSGDELA LYQQRLNQLQ KVYAELLSTS TKRLSDLDSL QHFLGQASAE LQWLNEKEQV EITRDWADKQ LDLPSVHRYY ENLMSELEKR EMHFATILDR GEALLNQQHP ASKCIEAHLT ALQQQWAWLL QLTLCLEVHL KHATEYHQFF GEIKDAEQWL AKRDEILNSK FSQSDFGLDQ GETLLRGMQD LREELNAFGE TVATLQRRAQ TVVPLNKRRQ PVNRQGPVQA ICAYKQQGQL QIEKGETVTL LDNSGRVKWR VRTAKGQEGP IPGACLLLPP PDQEAIDAAE RLKRLFDRSV ALWQKKHLRL RQNMIFATIR VVKGWDFDQF LAMGPEQRTA IRRALNDDAD KLLSEGDPND PQLRRLRREM DEVNRLFDEF EKRARAEEES KQASRIFTEE CLSIKSKLED MARELDQIIL APLPRDLDSL EHVLEIHSDY ERRLHLLEPE LKHLQETFRT IALKTPVLKK SLDNLMELWK ELNTQSGLHK DRLKLLEASL AGLEDNEHVI SELENELARH QDLPSTAEGL QQVFKQLNHM QDIITQQQPQ MDKMNDAADQ LGRMGVPTKV LGDLKRLHSN VERLNTRWSA VCNQLGERMR SCETAIGLMK NLQSSVQVEE SWVDGTTERL SAMPTATSAY ELDKLLGAAI ERKPKIENVN VAGGRLIREA KIYDSKCLRF VDWLVEARPS FSPPRRDLRP ADSDPGATQY YSQRLDNLNT KYDRLLEQLS QRLKTAIEVN GSDGLQYAES LQKPLKTFRV DFSAGSLPTG DGYAARQEDL YTTTYSTTQI SSTKTTKSST KSVYSSDGLD AASQDVSTAS LPQSQIQFNE IRTLKRSQQL GGHSVLDIAG IRDPRTGRVL TIGEAIQLRI LDVRTGEMLV GDRRITLEQA ADQGLIDLQL AKQLLEPGAG RDASGRELSL LEVIQREISE AESGYETAEK RIKQAVFEKF NMCEENVNDL LKWVTTVEQK ISSVGGPREK IDELRNQINA LKQIKDEIES QQRPVATCLE QIRQIVLTGG DVLSAPEVTT LENSGRELRS RVDRVNDRTV RLLRRLEAGR DELTKLRSEL DVFSDWLQVA RRTLEDKERS LSDLTRLPSQ ADSVREFVSD VIGHQADLRF ITMAAQKFVD ESKEFLAILN DFRTSLPERL PHVEPLSSAE SPIRQEVSLV SAQYKDLLNR VNALQDRVSG LGGRQREYQD ALDKANEWLR SVHPRVSRII SEPIAGDPKG VQDQMNEAKA LHNELLSSGR LVDNAQQALD NLLRSLGGQL SPMEINQLEL PIADLKNNYQ QLLDNLGEHC KTLDKTLVQS QGVQDALDSL VGWVNQAEDK FKMNLRPASL IKERLQEQIR EHKVLLADLQ SHQASIDSVQ VSAKHLLASA SNARIAKKVE SNLNDVTGKF EKLYEKANKR GEFLDDVYNR LSRYLDEIST VEQRMASLQE ALDSRETSLL STEELARRMN ELSRDKDQLA PQFEDCVRSG KDLISLRDVT DTGVLRDRIK ALESQWRNIN ISIDERAKLS KQKAEQQLAY EGLKDQVLSW LASTEARVNG LPPVAIDLDR IKQQHDELKP ICKDYRDYAP TIDKINDIGA QYDALIRPES PARKRSTYSP IKRTSPLRRM SGDARSPSPT KGGILSPLST GSSGFGSRRS SQDGFQLSEL SPVQQQLSEI NNRYGLIGVR LNDRQHELDN LNEELRKQYE NLKGL //