ID   Q7KAJ2_DROME            Unreviewed;      2285 AA.
AC   Q7KAJ2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   29-MAY-2024, entry version 126.
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).
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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:0005882; C:intermediate filament; IEA:TreeGrafter.
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:0016203; P:muscle attachment; TAS: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; 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
//