ID G3TCP0_LOXAF Unreviewed; 1764 AA.
AC G3TCP0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Kinase D interacting substrate 220 {ECO:0000313|Ensembl:ENSLAFP00000011847.4};
GN Name=KIDINS220 {ECO:0000313|Ensembl:ENSLAFP00000011847.4};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000011847.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000011847.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000011847.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000011847.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000011847.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 9785.ENSLAFP00000011847; -.
DR Ensembl; ENSLAFT00000014146.4; ENSLAFP00000011847.4; ENSLAFG00000014141.4.
DR eggNOG; KOG0502; Eukaryota.
DR GeneTree; ENSGT00940000156714; -.
DR HOGENOM; CLU_001438_2_0_1; -.
DR InParanoid; G3TCP0; -.
DR OMA; TGHDYLK; -.
DR TreeFam; TF344032; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011646; KAP_P-loop.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR24116; KINASE D-INTERACTING SUBSTRATE OF 220 KDA; 1.
DR PANTHER; PTHR24116:SF0; KINASE D-INTERACTING SUBSTRATE OF 220 KDA; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF07693; KAP_NTPase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 11.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 9.
DR PROSITE; PS50088; ANK_REPEAT; 10.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 497..518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 524..545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 655..680
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 37..69
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 70..102
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 103..135
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 136..168
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 169..201
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 202..234
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 235..267
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 268..300
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 334..366
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 367..390
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 440..952
FT /note="KAP NTPase"
FT /evidence="ECO:0000259|Pfam:PF07693"
FT REGION 1164..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1571..1626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1706..1764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1524..1558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1706..1750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1764 AA; 196265 MW; E68E5061273F5275 CRC64;
MSVLISQSVI NYVEEENIPA LKALLEKCKD VDERNECGQT PLMIAAEQGN LEIVKELIKN
GANCNLEDLD NWTALISASK EGHVHIVEEL LKCGVNLEHR DMGGWTALMW ACYKGRTDVV
QLLLSHGANP SVTGLYSVYP IIWAAGRGHA DIVHLLLQNG AKVNCSDKYG TTPLVWAARK
GHLECVKHLL AMGADVDQEG ANSMTALIVA VKGGYTQSVK EILKRNPNVN LTDKDGNTAL
MIASKEGHTE IVQDLLDAGT YVNIPDRSGD TVLIGAVRGG HVEIVRALLQ KYADIDIRGQ
DNKTALYWAV EKGNATMVRD ILQCNPDTET CTKDGETPLI KATKMRNIEV VELLLDKGAK
VSAVDKKGDT PLHIAIRGRS RKLAELLLRN PKDGRLLYRP NKSGETPYNI DCSHQKSILT
QIFGARHLSP TETDGDMLGY DLYSSALADI LSEPTMQPPI CVGLYAQWGS GKSFLLKKLE
DEMKTFAGQQ IEPLFQFSWL IVFLTLLLCG GFGLLFAFTV DPNLGIAVSL SLLALLHIFF
IVIYFGGRRE GESWNWAWVL STRLARHIGY LELLLKLMFV NPPELPEQTT KALPVRFLFT
DYNRLSSVGG ETSMAEMIAT LSDACEREFG FLATRLFRVF KTEDSQGKKK WKKTCCLPSF
VIFLFIFVCI IAGVTLLAIF RVDSKHLTVI FVVICVTSCS QLKFRSLQGS SYSVIYRSLL
RSFRWNHNWQ LVFKKKKKDF FVQVLKCEVE LMARMAKTID GFTQNQTRLV VIIDGLDACE
QDKVLQMLDT VRVLFSKGPF IAIFASDPHI IIKAINQNLN SVLRDSNING HDYMRNIVHL
PVFLNSRGLS NARKFLVTSA TNGDVPCSDP TVIQEDADRR VSQNSLGEVT KLGSKTALNR
RDTYRRRQIQ RTITRQMSFD LTKLLVTEDW FSDISPQTMR RLLNIVSVTG RLLRANQISF
NWDRLASWIN LTEQWPYRTS WLILYLEETE GVPDQMTLKT IYERISKNIP TTKDVEPLLE
IDGDIRNFEV FLSSRTPVLV ARDVKTFLPC TVNLDPKLRE IIADVRAARE QINIGGLAYP
PLPLHEAPPR PPSGYSQPPS VCSSSTSFNG PFGGGVVSPQ PHSSYYSGMT GPQHPFYNRP
FFAPYLYTPR YYPGSSHHLI SRPSVKTSLP RDQNNGLPCD CGSNRQRQGS GPASGPLISL
NSMNVDAVCE KLRQIEGLDQ SVLPQYCATI KKANINGRVL AQCNIDELKK EMNMNFGDWH
LFRSTVLEMR NAENQVVPED PRLLSENSSG PVPHGESARR ASHNELPHTE LSSQTPYTLN
FSFEELNTLG LDEGAPRHSN LSWQSQTRRT PSLSSLNSQD SSIEISKLTD KVQAEYRDAY
REYIAQMSQL EGGTGPTTIS GRSSPHSTYY MGQSSSGGSI HSNLEQEKGK DSEPKQDDGR
KSFLMKRGDV IDYSSSGVST NDASPLDPIT EEDEKSDQSG SKLLPSKKSS ERSSLFQTDL
KLKGGGLRYQ KLPSDEDESG TEESDNTPLL KDDKDKKAEG KVERTSKSPE HSAEPIRTLI
KAKEYLSDAL LDKKDSSDSG VRSSESSPNH SLHNEAADDS QLEKANLIEL EDDSHSGKRG
IPHSLSGLQD PVLARMSICS EDKKSPSECS LIASSPEENW PTCQKAYNLN RTPSTMTLNN
NSAPANRANQ NFDEMEGIRD TSQAILRPGS SSNPTVIQNE NLKSVTHKRS QRSSYTRLAK
DSSELHAAVS SDSTAFGEER ESIL
//