ID T1JXK5_TETUR Unreviewed; 2172 AA.
AC T1JXK5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Ion transport domain-containing protein {ECO:0000259|Pfam:PF00520};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur02g12280.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur02g12280.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Target cell membrane {ECO:0000256|ARBA:ARBA00004175}.
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DR EMBL; CAEY01000829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 32264.T1JXK5; -.
DR EnsemblMetazoa; tetur02g12280.1; tetur02g12280.1; tetur02g12280.
DR eggNOG; KOG3609; Eukaryota.
DR eggNOG; KOG4177; Eukaryota.
DR HOGENOM; CLU_001375_1_0_1; -.
DR OMA; HAREDTI; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
DR GO; GO:0034703; C:cation channel complex; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0044231; C:host cell presynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0044218; C:other organism cell membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005262; F:calcium channel activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 9.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR002153; TRPC_channel.
DR PANTHER; PTHR24123; ANKYRIN REPEAT-CONTAINING; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 9.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR01097; TRNSRECEPTRP.
DR SMART; SM00248; ANK; 29.
DR SUPFAM; SSF48403; Ankyrin repeat; 4.
DR PROSITE; PS50297; ANK_REP_REGION; 20.
DR PROSITE; PS50088; ANK_REPEAT; 21.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Neurotoxin {ECO:0000256|ARBA:ARBA00022699};
KW Presynaptic neurotoxin {ECO:0000256|ARBA:ARBA00023028};
KW Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Target cell membrane {ECO:0000256|ARBA:ARBA00022537};
KW Target membrane {ECO:0000256|ARBA:ARBA00023298};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1729..1750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1762..1788
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1800..1816
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1828..1847
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1877..1895
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1916..1938
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1991..2013
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 597..629
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 630..656
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 738..770
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 771..803
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 804..827
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 871..903
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 904..936
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 938..971
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 972..1004
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1122..1154
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1155..1187
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1188..1221
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1222..1254
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1255..1287
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1325..1357
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1358..1378
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1391..1424
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1432..1454
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1467..1499
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1501..1533
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1534..1566
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1875..2027
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2172 AA; 237184 MW; 0539FE100BCAE4F9 CRC64;
MVVNQPNNNP KESSDDEDNS ERRALVNGKS NSKQLVNRRK KKKRKSSKEG KVGETNSKPS
TSSSVATVRS TEPVKVQYRS GELVSIPRAE IQFEERTIND PGDELLAVIL DGQNDSKVLI
SPISRKPAPA PKSIIDSVKF ERESVNKKGK DDEEDDENED DDKLLLSQSK PENESDSTSL
TTVSLSNNSK SSPPDDDEDD NDVNCSSQPS QSNSQSKSFL ENCVQPKMDS KKDDKQIDDS
KNRNKTFNPP NNNGDKIVNG SEETDSLGKD KTVCDPAKTI PIPLENVENN PRKGSVKDGQ
PLGKDQVTKQ QNDGKPGKSV KNVKMAGNGE SSATISGPIS VGSTKQPNVL PLPTASTTAT
TTTTKTTTST TITITGSTTP LAPTKGLPGT SKKPATSTTS VTPVTVATTS ITLNPTLLTT
TTVSTLNGDK IAILNPSQKV TQTSSTSDSK GLIMSTQESS KNTVKQDEND KSGKDKKVKI
LANEGKEKKE STAAKDAAVI ESVRSMVAGP NKDDSDSETD SMDPAKMDSP SDTKASPSSK
AKQATPKTDP GLNAKSLISP SQRLIALCRR EEWLAVDTLL HQTDPSFFDV NIVSEGNLWT
PLMFAARDNR VNVIEKLVDI GYNVNSRALD GITALHLACA HAREDTIRLL LSRGADPLIA
GGPKDQLPVH VISMKQTGAA VAPLQLLLRS TPKSMRLIPD KDGNVPLILA AECGNHGVCR
ELLTAQAKEQ LAARKPGAED GPIHIATRRK DMMLLQCFVN HGADVNMQNA YGQTPLHISS
QDGDENIVKF LHESGANANL TDREERTALH LATEHGHSRI VDLLTERFRA NVNLRTKDGN
TLMHIASRCG QPATALHFLR KGVPLHMPNK DGSKAIHMAA SRGQIEIIRQ VLKSGESIDI
KNNAGLTPLH LAVESGQDHV VELLLGFGAS VHVATTYDME TPLHVAAKTK EGATCAKLLI
KSGANVNAIE KNGETPLHIA GRSGFLDIFK LLLEAGSDAS LQNTQGENVL HIVVKEAHFA
IARVLIDYII RRDSRDVAGK LINQQNKNGE SSVHYAGSIK PNGNRESNED RALMNLLLKN
GGDVNLGTNQ NQETAVHCCS KSGNTNVLRE IICQLPPIDA QNGWTPLLYA SNSGYPEIIE
ILLQQNARVD VFDDRGRAGL HLAAELGRLD VVDILLANNA FVNVRNKTGM TPLHLAAKMG
YNEMVKHLVS KYGAHLDAMT LNKQTPLHLA AEFGQLEVCN TLIGMKADIN AMDNQAQTPL
HLAAQSDHPE VLKLFLQYRP ELVSVPNKNG FTCAHIAATK GSVAVLKELM KFNVEVVKSA
RVKKTGSTAL HMAAEGGHTK VVRLLLQAGA KASDENLEGM TPLHLGAKQG HLRVLHALKG
AVDWKICSRK TGFTALHVAA ANGQTDFVSE MLTQVPANIL SEKPLADPGA DYGITPLHLA
AQNGHESVVR LLMNSTGVQV DAPTRVHGSI PMHLAAQGGH MLVAGLLISR SGDSLMSRDR
QGRTCVHLAS ATGHRDMVAL LLGQGAEINA QDKKGWTPLH YASRHGYLSV VQLLVESGAD
PTTASKDGKV PLCNAASAGH YDVLSYLLKK EHDSLQLMDD KLFLLDLMNC SKNHDNKPIR
EFVLVSDACI DTAVKLARSY ENLAAREKER ARDLETASAY CDTIAIDLLS IAATTNNAGA
LLRATDHKNT EFLDVLIELD RKDVVSQHAV QKYLTDVWMG NLRWPGLKFV ALFFSFLVCP
IIWIIVSTPI GHRLHRIPII KFMSYLTAHI FFIVVLVYTT VFPGTALYEH EDSIPLWNEW
LLTLWLVGIA VSDMINPSDK SGLGGIKVLI LVIGFTAVAV HGITFILDEY VFDRQDMVLD
DLWHVRRLDI LYIRNQLLAV AMLLSFIEFL NFLTFHPLFG PWGVIIQELI QDLLRFLAIL
SIFLTGFTLH ICAIYQPVYR APESWNMTQI PIGQHFLKPG KSFEMLFYAL FGLVEPDTMP
PMHLSPDFAK IIMKLVFGIY MMVTVIVLIN LLIAMMSNTY QRIEAQSDIE WKFGRAKLIR
NMNRTLSTPS PINLILGLPI LAFHKIKDKL HQDKMKEMAL AKKAFGHLTH QRPSVIAARQ
LLSRKSSHMS AATQMTSHFG MSILEAAIHE SKPISEVVNW PLIVQKYYES IGVASPNTGT
DQDEIMDDAS NE
//
