ID A0A3P6USJ0_LITSI Unreviewed; 1636 AA.
AC A0A3P6USJ0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=TOG domain-containing protein {ECO:0000259|SMART:SM01349};
GN ORFNames=NLS_LOCUS4889 {ECO:0000313|EMBL:VDK80391.1};
OS Litomosoides sigmodontis (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX NCBI_TaxID=42156 {ECO:0000313|EMBL:VDK80391.1, ECO:0000313|Proteomes:UP000277928};
RN [1] {ECO:0000313|EMBL:VDK80391.1, ECO:0000313|Proteomes:UP000277928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the TOG/XMAP215 family.
CC {ECO:0000256|ARBA:ARBA00025722}.
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; UYRX01000335; VDK80391.1; -; Genomic_DNA.
DR STRING; 42156.A0A3P6USJ0; -.
DR Proteomes; UP000277928; Unassembled WGS sequence.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0099080; C:supramolecular complex; IEA:UniProt.
DR GO; GO:0061863; F:microtubule plus end polymerase; IEA:InterPro.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IEA:InterPro.
DR GO; GO:0046785; P:microtubule polymerization; IEA:InterPro.
DR GO; GO:0007051; P:spindle organization; IEA:InterPro.
DR CDD; cd10428; LFG_like; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006214; Bax_inhibitor_1-related.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR045110; XMAP215.
DR InterPro; IPR048491; XMAP215_CLASP_TOG.
DR PANTHER; PTHR12609:SF0; CYTOSKELETON-ASSOCIATED PROTEIN 5; 1.
DR PANTHER; PTHR12609; MICROTUBULE ASSOCIATED PROTEIN XMAP215; 1.
DR Pfam; PF01027; Bax1-I; 1.
DR Pfam; PF21041; XMAP215_CLASP_TOG; 2.
DR SMART; SM01349; TOG; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000277928};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1316..1333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1426..1447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1459..1477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1489..1506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1512..1532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1544..1568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1574..1597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1609..1631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..238
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REPEAT 173..207
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 355..592
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 250..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1312
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1636 AA; 182943 MW; 7FFA3D4CFDBADAA2 CRC64;
MLDPVDVLAK LPGNFMEGID SKKWVDRRDA LQSLLVLCTE NPKLCPKANY GEFVALLKKI
LEKDANINVC ALAARCLTAF ATGLRKKFAQ HATVVAPTIF EKFKEKKPVL RDPLIDCIDA
VAASTTLEVL AEDIQTALDK QNPHIKIQTN LFLYRIFKRH NPQTVPKKVL KSLAPIIVKL
TGDSDPEVRD ASYAALGAVM KAVGEKSCMI LLADIAEDKV KITKIRDFCE KAVQEAGTDV
VSIMVQSMHK SNPENGTGAG GDNSNSASPL KPPAPGVGNS NVGGSAHSKE IIKEDSTEGK
LLKSSKKEVE ATKENEESMK RKDEFLVINK DKGARLKDER NLRVLKWNFD QPGLEHVEQL
KTLLGNVTQA SLLTYLFNKD FKQQLKGIDM LQSLVTDCPE SLISNSDLLL KWISLRFFET
NPTILLKVLD LTQGIFNLLL QYNEPFSEQE MYSFVPYLLI KLGEAKDSVR TPVRTIIQLV
TELISPPKIF PLVIEGLKTK NSRQRTECLQ VLEQLLDTTG MAATTTPALS LKQIAACIDD
RDNNVRNAAI NAIVVAWKEE GDRVFQLIGK MNDKSKAMLD ERIKRSGVVS KARGGPERIA
ASAKRANISV GVKGRTLRSN RSLSRMGRNT HRSSSISRDS SPVDEKENNR TFTMQGESVE
RCDDNDGTRK RFALNLDLLK LDNNDAAVEY PEVDINALEM LEPIEPAIRK RKHPPQYSDR
AESVSSLTSL ESAAGDVDKV VHGVASMSQA TATAAISQLQ FLFGDPSNFR YVADRTDAVV
QAIVTQSSII RSRHLDDVGT FDELNELVRT ICHFLSSLIK ETTTCSRISS EALKMLIQEF
LYLLKDERME QLKDIQSIFR SLNYLSIRIC DNADPTACFL ALCSMLTSAL HDPRNKTVEL
INKASIICIY KQSELFLRDV PMNLDEIVKA IHIFMQEFRP RVDESKNIKN SMHSMELCIQ
RLVAGTKASV MQHIGEILNP DSSEAVIYMR KCVRGLQNRS NQNSLASSMC GELPGQVPSS
NHEESVRNLI SKIIENPFGK GLRLLHTFLK LNPDARKILE EELRKQFRMR DFIALHLKKM
DLGDRETPEV TDELYNVVSE ICDELYSFKV MESIRAHREA LCSYRQTGWW TGNTASSLIT
STDENAKPVA AHRLHNILCH NFHYILIRPL LEGAPENEPV TPVHAKPKLT AIDVEPLKQL
LNMRRQQQAE WSSGMILASG ARGPGFDHRL SPPPLKLWLV NVAILPSTSG GIHHWTVYFD
FIDLPNEHKI IQECVKCFAV VKDITSCCVN DDKSDCDSDN NTDNDDGDDD DDDDDVARNL
SFIFFLLIPT LYLRKNKAMA QHYGYAGQPP YQYPGYQNGS NPYQQGPPYQ HAPPYNQPPP
AGFNPQVFMP PPPIHPGIDA YVEGGGMKSD FGFNSASVRA AFVRKVFTLV GIMLTVVTLM
TAIPFFHQET MKFVRTTPSM YFASYMIFLI VYFTLMCCEG VRRSFPGNLI ALSILTLSIG
YMTMMFCSYH KAVSVLLCLA ITVVCCGGVI LFSSQTKHDL TSMYGMLFIV SMVLLVFGII
AIIAAVAFHV TWLYTVYAGF AALLFMVYLA VDVQTIMGGR KHEISPEDYI FAAVQVFLDI
VYIFWMLLTL FGSDRS
//
