ID G0RYX5_CHATD Unreviewed; 2052 AA.
AC G0RYX5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Protein BTN {ECO:0008006|Google:ProtNLM};
GN ORFNames=CTHT_0000920 {ECO:0000313|EMBL:EGS23403.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS23403.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the battenin family.
CC {ECO:0000256|ARBA:ARBA00007467}.
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DR EMBL; GL988032; EGS23403.1; -; Genomic_DNA.
DR RefSeq; XP_006690645.1; XM_006690582.1.
DR STRING; 759272.G0RYX5; -.
DR GeneID; 18254130; -.
DR KEGG; cthr:CTHT_0000920; -.
DR eggNOG; KOG3880; Eukaryota.
DR HOGENOM; CLU_001373_1_1_1; -.
DR OrthoDB; 2912995at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProt.
DR CDD; cd06174; MFS; 1.
DR InterPro; IPR003492; Battenin_disease_Cln3.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR10981; BATTENIN; 1.
DR PANTHER; PTHR10981:SF0; BATTENIN; 1.
DR Pfam; PF02487; CLN3; 1.
DR PRINTS; PR01315; BATTENIN.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
PE 3: Inferred from homology;
KW Amino-acid transport {ECO:0000256|ARBA:ARBA00022970};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 1645..1670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1691..1710
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1722..1742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1751..1771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1783..1802
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1877..1895
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1915..1933
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1945..1965
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1971..1990
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1048
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2052 AA; 219718 MW; 68369CBF80EB9E11 CRC64;
MPTARYNAVA QHDSDDDEAT PPGYTESGVM LPRTDADSPG LQDPEQPLQV AKGKPVPGPS
NVPSTMTIGS NLPYLALDEQ AFTPLSMESS EFALESQSQS LTKNQQQDAL QPTPSRTKSR
SARRPPSPPK KSPGALEAER LVRTAKSLER LRTARSMERL RRQANASAAS SSKESNSSAN
AAGRGTSPAP GTQIHVEEVV QSFEKLHKAA VSDAEKLVRS KSQGHRERPP VPPVPSTLSL
NLGSKQEQDE RGEGQRTQDP DESATADAGP AAASADQQLQ STVGEGSHQG ATPLLTGGIS
NSSGSGNAVG ARAADDNHEN ETDFRSREAV PRASNAALPD PSKDTSATAN GDRYSKLLSS
EEPDPVPQTI IAQTTLIRPT PSAPQSPVRT RTRDRAPSSP KAIRPPLVRT ASTASVTLSH
PVPDSNKLSQ AGGFLGNIAA LEATAERLAS CGDSTLEDAI REEHNELKRS ESRRSRASTY
RRTRGESISE DQQQVGTGVG VSRQSSVRST HAVTRSNMAA SGYMMSPKRL RSGSKASSTG
FSGQIPETEI TTGAGQENED GSHPPPARSS FLSRHGPGKA SVRSVASSRI SLTQIAELEP
PSAITQEALD AADRAAATGQ HDDDDDEDVL RARAHQYIED EFAEMLKDVP DQPLGVSLGL
SDFSLPPPAT SSAPTQIPGA ETGGLNFQEY RDEPFPRLQL HQPDNYQPYG ASQPLEHHLR
PATTASTYDT EAAAAQAAFD DFDGVHCDPD APDPRHSLPP SSAEHGSVRP LPTYTAYGPA
PPRPQPRLGS QQRPTSYIDP ITGQQMIYYP APVPAMLNLP PKLSKKPKAA QRNARRSQIV
SHMPQAARES RTWLPDPTEG LRETSDFSMD VLGRESEEGP VRMSGDGQTQ SDGPGVRHSV
SFSVDSTGQQ PSCYGPRQEQ PVPGPVPGVE PQNLRVPQSL KENRKSSINP HLRASAFFDL
PSTTLPKLEV KNGSAMDTLD SILDASATAP VNAFTDHVFA GKLGAEVYGP EKRKKRVKKS
TTGQTQEDKK DDEAKDKDSD EKKPKKLVKS NSAGNLLDPN QAQEKDKKRA SRFSLFTHKR
SPSSSSTSPS DDEDAHPHPQ KQDSESEYTT ETEEEPEPIY QGPPTTLLAE LQIRKQQVKN
RTRLPAHART NGMHTTLLEL DAVAEMERKA RLGKRVTLAW EDPAASKQDE ESDEDVPLGM
LYAAKVAGGA KRSSTMDISI LMSEVSRPLG LMEKRELEDN EPLSRRRERL LAGKDPSPAA
NQGLSLEMLQ KRLTLVPGAA PTGLQLRRES RLAIPGQGAS SGSNPRTSLS RPGSRAQSLV
GVAGVAPVGL GGKESEESEH EEETLAARKE RLKKANLPEP RPVSGAFSAE VLSQFAPEDK
GEKEKDPPAH SRNVSSVSAT AAAQPQTQDV PEEEETLAQR RARLQREREM AGAGGSLPRS
TTPLPSLNLN LPVPSLNLPT NTNNRHTLAP GAISASSGGL STFLTRPPSA FVMNDPREAE
RLRKEADAAR GTEWGFHGGV FNDGFAGAGS VGSINGRPVT SYYGTSAGGG MTLLQQREML
DYQQQQQQQF RPGTGTLLGQ IHPQQGIGMN MGYAGGMGLQ SGFGASTPNL AMGTGTGIGG
AGYAGNVGGG GLVGGFRKIG LINNVLYVIL LSAAQDLVGL ATPKALVLLA DVAPSFLTKL
IAPYFIHRVP YSVRIAIFVS FSLAGMLVVA SAPVKGSVPR KLFGIVLASL SSGGGELSFL
GLTHYYGHMS LAAWGSGTGA AGLAGAGLYV LLTGWLQLGV RKSLYMCAVL PFGMVVAFWG
ILPRAKLKAA GTAVVYERLA DEDGEDFGDV PPAAASSSLL SPGPAAASTA FHTPSATLTT
AKSSESFTSK LRRARSLFIP YMFPLLLVYI AEYTINQGVA PTLLFPLDKS PFTEYRAFYP
FYGFLYQLGV FISRSSTPFI RIHNLYTPSL LQVANLMLLI FHAMWDFIPS VYIIFIIIFW
EGLLGGAVYV NTFAEIMESV PAEEREFSLG ATSVSDSGGI CIASFLGMVL EVWLCQWQVS
QGRDYCRRIE RG
//