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Database: UniProt
Entry: A0A139WM47_TRICA
LinkDB: A0A139WM47_TRICA
Original site: A0A139WM47_TRICA 
ID   A0A139WM47_TRICA        Unreviewed;      1450 AA.
AC   A0A139WM47;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Potassium channel subfamily T member 1-like Protein {ECO:0000313|EMBL:KYB29020.1};
GN   Name=AUGUSTUS-3.0.2_32248 {ECO:0000313|EMBL:KYB29020.1};
GN   ORFNames=TcasGA2_TC032248 {ECO:0000313|EMBL:KYB29020.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:KYB29020.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:KYB29020.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB29020.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:KYB29020.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB29020.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KQ971314; KYB29020.1; -; Genomic_DNA.
DR   STRING; 7070.A0A139WM47; -.
DR   EnsemblMetazoa; TC032248_001; TC032248_001; TC032248.
DR   eggNOG; KOG3193; Eukaryota.
DR   InParanoid; A0A139WM47; -.
DR   OMA; SADASHY; -.
DR   Proteomes; UP000007266; Linkage group 2.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005228; F:intracellular sodium-activated potassium channel activity; IBA:GO_Central.
DR   GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR003929; K_chnl_BK_asu.
DR   InterPro; IPR013099; K_chnl_dom.
DR   InterPro; IPR047871; K_chnl_Slo-like.
DR   PANTHER; PTHR10027; CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA CHAIN; 1.
DR   PANTHER; PTHR10027:SF10; SLOWPOKE 2, ISOFORM D; 1.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF07885; Ion_trans_2; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000313|EMBL:KYB29020.1};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
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        97..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        300..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          277..339
FT                   /note="Potassium channel"
FT                   /evidence="ECO:0000259|Pfam:PF07885"
FT   DOMAIN          501..594
FT                   /note="Calcium-activated potassium channel BK alpha
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF03493"
FT   REGION          693..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1255..1300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..715
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..744
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1275..1300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1450 AA;  162933 MW;  3B75C98C8F73691F CRC64;
     MSMYFFRLHN LRRAEEDKKK KQQSRRRGKV VGCHRLTTNA LTLAPSRLFE RPPLTPSDSL
     DEVALQIPRV RVEYYVNENT FKERLQLYFI KNQRSSLRIR IANLFLKLLS CILYIIRVVT
     DLDPTYAACY GCTPGDKSEY IISANLTEEK FQENPIINWD AILWVNRPLE LWIVQVVLAM
     ISLTEALLLA YLGYKGNIWQ QLLSFHFILE IVNTIPFTLT LFYPPLRNLF IPVFLNCWLA
     KHALENMFND LHRAMQKSQS ALSQQLTILS ATLVCLVFTS VCGIQHFQRA GHRHLNLFQA
     TYYVVVTFST VGYGDFVPDI WPSQLYMVIM ICVALIVLPT QFEQLAFTWM ERQKLGGSYS
     SHRAQSEKHV VVCSTTLHAD TIMDFLNEFY AHPLLQDYYV VLLSPMELDT TMRMILQVPI
     WAQRVIYIQG SCLKDGDLAR ARMNEAEACF VLAARNYADK TAADEHTILR SWAVKDFAPN
     VAQYVQIFRP ENKIHVKFAE YVVCEDEFKY ALLANNCTCP GASTLVTLLL HTSRGQEGQQ
     SQEEWHRLYG RCSGNEIYHI TLGDSRFFGE YEGKSFTYAS FHSHRKYGVA LVGVRPAELP
     EFYEDTILLN PGPRHIMKKS DTCYYMSITK EENSSFTVAN QPQGNNNNTS TEPVIVTAEE
     KSQAPATKDG TGSPQLILQV PTCVTTFPDN AGLSDSRQCL KESSPGSTTI DVSITGNHLD
     IPRSGDNPNL LSPEMINQRR NSRRPSILPV PDMFTSSSLN IPQDVADEGD ESEDELEDDV
     PWRSPSEKIA SSLTDDSGDS ERPAWHDECA RIVKGFPPVS PYIGVSPTLC YLLKEKKPLC
     CLQLAQVCEH CSYRNARDYQ WQNKTIILAA DYASNGIYNF IIPLRAHFRS KTSLNPIILL
     LERRPDIAFL DAISYFPLVY WMLGTIDCLD DLLRAGITLA ENVVVVNKEL SNSAEEDSLA
     DCNTIVAVQT MFKFFPSIKS ITELSQSSNM RFMQFRAHDK YALHLSKMEK REKERGSHIS
     YMFRLPFAAG SVFSASMLDT LLYQAFVKDY VITFVRLLLG IDQAPGSGFL TSMKITKDDM
     WIRTYGRLYQ KLCSTTCEIP IGIYRTQDTS LSDSSHLDEE LGPDRVGVTY RPKEGTNCLG
     CTDRRNSMFS INMADEAKDN HEQQIERAEI ANLVRSRMES LNLPTIDYND VSEKRNSLSY
     VIINPSCDLK LEEGDIIYLV RPSPFSAQKT FERHNSRRKS NISFCSQTLI QQMAAASQAG
     SRRGSGLGLT GYQSPRPPPL STTKSNSLSL PDSPTVAGYQ RGRSNSLRVI DDILLRRSNS
     LRQGLTSVGS GRRKSSLEDI GLSHFSTNYN NPIKIALNGS IGLEVTPPEE NSPPVISSNT
     AMVVNAAAHT GSTISLAQSG LPSSSSSLPQ PLNLGINVPT NFGEAAPVQQ AALPPPAAPT
     DPQHLQGTIV
//
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