Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

GM25917

Gene

Dsec\GM25917

Organism
Drosophila sechellia (Fruit fly)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein inferred from homologyi

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ion channelUniRule annotationSAAS annotation

Keywords - Biological processi

Ion transport, Transport

Names & Taxonomyi

Protein namesi
Submitted name:
GM25917Imported
Gene namesi
Name:Dsec\GM25917Imported
ORF Names:Dsec_GM25917Imported, GM25917Imported
OrganismiDrosophila sechellia (Fruit fly)Imported
Taxonomic identifieri7238 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000001292 Componenti: Unassembled WGS sequence

Organism-specific databases

FlyBaseiFBgn0180773. Dsec\GM25917.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei6 – 2924HelicalSequence analysisAdd
BLAST
Transmembranei108 – 12518HelicalSequence analysisAdd
BLAST
Transmembranei157 – 17721HelicalSequence analysisAdd
BLAST
Transmembranei189 – 20820HelicalSequence analysisAdd
BLAST
Transmembranei220 – 24728HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Structurei

3D structure databases

ProteinModelPortaliB4HFQ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 13258Ion_trans_2InterPro annotationAdd
BLAST
Domaini169 – 24678Ion_trans_2InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the two pore domain potassium channel (TC 1.A.1.8) family. [View classification]UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysisSAAS annotation

Phylogenomic databases

KOiK04919.
OMAiNNDAENQ.
OrthoDBiEOG7B05DC.
PhylomeDBiB4HFQ2.

Family and domain databases

InterProiIPR003280. 2pore_dom_K_chnl.
IPR003092. 2pore_dom_K_chnl_TASK.
IPR013099. K_chnl_dom.
[Graphical view]
PfamiPF07885. Ion_trans_2. 2 hits.
[Graphical view]
PRINTSiPR01333. 2POREKCHANEL.
PR01095. TASKCHANNEL.

Sequencei

Sequence statusi: Complete.

B4HFQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKQNVRTIS LIVCTFTYLL VGAAVFDALE SETEKRRWEA LQDAEDMIIR
60 70 80 90 100
KYNISQEDFK VMETVVLKSE SHKAGQQWKF TGAFYYATTV LTTIGYGHST
110 120 130 140 150
PSTVGGKLFT MCYAIVGIPL GLVMFQSIGE RVNRLSSYVI KAVRSSLRCK
160 170 180 190 200
RTVASEVDLI CVVTTLSSLT IAGGAAAFSK FEGWSYFDSV YYCFITLTTI
210 220 230 240 250
GFGDMVALQR DNALNRKPEY VMFALIFILF GLAIVAASLN LLVLRFVTMN
260 270 280 290 300
TEDERRDEAQ AMQALQVAVK LEGDVITSNG SILSGYEGHD GQSLNGSNTS
310 320 330 340 350
SMCSCHCICL NGNRLKKSSN LGKNNDAENQ YKLRRSPTHI RQLLPEVVPM
360 370 380 390 400
QDLNYDYDTQ SLHTLADRGT MDSSYMGVDM ADMGDTASME LRTHTLLKRN

VSLLSIRI
Length:408
Mass (Da):45,371
Last modified:September 23, 2008 - v1
Checksum:i3CAFEC661468AD09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH480815 Genomic DNA. Translation: EDW42287.1.
RefSeqiXP_002031301.1. XM_002031265.1.

Genome annotation databases

EnsemblMetazoaiFBtr0208902; FBpp0207394; FBgn0180773.
GeneIDi6606500.
KEGGidse:Dsec_GM25917.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH480815 Genomic DNA. Translation: EDW42287.1.
RefSeqiXP_002031301.1. XM_002031265.1.

3D structure databases

ProteinModelPortaliB4HFQ2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0208902; FBpp0207394; FBgn0180773.
GeneIDi6606500.
KEGGidse:Dsec_GM25917.

Organism-specific databases

FlyBaseiFBgn0180773. Dsec\GM25917.

Phylogenomic databases

KOiK04919.
OMAiNNDAENQ.
OrthoDBiEOG7B05DC.
PhylomeDBiB4HFQ2.

Family and domain databases

InterProiIPR003280. 2pore_dom_K_chnl.
IPR003092. 2pore_dom_K_chnl_TASK.
IPR013099. K_chnl_dom.
[Graphical view]
PfamiPF07885. Ion_trans_2. 2 hits.
[Graphical view]
PRINTSiPR01333. 2POREKCHANEL.
PR01095. TASKCHANNEL.
ProtoNetiSearch...

Publicationsi

  1. "Evolution of genes and genomes on the Drosophila phylogeny."
    Drosophila 12 Genomes Consortium
    Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.
    , Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.
    Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Rob3c / Tucson 14021-0248.25Imported.

Entry informationi

Entry nameiB4HFQ2_DROSE
AccessioniPrimary (citable) accession number: B4HFQ2
Entry historyi
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: June 8, 2016
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.