ID A0A0Q9W0U7_DROVI Unreviewed; 959 AA.
AC A0A0Q9W0U7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Uncharacterized protein, isoform B {ECO:0000313|EMBL:KRF78693.1};
DE SubName: Full=Uncharacterized protein, isoform C {ECO:0000313|EMBL:KRF78694.1};
DE SubName: Full=Uncharacterized protein, isoform D {ECO:0000313|EMBL:KRF78695.1};
DE SubName: Full=Uncharacterized protein, isoform E {ECO:0000313|EMBL:KRF78696.1};
DE SubName: Full=Uncharacterized protein, isoform F {ECO:0000313|EMBL:KRF78697.1};
DE SubName: Full=Uncharacterized protein, isoform G {ECO:0000313|EMBL:KRF78698.1};
DE SubName: Full=Uncharacterized protein, isoform I {ECO:0000313|EMBL:KRF78700.1};
GN Name=Dvir\GJ10698 {ECO:0000313|EMBL:KRF78696.1};
GN ORFNames=Dvir_GJ10698 {ECO:0000313|EMBL:KRF78696.1};
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244 {ECO:0000313|EMBL:KRF78696.1, ECO:0000313|Proteomes:UP000008792};
RN [1] {ECO:0000313|EMBL:KRF78696.1, ECO:0000313|Proteomes:UP000008792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:KRF78696.1}, and Tucson
RC 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [2] {ECO:0000313|EMBL:KRF78696.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:KRF78696.1};
RX PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT "Assembly reconciliation.";
RL Bioinformatics 24:42-45(2008).
RN [3] {ECO:0000313|EMBL:KRF78696.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:KRF78696.1};
RG FlyBase;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:69955, ChEBI:CHEBI:29101, ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00033667};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. SLC8 subfamily. {ECO:0000256|ARBA:ARBA00007489}.
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DR EMBL; CH940652; KRF78693.1; -; Genomic_DNA.
DR EMBL; CH940652; KRF78694.1; -; Genomic_DNA.
DR EMBL; CH940652; KRF78695.1; -; Genomic_DNA.
DR EMBL; CH940652; KRF78696.1; -; Genomic_DNA.
DR EMBL; CH940652; KRF78697.1; -; Genomic_DNA.
DR EMBL; CH940652; KRF78698.1; -; Genomic_DNA.
DR EMBL; CH940652; KRF78700.1; -; Genomic_DNA.
DR RefSeq; XP_015026021.1; XM_015170535.1.
DR RefSeq; XP_015026022.1; XM_015170536.1.
DR RefSeq; XP_015026023.1; XM_015170537.1.
DR RefSeq; XP_015026024.1; XM_015170538.1.
DR RefSeq; XP_015026025.1; XM_015170539.1.
DR RefSeq; XP_015026026.1; XM_015170540.1.
DR RefSeq; XP_015026028.1; XM_015170542.1.
DR AlphaFoldDB; A0A0Q9W0U7; -.
DR SMR; A0A0Q9W0U7; -.
DR STRING; 7244.A0A0Q9W0U7; -.
DR EnsemblMetazoa; FBtr0434444; FBpp0391506; FBgn0197975.
DR EnsemblMetazoa; FBtr0436561; FBpp0393450; FBgn0197975.
DR EnsemblMetazoa; FBtr0436908; FBpp0393770; FBgn0197975.
DR EnsemblMetazoa; FBtr0437637; FBpp0394448; FBgn0197975.
DR EnsemblMetazoa; FBtr0437830; FBpp0394632; FBgn0197975.
DR EnsemblMetazoa; FBtr0438082; FBpp0394865; FBgn0197975.
DR EnsemblMetazoa; FBtr0439647; FBpp0396306; FBgn0197975.
DR GeneID; 6632312; -.
DR InParanoid; A0A0Q9W0U7; -.
DR OrthoDB; 462435at2759; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:EnsemblMetazoa.
DR GO; GO:0005432; F:calcium:sodium antiporter activity; IEA:EnsemblMetazoa.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IEA:EnsemblMetazoa.
DR GO; GO:0007602; P:phototransduction; IEA:EnsemblMetazoa.
DR Gene3D; 2.60.40.2030; -; 2.
DR Gene3D; 1.20.1420.30; NCX, central ion-binding region; 2.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR004836; Na_Ca_Ex.
DR InterPro; IPR032452; Na_Ca_Ex_C-exten.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR NCBIfam; TIGR00845; caca; 1.
DR PANTHER; PTHR11878:SF65; NA_CA-EXCHANGE PROTEIN, ISOFORM G; 1.
DR PANTHER; PTHR11878; SODIUM/CALCIUM EXCHANGER; 1.
DR Pfam; PF03160; Calx-beta; 2.
DR Pfam; PF01699; Na_Ca_ex; 2.
DR Pfam; PF16494; Na_Ca_ex_C; 1.
DR PRINTS; PR01259; NACAEXCHNGR.
DR SMART; SM00237; Calx_beta; 2.
DR SUPFAM; SSF141072; CalX-like; 2.
PE 3: Inferred from homology;
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
KW Calcium {ECO:0000256|ARBA:ARBA00022568};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008792};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
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 116..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 787..811
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 823..842
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 862..881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 893..913
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 933..954
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 418..517
FT /note="Calx-beta"
FT /evidence="ECO:0000259|SMART:SM00237"
FT DOMAIN 531..630
FT /note="Calx-beta"
FT /evidence="ECO:0000259|SMART:SM00237"
SQ SEQUENCE 959 AA; 106990 MW; 7D503288D8FB7A5E CRC64;
MLLIRKTVAS VATCAILLLL VYVKGHTFAL ATSRQDVSQE SDSTLNGTSL QSSIEQIRSR
QKRAVEDVTD DDEEVITSQV RGGREASEIG TCSEGLVLPL WMPQSPITSG DRAIRGFVYF
MLMIYLFVGV SIISDRFMAS IEAITSIERN VTVKGPKGEK QTMRVRIWNE TVANLTLMAL
GSSAPEILLS VIEIYAKNFE SGDLGPGTIV GSAAYNLFII IALCMVLIPK GETRRIRHLR
VFMVTASLSV LAYVWLWVIL SVSSPGIVEV WEGLVTLIMF PLTVLWAYIA ERRLLVYKYM
DKNYRMNKRG TVVAGEHDSV EMGGDEPKRL VNINSSANAY NEARLEYIQL LAELRQKYPD
ADLDQLEMMA QEQMISRGNK SRAFYRIQAT RKLIGSGNLM RKIQERAHDD LTQVKAQLHQ
FSDDDDEPTR IYFEPGHYTV MENCGEFEVR VVRRGDISGY SKVEFETQDG TASAGSDYVG
KKGALTFPPG VDEQRFKIEI IDDDIFEEDE CFYIRLFNPS ENVNLAVPQI ATIMILDDDH
AGIFAFADSL IEVSESVGVY DLAVMRYSGA RGTVIVPYWS EDVTAIGGRH FGEVRGELIF
ENNVSEQYIS IPILEESKYQ KDVKFKMHIG EPRLAPDDTN QESFFNRFFE NHTGDHTHDE
LLEKIKEAEQ KSPKDLTELE RILLMSRPRN GELTTTYIRI RESQEFRATV DKLVARANVS
AVLGTSSWKE QFKDALTVVP ADESEFDTDE DVEEDVPKCF DYISHFVCLF WKVLFAFVPP
TDICGGYVTF VISIFVIGVL TAIIGDAATY FGCVLNIKDS VTAICFVALG TSIPDTFASI
IAAKQDETAD NCIGNVTGSN AVNVFLGIGL AWSIASIYHM ANGTTFNVEP GTIGFAVALF
CGSAVIAVGV MMYRRVNKSI RAELGGPKTS KWIHASILIS LWCIYLVVST LEAYDIIQI
//
