ID B3MA80_DROAN Unreviewed; 559 AA.
AC B3MA80;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE RecName: Full=Sorting nexin {ECO:0000256|PIRNR:PIRNR027744};
GN Name=Dana\GF25132 {ECO:0000313|EMBL:EDV39094.1};
GN Synonyms=dana_GLEANR_9810 {ECO:0000313|EMBL:EDV39094.1};
GN ORFNames=GF25132 {ECO:0000313|EMBL:EDV39094.1};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV39094.1, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:EDV39094.1, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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).
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883, ECO:0000256|PIRNR:PIRNR027744}.
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DR EMBL; CH902618; EDV39094.1; -; Genomic_DNA.
DR RefSeq; XP_001956288.1; XM_001956252.2.
DR AlphaFoldDB; B3MA80; -.
DR SMR; B3MA80; -.
DR STRING; 7217.B3MA80; -.
DR EnsemblMetazoa; FBtr0129832; FBpp0128324; FBgn0102124.
DR GeneID; 6507758; -.
DR KEGG; dan:6507758; -.
DR eggNOG; KOG2528; Eukaryota.
DR HOGENOM; CLU_021494_1_0_1; -.
DR InParanoid; B3MA80; -.
DR OMA; MGVNYCL; -.
DR OrthoDB; 5401713at2759; -.
DR PhylomeDB; B3MA80; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:EnsemblMetazoa.
DR GO; GO:0005768; C:endosome; IEA:EnsemblMetazoa.
DR GO; GO:0043025; C:neuronal cell body; IEA:EnsemblMetazoa.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:EnsemblMetazoa.
DR GO; GO:0042734; C:presynaptic membrane; IEA:EnsemblMetazoa.
DR GO; GO:0071212; C:subsynaptic reticulum; IEA:EnsemblMetazoa.
DR GO; GO:0019900; F:kinase binding; IEA:EnsemblMetazoa.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0000045; P:autophagosome assembly; IEA:EnsemblMetazoa.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:EnsemblMetazoa.
DR GO; GO:0007032; P:endosome organization; IEA:EnsemblMetazoa.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:EnsemblMetazoa.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IEA:EnsemblMetazoa.
DR GO; GO:1990709; P:presynaptic active zone organization; IEA:EnsemblMetazoa.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR CDD; cd07626; BAR_SNX9_like; 1.
DR CDD; cd06862; PX_SNX9_18_like; 1.
DR CDD; cd11763; SH3_SNX9_like; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR014536; Snx9_fam.
DR InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR PANTHER; PTHR45827; SORTING NEXIN; 1.
DR PANTHER; PTHR45827:SF1; SORTING NEXIN; 1.
DR Pfam; PF10456; BAR_3_WASP_bdg; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF027744; Snx9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..62
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 213..323
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 71..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 249
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT BINDING 251
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT BINDING 289
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
SQ SEQUENCE 559 AA; 62533 MW; 5541A0BFB78AAEC0 CRC64;
MTSYVRAMYD FSGEPGSSEL SIVTGEVLSV TRSDVGEGWW EGKNARGQIG LFPAAYVEVL
SAAEAQKLNS SGAAAVPQVP DPFATSPPPR YDQTAEDWDD DDDWSDDNDT YSEIGQGAQK
APAAAGATSA RIGDYDHKSL PGPPNDDTQS LASAAGTGAG GSGTVKKGMF AKSSDSYILG
LSNTTEKIPE SELAYITQVE DTIYQWTKNQ SPYSVVVASP KKESKFKGMK TFIAYQLTPS
FNNISVSRRY KHFDWLHERL VDKFALIPVP PLPDKQISGR YEEQFVEHRR VQLQEFVDWV
CRHPVMSKCE VWHHFLTCRD EKIWKSGKRK AERDPYMGVN YCLAIFPPDR HILPSVIETP
LETGIQFIHS MDAAVRNLNN ISNDMAKRSL AQSKKEFQRI GDGLSDMAKA LAIDERRAPT
RNGIPLSESV GRIGGIFIGI GQTFGDQAKH DWIPLSDRLH IYRGVLNCFP DIFSTHKGAI
QKRKDCQRSH DEGKMSNPQL QDVNRRTDVV TYTVMAELTH FKSERDTHLK QTLKTFINEQ
IKFYQGVVAR LQEAARQIE
//
