UniProt: B4IT24

Database: UniProt
Entry: B4IT24_DROYA

LinkDB:  B4IT24_DROYA 
Original site:  B4IT24_DROYA

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Ontology (10)   
   GO (10)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (6)   
   Pfam (1)   
   PROSITE (1)   
   SMART (1)   
Literature (2)   
   PubMed (2)   
All databases (25)   

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ID   B4IT24_DROYA            Unreviewed;       843 AA.
AC   B4IT24;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Vacuolar protein sorting-associated protein 41 homolog {ECO:0000256|PIRNR:PIRNR028921};
GN   Name=Dyak\GE14043 {ECO:0000313|EMBL:EDW99414.1};
GN   ORFNames=Dyak_GE14043 {ECO:0000313|EMBL:EDW99414.1};
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245 {ECO:0000313|EMBL:EDW99414.1, ECO:0000313|Proteomes:UP000002282};
RN   [1] {ECO:0000313|EMBL:EDW99414.1, ECO:0000313|Proteomes:UP000002282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01
RC   {ECO:0000313|Proteomes:UP000002282};
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:EDW99414.1, ECO:0000313|Proteomes:UP000002282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01
RC   {ECO:0000313|Proteomes:UP000002282};
RX   PubMed=17550304; DOI=10.1371/journal.pbio.0050152;
RA   Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W., Roote J.,
RA   Ashburner M., Bergman C.M.;
RT   "Principles of genome evolution in the Drosophila melanogaster species
RT   group.";
RL   PLoS Biol. 5:E152-E152(2007).
CC   -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking to
CC       lysosomal compartments including the endocytic membrane transport
CC       pathways. {ECO:0000256|PIRNR:PIRNR028921}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane
CC       {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein
CC       {ECO:0000256|PIRNR:PIRNR028921}. Late endosome membrane
CC       {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein
CC       {ECO:0000256|PIRNR:PIRNR028921}. Early endosome membrane
CC       {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein
CC       {ECO:0000256|PIRNR:PIRNR028921}. Lysosome membrane
CC       {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein
CC       {ECO:0000256|PIRNR:PIRNR028921}. Golgi apparatus, trans-Golgi network
CC       {ECO:0000256|PIRNR:PIRNR028921}. Cytoplasmic vesicle, clathrin-coated
CC       vesicle {ECO:0000256|PIRNR:PIRNR028921}.
CC   -!- SIMILARITY: Belongs to the VPS41 family.
CC       {ECO:0000256|ARBA:ARBA00009582, ECO:0000256|PIRNR:PIRNR028921}.
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DR   EMBL; CH891639; EDW99414.1; -; Genomic_DNA.
DR   RefSeq; XP_002086136.1; XM_002086100.2.
DR   AlphaFoldDB; B4IT24; -.
DR   EnsemblMetazoa; FBtr0260561; FBpp0259053; FBgn0231671.
DR   GeneID; 6539249; -.
DR   KEGG; dya:Dyak_GE14043; -.
DR   eggNOG; KOG2066; Eukaryota.
DR   HOGENOM; CLU_001285_2_2_1; -.
DR   OMA; PQLVWQD; -.
DR   OrthoDB; 8838at2759; -.
DR   PhylomeDB; B4IT24; -.
DR   Proteomes; UP000002282; Unassembled WGS sequence.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030897; C:HOPS complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034058; P:endosomal vesicle fusion; IEA:UniProtKB-UniRule.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006623; P:protein targeting to vacuole; IEA:InterPro.
DR   GO; GO:0007034; P:vacuolar transport; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR016902; VPS41.
DR   InterPro; IPR045111; Vps41/Vps8.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR12616; VACUOLAR PROTEIN SORTING VPS41; 1.
DR   PANTHER; PTHR12616:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 41 HOMOLOG; 1.
DR   Pfam; PF00637; Clathrin; 1.
DR   PIRSF; PIRSF028921; VPS41; 1.
DR   SMART; SM00299; CLH; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50236; CHCR; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR028921};
KW   Endosome {ECO:0000256|PIRNR:PIRNR028921};
KW   Golgi apparatus {ECO:0000256|PIRNR:PIRNR028921};
KW   Lysosome {ECO:0000256|PIRNR:PIRNR028921};
KW   Protein transport {ECO:0000256|PIRNR:PIRNR028921};
KW   Transport {ECO:0000256|PIRNR:PIRNR028921}.
SQ   SEQUENCE   843 AA;  97439 MW;  A253A8FBBD0967F6 CRC64;
     MAKSLPSISC VFGTDSINEE DVEPKFKYQR LANDLKNMLN ADVISCSAVH LKFLIFGTFR
     GRVYIFDHQG NSVYSNLSIS ERHTHQVAVN NINVDHKGEY VATCSDDGKV NITGLFSCEN
     NHSLNFGKCI KVVSMDPESK AHIKRFVVGD DKLILYERNL LKKLKPCELC SVEGSVLSIC
     WHGNFIAWAS HIGVRVYDLN ERCSLGLIKW EVPSQERLEN FRCHLRWSNN NTLLIGWVDT
     IRVCVIRKRN SIEASTGNLP VNIVDPISTF QTTFYVCGLA PLSEKQLVVL GYRKEKCSSF
     KALRPVLCVI EYKMNNSEEI CTDSLTLRGF EEYTVNDYSL GGLIEEKRFF IVAPKDIVVA
     SLIETDDRIE WLVKHSKFEE AMELIAANGS NVTVLSVAKL YINHLLALKK YDDAAKLCLR
     MLGNDKVLWE EEVFKFVKCQ QLRSVSAYLP TSNECKLDPH VYEMVLYEFL KFDVFGFLNI
     IKEWPSHLYD GLAVINAIHD NFRKQHANQL LESLALLYSY QGDFESALRM YLKLQNKDVF
     QLIRRYELYD VISKLIIPLI QLDRKCSFEI LLDKNKIKTE IVVNQLEHNQ EYLYWYLDSL
     LKKDPNNGFQ KKLVFLYANF DRKKLLPFLV RSKDYDIQEA LVICKQENFY PEMVYLLGRM
     GGVEAAEALN IIIHSIRDIE MAIEFCKEHD DNDLWNALIN EFSKHPEIVT KVLDGIVDYV
     NPAVVVEKIK MGQNIPNLRP SLIKMLWHYN IHGEVLSSAQ QIQLNDYFEI HSEIVTKQRR
     GHHVSYEQLC SMCQRPVLMI GTHYNCIIRF ECGHVYHKPC TQGKLQKNCT ECYLWNLAVE
     KYV
//

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