ID   EFR3B_DANRE             Reviewed;         816 AA.
AC   Q5SPP5;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Protein EFR3 homolog B;
GN   Name=efr3b; ORFNames=si:ch211-203k16.1, si:ch211-215m21.18;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Component of a complex required to localize
CC       phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The
CC       complex acts as a regulator of phosphatidylinositol 4-phosphate
CC       (PtdIns(4)P) synthesis. In the complex, efr3b probably acts as the
CC       membrane-anchoring component. {ECO:0000250|UniProtKB:Q9Y2G0}.
CC   -!- SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex.
CC       {ECO:0000250|UniProtKB:Q9Y2G0}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y2G0};
CC       Lipid-anchor {ECO:0000250|UniProtKB:Q9Y2G0}. Note=Palmitoylation
CC       anchors the protein to the plasma membrane.
CC       {ECO:0000250|UniProtKB:Q9Y2G0}.
CC   -!- PTM: Palmitoylated at its N-terminus, anchoring the protein to the
CC       plasma membrane. {ECO:0000250|UniProtKB:Q9Y2G0}.
CC   -!- SIMILARITY: Belongs to the EFR3 family. {ECO:0000305}.
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DR   EMBL; AL845420; CAI11752.2; -; Genomic_DNA.
DR   EMBL; AL928995; CAI11752.2; JOINED; Genomic_DNA.
DR   RefSeq; XP_005170258.1; XM_005170201.3.
DR   AlphaFoldDB; Q5SPP5; -.
DR   STRING; 7955.ENSDARP00000112891; -.
DR   PaxDb; Q5SPP5; -.
DR   GeneID; 561353; -.
DR   KEGG; dre:561353; -.
DR   CTD; 561353; -.
DR   ZFIN; ZDB-GENE-041014-293; efr3bb.
DR   eggNOG; KOG1877; Eukaryota.
DR   HOGENOM; CLU_012674_1_0_1; -.
DR   InParanoid; Q5SPP5; -.
DR   OMA; CQHIREV; -.
DR   OrthoDB; 173880at2759; -.
DR   PhylomeDB; Q5SPP5; -.
DR   TreeFam; TF314098; -.
DR   PRO; PR:Q5SPP5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome.
FT   CHAIN           1..816
FT                   /note="Protein EFR3 homolog B"
FT                   /id="PRO_0000312297"
FT   REGION          206..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   816 AA;  91960 MW;  EE14FC04D8CF75E4 CRC64;
     MTGVCGCCGA LRPRYKRLVD NIFPEDPEDG LVKANMEKLT FYALSAPEKL DRIGAYLSER
     LSRDVARHRY GYVCIAMEAL DQLLMACHCQ SINLFVESFL KMVRKLLEAD KPNLQILGTN
     SFVKFANIEE DTPSYHRSYD FFVSRFSEMC HSGYEDPDIR TKIRMAGIKG LQGVVRKTVN
     DELQANIWDP QHMDKIVPSL LFNLQSGEGT ESRSPSPLQA SEKEKESPAE LTERCFRELL
     GRAAYGNIKN AVTPVLMHLD NHSLWEGKTF AVRCFKIIMY SIQSQHSHLV IQQLLGHLDA
     NSKSSATVRA GIVEVLLEVA AIAASGSVGP TVLEVFNTLL RHLRLSVDYE LTGSYDCTNI
     GTKIIKEHEE RQLQEAVIRT IGSFANTLPT YQRSEVMLFI MGKVPIPGLH PTLPSIGSGP
     EGNRMIQVML LKSLRQVTCG FQTTNMLTAL PNSFLDPMLS FALLEDAEIR LLVLEILVSL
     IDRHDNLPKF SNISIISDIS VLKLKVDKCS RQDNLFMKKH AQHLYRHIYL CSKEQSSVQP
     HFEKLYSLLA LISMELANEE VVVDLIRVAL ALQDLALSSE EMLPVYNRCA IHALSSAYLN
     LISQLTTVPA FCQHVHEVIE MRQKEIPYLL PEDVFIENPK IPKTLEKLEG DVLFQQAKIT
     EVLGGSGYNT ERLATPYVPQ FTDEDRLSKR KSIGETISLQ VEVDSRNSPE KEERTPAEEI
     TFETLKNAIV DSVGVEEQEK ERRRQVVEKF QKAPFEEIAA HCGARATMLQ SKLNQIFEIT
     IRPPPSPSGT ITSSYGQTQS RSVPVYEMKF PDLCVY