ID EFR3A_MOUSE Reviewed; 819 AA. AC Q8BG67; Q6ZQI4; Q8BXQ7; Q8C0Q0; Q922I2; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 08-JUN-2016, entry version 100. DE RecName: Full=Protein EFR3 homolog A {ECO:0000305}; DE AltName: Full=Protein EFR3-like; GN Name=Efr3a {ECO:0000312|MGI:MGI:1923990}; GN Synonyms=Kiaa0143 {ECO:0000303|PubMed:15363888}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND INDUCTION. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=15363888; DOI=10.1016/j.molbrainres.2004.06.022; RA Munemoto Y., Houtani T., Kase M., Sakuma S., Baba K., Yamashita T., RA Sugimoto T.; RT "Mouse homolog of KIAA0143 protein: hearing deficit induces specific RT changes of expression in auditory brainstem neurons."; RL Brain Res. Mol. Brain Res. 128:131-140(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Embryonic tail; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; RC TISSUE=Brain cortex, Olfactory bulb, Retina, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=Czech II; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 AND SER-363, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [7] RP TISSUE SPECIFICITY. RX PubMed=25380825; DOI=10.1242/jcs.157495; RA Bojjireddy N., Guzman-Hernandez M.L., Reinhard N.R., Jovic M., RA Balla T.; RT "EFR3s are palmitoylated plasma membrane proteins that control RT responsiveness to G-protein-coupled receptors."; RL J. Cell Sci. 128:118-128(2015). 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, EFR3A probably acts as the CC membrane-anchoring component. Also involved in responsiveness to CC G-protein-coupled receptors; it is however unclear whether this CC role is direct or indirect. {ECO:0000250|UniProtKB:Q14156}. CC -!- SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) CC complex, composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or CC TTC7B) and FAM126 (FAM126A or FAM126B). CC {ECO:0000250|UniProtKB:Q14156}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15363888}; CC Lipid-anchor {ECO:0000250|UniProtKB:Q14156}. Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q14156}. Note=Palmitoylation anchors the CC protein to the plasma membrane. A small amount is observed in the CC cytosol. {ECO:0000250|UniProtKB:Q14156}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8BG67-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BG67-2; Sequence=VSP_022219; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:25380825). Expressed CC in neurons of the superior olivary complex of the auditory CC brainstem. Also expressed at lower levels in the cochlear nucleus, CC the lateral leminiscal nuclei and the inferior collicus CC (PubMed:15363888). {ECO:0000269|PubMed:15363888, CC ECO:0000269|PubMed:25380825}. CC -!- INDUCTION: Expression is reduced in animals with impaired hearing. CC {ECO:0000269|PubMed:15363888}. CC -!- PTM: Palmitoylated at its N-terminus, anchoring the protein to the CC plasma membrane. {ECO:0000250|UniProtKB:Q14156}. CC -!- SIMILARITY: Belongs to the EFR3 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC97875.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB158474; BAD52086.1; -; mRNA. DR EMBL; AK129065; BAC97875.1; ALT_INIT; mRNA. DR EMBL; AK030074; BAC26768.1; -; mRNA. DR EMBL; AK032461; BAC27881.1; -; mRNA. DR EMBL; AK044000; BAC31732.1; -; mRNA. DR EMBL; AK044475; BAC31942.1; -; mRNA. DR EMBL; AK161250; BAE36269.1; -; mRNA. DR EMBL; BC007482; AAH07482.1; -; mRNA. DR CCDS; CCDS27507.1; -. [Q8BG67-1] DR RefSeq; NP_598527.2; NM_133766.3. [Q8BG67-1] DR UniGene; Mm.260647; -. DR ProteinModelPortal; Q8BG67; -. DR IntAct; Q8BG67; 1. DR STRING; 10090.ENSMUSP00000015146; -. DR iPTMnet; Q8BG67; -. DR PhosphoSite; Q8BG67; -. DR SwissPalm; Q8BG67; -. DR EPD; Q8BG67; -. DR MaxQB; Q8BG67; -. DR PaxDb; Q8BG67; -. DR PRIDE; Q8BG67; -. DR Ensembl; ENSMUST00000015146; ENSMUSP00000015146; ENSMUSG00000015002. [Q8BG67-1] DR Ensembl; ENSMUST00000173858; ENSMUSP00000134385; ENSMUSG00000015002. [Q8BG67-2] DR GeneID; 76740; -. DR KEGG; mmu:76740; -. DR UCSC; uc007vzu.1; mouse. [Q8BG67-1] DR CTD; 23167; -. DR MGI; MGI:1923990; Efr3a. DR eggNOG; KOG1877; Eukaryota. DR eggNOG; ENOG410YJSK; LUCA. DR GeneTree; ENSGT00390000002143; -. DR HOGENOM; HOG000007148; -. DR HOVERGEN; HBG060233; -. DR InParanoid; Q8BG67; -. DR OMA; CCCAALR; -. DR OrthoDB; EOG76T9RC; -. DR PhylomeDB; Q8BG67; -. DR TreeFam; TF314098; -. DR PRO; PR:Q8BG67; -. DR Proteomes; UP000000589; Chromosome 15. DR Bgee; Q8BG67; -. DR CleanEx; MM_EFR3A; -. DR ExpressionAtlas; Q8BG67; baseline and differential. DR Genevisible; Q8BG67; MM. DR GO; GO:0001533; C:cornified envelope; ISO:MGI. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0005622; C:intracellular; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI. DR GO; GO:0090002; P:establishment of protein localization to plasma membrane; ISS:UniProtKB. DR GO; GO:0016337; P:single organismal cell-cell adhesion; ISO:MGI. DR Gene3D; 1.25.10.10; -; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR SUPFAM; SSF48371; SSF48371; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome. FT CHAIN 1 819 Protein EFR3 homolog A. FT /FTId=PRO_0000270766. FT MOD_RES 213 213 Phosphoserine. FT {ECO:0000250|UniProtKB:Q6ZQ18}. FT MOD_RES 219 219 Phosphoserine. FT {ECO:0000250|UniProtKB:Q6ZQ18}. FT MOD_RES 360 360 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 363 363 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 420 420 Phosphoserine. FT {ECO:0000250|UniProtKB:Q14156}. FT MOD_RES 692 692 Phosphoserine. FT {ECO:0000244|PubMed:19144319}. FT VAR_SEQ 786 819 PPPSPSGTLTVTSGHTQYQSVPVYEMKFPDLCVY -> QRR FT ESMLYKTEAEPCYTQPMAWGQRRIKEKYKAVVK (in FT isoform 2). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_022219. FT CONFLICT 70 70 R -> H (in Ref. 3; BAC31942). FT {ECO:0000305}. FT CONFLICT 364 364 V -> I (in Ref. 4; AAH07482). FT {ECO:0000305}. FT CONFLICT 585 585 D -> G (in Ref. 3; BAC31942). FT {ECO:0000305}. FT CONFLICT 693 693 R -> T (in Ref. 3; BAC26768). FT {ECO:0000305}. SQ SEQUENCE 819 AA; 92613 MW; BF3BCD87C508CD1A CRC64; MPTRVCCCCS ALRPRYKRLV DNIFPEDPKD GLVKADMEKL TFYAVSAPEK LDRIGAYLAE RLSRDVVRHR SGYVLIAMEA LDQLLMACHS QSIKPFVESF LHMVAKLLES GEPKLQVLGT NSFVKFANIE EDTPSYHRRY DFFVSRFSAM CHSCHSDPEI RTEIRIAGIR GIQGVVRKTV NDELRATIWE PQHMDKIVPS LLFNMQKIEE VDSRLGPPSS PSAADKEENP AVLAESCFRE LLGRATFGNM NNAVRPVFAH LDHHKLWDPN EFAVHCFKII MYSIQAQYSH HVIQEILGHL DARRKDSPRV RAGIIQVLLE AVAIAAKGSI GPTVLEVFNT LLKHLRLSVE LEANDSQKGS VGSVTVSSKD NDEKIVQNAV IQTIGFFGSN LPDYQRSEIM MFIMGKVPVF GTSTHTLDIS QLGDLGTRRI QIMLLRSLLM VTSGYKAKTI VTALPGSFLD PLLSPSLMED YELRQLVLEV MHNLMDRHDN RAKLRGIRII PDVADLKIKR EKICRQDTSF MKKNGQQLYR HIYLGCKEED NVQKNYELLY TSLALITIEL ANEEVVIDLI RLAIALQDSA IINEDNLSMF HRCGIMALVA AYLNFVSQMI AVPAFCQHVS KVIETRTMEA PYFLPEHIFR DKCMLPKSLE KHDKNLYFLT NKIAESLGGS GYSVERLTVP YVPQVTDEDR LSRRKSIVDT VSIQVDILSN SVPSDDVVSN TEEITFEALK KAIDTNGMEE QEKEKRRLVI EKFQKAPFEE IAAQCESKAN LLHDRLAQIL ELTIRPPPSP SGTLTVTSGH TQYQSVPVYE MKFPDLCVY //