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 07-APR-2021, entry version 125. 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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: III. RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT 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; 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., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., 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., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692, AND IDENTIFICATION BY RP 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, Pancreas, RC 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 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., 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 G- CC protein-coupled receptors; it is however unclear whether this role is CC direct or indirect. {ECO:0000250|UniProtKB:Q14156}. CC -!- SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex, CC composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and CC FAM126 (FAM126A or FAM126B). {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 protein CC to the plasma membrane. A small amount is observed in the cytosol. CC {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 -!- TISSUE SPECIFICITY: Widely expressed (PubMed:25380825). Expressed in CC neurons of the superior olivary complex of the auditory brainstem. Also CC expressed at lower levels in the cochlear nucleus, the lateral CC leminiscal nuclei and the inferior collicus (PubMed:15363888). CC {ECO:0000269|PubMed:15363888, 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 BioGRID; 218290; 1. DR IntAct; Q8BG67; 1. DR STRING; 10090.ENSMUSP00000015146; -. DR iPTMnet; Q8BG67; -. DR PhosphoSitePlus; Q8BG67; -. DR SwissPalm; Q8BG67; -. DR EPD; Q8BG67; -. DR jPOST; Q8BG67; -. DR PaxDb; Q8BG67; -. DR PeptideAtlas; Q8BG67; -. DR PRIDE; Q8BG67; -. DR ProteomicsDB; 277729; -. [Q8BG67-1] DR ProteomicsDB; 277730; -. [Q8BG67-2] DR Antibodypedia; 14097; 123 antibodies. 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 GeneTree; ENSGT00390000002143; -. DR HOGENOM; CLU_012674_1_0_1; -. DR InParanoid; Q8BG67; -. DR OMA; HRHSWVD; -. DR OrthoDB; 173880at2759; -. DR PhylomeDB; Q8BG67; -. DR TreeFam; TF314098; -. DR BioGRID-ORCS; 76740; 18 hits in 56 CRISPR screens. DR ChiTaRS; Efr3a; mouse. DR PRO; PR:Q8BG67; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; Q8BG67; protein. DR Bgee; ENSMUSG00000015002; Expressed in pontine nuclear group and 294 other tissues. 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; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI. DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI. DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB. DR InterPro; IPR016024; ARM-type_fold. DR SUPFAM; SSF48371; SSF48371; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Cytoplasm; Lipoprotein; Membrane; KW Palmitate; Phosphoprotein; Reference proteome. FT CHAIN 1..819 FT /note="Protein EFR3 homolog A" FT /id="PRO_0000270766" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 363 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 420 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q14156" FT MOD_RES 692 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT VAR_SEQ 786..819 FT /note="PPPSPSGTLTVTSGHTQYQSVPVYEMKFPDLCVY -> QRRESMLYKTEAEP FT CYTQPMAWGQRRIKEKYKAVVK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_022219" FT CONFLICT 70 FT /note="R -> H (in Ref. 3; BAC31942)" FT /evidence="ECO:0000305" FT CONFLICT 364 FT /note="V -> I (in Ref. 4; AAH07482)" FT /evidence="ECO:0000305" FT CONFLICT 585 FT /note="D -> G (in Ref. 3; BAC31942)" FT /evidence="ECO:0000305" FT CONFLICT 693 FT /note="R -> T (in Ref. 3; BAC26768)" FT /evidence="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 //