EFR3A_MOUSE
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 03-AUG-2022, entry version 130.
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};
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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 AlphaFoldDB; Q8BG67; -.
DR BioGRID; 218290; 1.
DR STRING; 10090.ENSMUSP00000015146; -.
DR iPTMnet; Q8BG67; -.
DR PhosphoSitePlus; Q8BG67; -.
DR SwissPalm; Q8BG67; -.
DR EPD; Q8BG67; -.
DR jPOST; Q8BG67; -.
DR MaxQB; Q8BG67; -.
DR PaxDb; Q8BG67; -.
DR PeptideAtlas; Q8BG67; -.
DR PRIDE; Q8BG67; -.
DR ProteomicsDB; 277729; -. [Q8BG67-1]
DR ProteomicsDB; 277730; -. [Q8BG67-2]
DR Antibodypedia; 14097; 124 antibodies from 18 providers.
DR DNASU; 76740; -.
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 VEuPathDB; HostDB:ENSMUSG00000015002; -.
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; 20 hits in 75 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 248 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
