EFR3B_HUMAN
ID EFR3B_HUMAN Reviewed; 817 AA.
AC Q9Y2G0; B7WPL8; Q86XU6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein EFR3 homolog B {ECO:0000305};
GN Name=EFR3B {ECO:0000312|HGNC:HGNC:29155};
GN Synonyms=KIAA0953 {ECO:0000303|PubMed:10231032};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE PI4K COMPLEX, SUBCELLULAR LOCATION,
RP PALMITOYLATION, AND MUTAGENESIS OF 5-CYS--CYS-8.
RX PubMed=23229899; DOI=10.1083/jcb.201206095;
RA Nakatsu F., Baskin J.M., Chung J., Tanner L.B., Shui G., Lee S.Y.,
RA Pirruccello M., Hao M., Ingolia N.T., Wenk M.R., De Camilli P.;
RT "PtdIns4P synthesis by PI4KIIIalpha at the plasma membrane and its impact
RT on plasma membrane identity.";
RL J. Cell Biol. 199:1003-1016(2012).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN THE PI4K COMPLEX.
RX PubMed=25608530; DOI=10.15252/embr.201439151;
RA Chung J., Nakatsu F., Baskin J.M., De Camilli P.;
RT "Plasticity of PI4KIIIalpha interactions at the plasma membrane.";
RL EMBO Rep. 16:312-320(2015).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION, AND MUTAGENESIS OF
RP 5-CYS--CYS-8.
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).
RN [10]
RP FUNCTION, AND IDENTIFICATION IN THE PI4K COMPLEX.
RX PubMed=26571211; DOI=10.1038/ncb3271;
RA Baskin J.M., Wu X., Christiano R., Oh M.S., Schauder C.M., Gazzerro E.,
RA Messa M., Baldassari S., Assereto S., Biancheri R., Zara F., Minetti C.,
RA Raimondi A., Simons M., Walther T.C., Reinisch K.M., De Camilli P.;
RT "The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis
RT at the plasma membrane.";
RL Nat. Cell Biol. 18:132-138(2016).
CC -!- FUNCTION: Component of a complex required to localize
CC phosphatidylinositol 4-kinase (PI4K) to the plasma membrane
CC (PubMed:23229899, PubMed:25608530, PubMed:26571211). The complex acts
CC as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P)
CC synthesis (Probable). In the complex, EFR3B probably acts as the
CC membrane-anchoring component (PubMed:23229899). Also involved in
CC responsiveness to G-protein-coupled receptors; it is however unclear
CC whether this role is direct or indirect (PubMed:25380825).
CC {ECO:0000269|PubMed:23229899, ECO:0000269|PubMed:25380825,
CC ECO:0000269|PubMed:25608530, ECO:0000269|PubMed:26571211, ECO:0000305}.
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:0000269|PubMed:23229899,
CC ECO:0000269|PubMed:25608530, ECO:0000269|PubMed:26571211}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23229899,
CC ECO:0000269|PubMed:25380825}; Lipid-anchor
CC {ECO:0000269|PubMed:23229899, ECO:0000269|PubMed:25380825}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:25380825}. Note=Palmitoylation anchors the
CC protein to the plasma membrane (PubMed:23229899, PubMed:25380825). A
CC small amount is observed in the cytosol (PubMed:25380825).
CC {ECO:0000269|PubMed:23229899, ECO:0000269|PubMed:25380825}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y2G0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2G0-2; Sequence=VSP_029806;
CC Name=3;
CC IsoId=Q9Y2G0-3; Sequence=VSP_029807;
CC -!- PTM: Palmitoylated at its N-terminus, anchoring the protein to the
CC plasma membrane. {ECO:0000269|PubMed:23229899,
CC ECO:0000269|PubMed:25380825}.
CC -!- SIMILARITY: Belongs to the EFR3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76797.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB023170; BAA76797.1; ALT_INIT; mRNA.
DR EMBL; AC012457; AAY24353.1; -; Genomic_DNA.
DR EMBL; AC013267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00733.1; -; Genomic_DNA.
DR EMBL; BC049384; AAH49384.1; -; mRNA.
DR CCDS; CCDS46231.1; -. [Q9Y2G0-1]
DR RefSeq; NP_055786.1; NM_014971.1. [Q9Y2G0-1]
DR AlphaFoldDB; Q9Y2G0; -.
DR BioGRID; 116628; 64.
DR IntAct; Q9Y2G0; 12.
DR MINT; Q9Y2G0; -.
DR STRING; 9606.ENSP00000384081; -.
DR iPTMnet; Q9Y2G0; -.
DR PhosphoSitePlus; Q9Y2G0; -.
DR BioMuta; EFR3B; -.
DR DMDM; 162416214; -.
DR EPD; Q9Y2G0; -.
DR jPOST; Q9Y2G0; -.
DR MassIVE; Q9Y2G0; -.
DR MaxQB; Q9Y2G0; -.
DR PaxDb; Q9Y2G0; -.
DR PeptideAtlas; Q9Y2G0; -.
DR PRIDE; Q9Y2G0; -.
DR ProteomicsDB; 85756; -. [Q9Y2G0-1]
DR ProteomicsDB; 85757; -. [Q9Y2G0-2]
DR ProteomicsDB; 85758; -. [Q9Y2G0-3]
DR Antibodypedia; 51573; 69 antibodies from 14 providers.
DR DNASU; 22979; -.
DR Ensembl; ENST00000401432.7; ENSP00000386082.3; ENSG00000084710.14. [Q9Y2G0-3]
DR Ensembl; ENST00000403714.8; ENSP00000384081.3; ENSG00000084710.14. [Q9Y2G0-1]
DR Ensembl; ENST00000405108.5; ENSP00000384454.1; ENSG00000084710.14. [Q9Y2G0-2]
DR GeneID; 22979; -.
DR KEGG; hsa:22979; -.
DR MANE-Select; ENST00000403714.8; ENSP00000384081.3; NM_014971.2; NP_055786.1.
DR UCSC; uc002rfw.3; human. [Q9Y2G0-1]
DR CTD; 22979; -.
DR DisGeNET; 22979; -.
DR GeneCards; EFR3B; -.
DR HGNC; HGNC:29155; EFR3B.
DR HPA; ENSG00000084710; Tissue enhanced (brain, skeletal muscle).
DR neXtProt; NX_Q9Y2G0; -.
DR OpenTargets; ENSG00000084710; -.
DR PharmGKB; PA162384473; -.
DR VEuPathDB; HostDB:ENSG00000084710; -.
DR eggNOG; KOG1877; Eukaryota.
DR GeneTree; ENSGT00390000002143; -.
DR HOGENOM; CLU_012674_1_0_1; -.
DR InParanoid; Q9Y2G0; -.
DR OMA; CQHIREV; -.
DR PhylomeDB; Q9Y2G0; -.
DR TreeFam; TF314098; -.
DR PathwayCommons; Q9Y2G0; -.
DR SignaLink; Q9Y2G0; -.
DR BioGRID-ORCS; 22979; 7 hits in 1063 CRISPR screens.
DR ChiTaRS; EFR3B; human.
DR GenomeRNAi; 22979; -.
DR Pharos; Q9Y2G0; Tbio.
DR PRO; PR:Q9Y2G0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y2G0; protein.
DR Bgee; ENSG00000084710; Expressed in pons and 141 other tissues.
DR ExpressionAtlas; Q9Y2G0; baseline and differential.
DR Genevisible; Q9Y2G0; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome.
FT CHAIN 1..817
FT /note="Protein EFR3 homolog B"
FT /id="PRO_0000312295"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ18"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ18"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQ18"
FT VAR_SEQ 1..148
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029806"
FT VAR_SEQ 715..817
FT /note="RVPAEEITYETLKKAIVDSVAVEEQERERRRQVVEKFQKAPFEEIAAHCGAR
FT ASLLQSKLNQIFEITIRPPPSPSGTITAAYGQPQNHSIPVYEMKFPDLCVY -> VSVR
FT ATVLGQPHLL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_029807"
FT MUTAGEN 5..8
FT /note="CGCC->SGSS: Induces localization to the cytosol."
FT /evidence="ECO:0000269|PubMed:23229899,
FT ECO:0000269|PubMed:25380825"
SQ SEQUENCE 817 AA; 92487 MW; 30F4AB3C957AAEE6 CRC64;
MYGVCGCCGA LRPRYKRLVD NIFPEDPEDG LVKTNMEKLT FYALSAPEKL DRIGAYLSER
LIRDVGRHRY GYVCIAMEAL DQLLMACHCQ SINLFVESFL KMVAKLLESE KPNLQILGTN
SFVKFANIEE DTPSYHRSYD FFVSRFSEMC HSSHDDLEIK TKIRMSGIKG LQGVVRKTVN
DELQANIWDP QHMDKIVPSL LFNLQHVEEA ESRSPSPLQA PEKEKESPAE LAERCLRELL
GRAAFGNIKN AIKPVLIHLD NHSLWEPKVF AIRCFKIIMY SIQPQHSHLV IQQLLGHLDA
NSRSAATVRA GIVEVLSEAA VIAATGSVGP TVLEMFNTLL RQLRLSIDYA LTGSYDGAVS
LGTKIIKEHE ERMFQEAVIK TVGSFASTLP TYQRSEVILF IMSKVPRPSL HQAVDTGRTG
ENRNRLTQIM LLKSLLQVST GFQCNNMMSA LPSNFLDRLL STALMEDAEI RLFVLEILIS
FIDRHGNRHK FSTISTLSDI SVLKLKVDKC SRQDTVFMKK HSQQLYRHIY LSCKEETNVQ
KHYEALYGLL ALISIELANE EVVVDLIRLV LAVQDVAQVN EENLPVYNRC ALYALGAAYL
NLISQLTTVP AFCQHIHEVI ETRKKEAPYM LPEDVFVERP RLSQNLDGVV IELLFRQSKI
SEVLGGSGYN SDRLCLPYIP QLTDEDRLSK RRSIGETISL QVEVESRNSP EKEERVPAEE
ITYETLKKAI VDSVAVEEQE RERRRQVVEK FQKAPFEEIA AHCGARASLL QSKLNQIFEI
TIRPPPSPSG TITAAYGQPQ NHSIPVYEMK FPDLCVY
