ID   EFR3A_HUMAN             Reviewed;         821 AA.
AC   Q14156; A7MD19; Q2VPK2; Q63HL7; Q68DX1; Q6IQ18;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 177.
DE   RecName: Full=Protein EFR3 homolog A {ECO:0000305};
DE   AltName: Full=Protein EFR3-like;
GN   Name=EFR3A {ECO:0000312|HGNC:HGNC:28970};
GN   Synonyms=KIAA0143 {ECO:0000303|PubMed:8590280};
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 1).
RC   TISSUE=Bone marrow;
RX   PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA   Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. IV. The
RT   coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 2:167-174(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 469-821 (ISOFORM 3), AND VARIANT ASP-365.
RC   TISSUE=Rectum tumor, and Retina;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-365.
RC   TISSUE=Skin, and Testis;
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-694, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-694, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-694, AND IDENTIFICATION BY
RP   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   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION, AND MUTAGENESIS OF
RP   6-CYS--CYS-9.
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-694, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   POSSIBLE INVOLVEMENT IN AUTISM, AND VARIANTS ARG-14; GLU-50; CYS-55;
RP   CYS-70; LEU-100; PRO-118; LEU-123; VAL-194; ALA-243; GLY-268; ASP-320;
RP   SER-321; LEU-337; SER-338; ASP-354; MET-451; GLY-504; PRO-508; VAL-510;
RP   ARG-528; TRP-532; THR-534; VAL-570; VAL-646 AND ALA-785.
RX   PubMed=24860643; DOI=10.1186/2040-2392-5-31;
RA   Gupta A.R., Pirruccello M., Cheng F., Kang H.J., Fernandez T.V.,
RA   Baskin J.M., Choi M., Liu L., Ercan-Sencicek A.G., Murdoch J.D., Klei L.,
RA   Neale B.M., Franjic D., Daly M.J., Lifton R.P., De Camilli P., Zhao H.,
RA   Sestan N., State M.W.;
RT   "Rare deleterious mutations of the gene EFR3A in autism spectrum
RT   disorders.";
RL   Mol. Autism 5:31-31(2014).
RN   [12]
RP   FUNCTION.
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   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION, AND MUTAGENESIS OF
RP   6-CYS--CYS-9.
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   [14]
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, EFR3A 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: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       HYCC (HYCC1 or HYCC2) (PubMed:26571211). {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,
CC       PubMed:26571211). A small amount is observed in the cytosol
CC       (PubMed:25380825). {ECO:0000269|PubMed:23229899,
CC       ECO:0000269|PubMed:25380825, ECO:0000269|PubMed:26571211}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q14156-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14156-2; Sequence=VSP_022217;
CC       Name=3;
CC         IsoId=Q14156-3; Sequence=VSP_022218;
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   -!- DISEASE: Note=Genetic variations in EFR3A may be associated with
CC       susceptibility to autism. {ECO:0000305|PubMed:24860643}.
CC   -!- SIMILARITY: Belongs to the EFR3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH71611.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI08668.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI08668.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=BAA09764.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D63477; BAA09764.1; ALT_INIT; mRNA.
DR   EMBL; BX648595; CAH56143.1; -; mRNA.
DR   EMBL; CR749243; CAH18099.1; -; mRNA.
DR   EMBL; AC092817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC071611; AAH71611.1; ALT_INIT; mRNA.
DR   EMBL; BC108667; AAI08668.1; ALT_SEQ; mRNA.
DR   EMBL; BC152442; AAI52443.1; -; mRNA.
DR   CCDS; CCDS34942.2; -. [Q14156-1]
DR   CCDS; CCDS83328.1; -. [Q14156-2]
DR   RefSeq; NP_001310482.1; NM_001323553.2. [Q14156-2]
DR   RefSeq; NP_001310483.1; NM_001323554.2. [Q14156-2]
DR   RefSeq; NP_001310484.1; NM_001323555.2. [Q14156-2]
DR   RefSeq; NP_001310485.1; NM_001323556.2. [Q14156-2]
DR   RefSeq; NP_001310486.1; NM_001323557.2. [Q14156-2]
DR   RefSeq; NP_001310487.1; NM_001323558.2.
DR   RefSeq; NP_055952.2; NM_015137.6. [Q14156-1]
DR   PDB; 9BAX; EM; 3.65 A; C/H=721-791.
DR   AlphaFoldDB; Q14156; -.
DR   EMDB; EMD-44413; -.
DR   SMR; Q14156; -.
DR   BioGRID; 116779; 131.
DR   FunCoup; Q14156; 2671.
DR   IntAct; Q14156; 61.
DR   MINT; Q14156; -.
DR   STRING; 9606.ENSP00000254624; -.
DR   GlyGen; Q14156; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q14156; -.
DR   PhosphoSitePlus; Q14156; -.
DR   SwissPalm; Q14156; -.
DR   BioMuta; EFR3A; -.
DR   DMDM; 122065174; -.
DR   jPOST; Q14156; -.
DR   MassIVE; Q14156; -.
DR   PaxDb; 9606-ENSP00000254624; -.
DR   PeptideAtlas; Q14156; -.
DR   ProteomicsDB; 59864; -. [Q14156-1]
DR   ProteomicsDB; 59865; -. [Q14156-2]
DR   ProteomicsDB; 59866; -. [Q14156-3]
DR   Pumba; Q14156; -.
DR   Antibodypedia; 14097; 118 antibodies from 17 providers.
DR   DNASU; 23167; -.
DR   Ensembl; ENST00000254624.10; ENSP00000254624.5; ENSG00000132294.16. [Q14156-1]
DR   Ensembl; ENST00000519656.1; ENSP00000428086.1; ENSG00000132294.16. [Q14156-2]
DR   GeneID; 23167; -.
DR   KEGG; hsa:23167; -.
DR   MANE-Select; ENST00000254624.10; ENSP00000254624.5; NM_015137.6; NP_055952.2.
DR   UCSC; uc003yte.4; human. [Q14156-1]
DR   AGR; HGNC:28970; -.
DR   ClinPGx; PA162384422; -.
DR   CTD; 23167; -.
DR   DisGeNET; 23167; -.
DR   GeneCards; EFR3A; -.
DR   HGNC; HGNC:28970; EFR3A.
DR   HPA; ENSG00000132294; Tissue enhanced (retina).
DR   MalaCards; EFR3A; -.
DR   MIM; 611798; gene.
DR   OpenTargets; ENSG00000132294; -.
DR   VEuPathDB; HostDB:ENSG00000132294; -.
DR   eggNOG; KOG1877; Eukaryota.
DR   GeneTree; ENSGT00390000002143; -.
DR   HOGENOM; CLU_012674_1_0_1; -.
DR   InParanoid; Q14156; -.
DR   OMA; QMCHANP; -.
DR   OrthoDB; 19232at2759; -.
DR   PAN-GO; Q14156; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q14156; -.
DR   PathwayCommons; Q14156; -.
DR   SignaLink; Q14156; -.
DR   SIGNOR; Q14156; -.
DR   Agora; ENSG00000132294; -.
DR   BioGRID-ORCS; 23167; 264 hits in 1175 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   ChiTaRS; EFR3A; human.
DR   GenomeRNAi; 23167; -.
DR   Pharos; Q14156; Tbio.
DR   PRO; PR:Q14156; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q14156; protein.
DR   Bgee; ENSG00000132294; Expressed in choroid plexus epithelium and 207 other cell types or tissues.
DR   ExpressionAtlas; Q14156; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; TAS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR   GO; GO:0016082; P:synaptic vesicle priming; IEA:Ensembl.
DR   FunFam; 1.25.10.10:FF:000347; EFR3 homolog A (S. cerevisiae); 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR049152; EFR3-like_ARM.
DR   InterPro; IPR051851; EFR3_Homologs.
DR   PANTHER; PTHR12444:SF1; PROTEIN EFR3 HOMOLOG A; 1.
DR   PANTHER; PTHR12444; PROTEIN EFR3 HOMOLOG CMP44E; 1.
DR   Pfam; PF21052; EFR3_ARM; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PDBsum; 9BAX; -.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Autism; Autism spectrum disorder;
KW   Cell membrane; Cytoplasm; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Proteomics identification; Reference proteome.
FT   CHAIN           1..821
FT                   /note="Protein EFR3 homolog A"
FT                   /id="PRO_0000050724"
FT   MOD_RES         360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BG67"
FT   MOD_RES         363
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BG67"
FT   MOD_RES         422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976"
FT   MOD_RES         694
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..36
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_022217"
FT   VAR_SEQ         619..662
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_022218"
FT   VARIANT         14
FT                   /note="P -> R"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075101"
FT   VARIANT         50
FT                   /note="K -> E"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075102"
FT   VARIANT         55
FT                   /note="G -> C (in dbSNP:rs749463078)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075103"
FT   VARIANT         70
FT                   /note="R -> C (in dbSNP:rs1212454955)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075104"
FT   VARIANT         100
FT                   /note="F -> L"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075105"
FT   VARIANT         118
FT                   /note="L -> P (in dbSNP:rs1818455073)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075106"
FT   VARIANT         123
FT                   /note="F -> L (in dbSNP:rs1323253445)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075107"
FT   VARIANT         194
FT                   /note="M -> V (in dbSNP:rs780864616)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075108"
FT   VARIANT         243
FT                   /note="G -> A (in dbSNP:rs1818959817)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075109"
FT   VARIANT         268
FT                   /note="D -> G"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075110"
FT   VARIANT         320
FT                   /note="E -> D"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075111"
FT   VARIANT         321
FT                   /note="A -> S (in dbSNP:rs774959333)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075112"
FT   VARIANT         337
FT                   /note="V -> L"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075113"
FT   VARIANT         338
FT                   /note="F -> S (in dbSNP:rs1395349665)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075114"
FT   VARIANT         354
FT                   /note="N -> D (in dbSNP:rs754610866)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075115"
FT   VARIANT         358
FT                   /note="G -> R (in dbSNP:rs2270877)"
FT                   /id="VAR_047247"
FT   VARIANT         365
FT                   /note="N -> D (in dbSNP:rs1051221)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:17974005"
FT                   /id="VAR_047248"
FT   VARIANT         451
FT                   /note="T -> M (in dbSNP:rs770980074)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075116"
FT   VARIANT         504
FT                   /note="D -> G"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075117"
FT   VARIANT         508
FT                   /note="L -> P"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075118"
FT   VARIANT         510
FT                   /note="I -> V"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075119"
FT   VARIANT         528
FT                   /note="Q -> R (in dbSNP:rs1820754943)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075120"
FT   VARIANT         532
FT                   /note="R -> W (in dbSNP:rs779475356)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075121"
FT   VARIANT         534
FT                   /note="I -> T (in dbSNP:rs374094815)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075122"
FT   VARIANT         570
FT                   /note="D -> V"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075123"
FT   VARIANT         646
FT                   /note="M -> V (in dbSNP:rs759848268)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075124"
FT   VARIANT         785
FT                   /note="T -> A (in dbSNP:rs1467962026)"
FT                   /evidence="ECO:0000269|PubMed:24860643"
FT                   /id="VAR_075125"
FT   MUTAGEN         6..9
FT                   /note="CCCC->SSSS: Induces localization to the cytosol."
FT                   /evidence="ECO:0000269|PubMed:23229899,
FT                   ECO:0000269|PubMed:25380825"
FT   CONFLICT        486
FT                   /note="L -> P (in Ref. 2; CAH56143)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        696
FT                   /note="R -> G (in Ref. 2; CAH56143)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   821 AA;  92924 MW;  A5FCEF6A189A5145 CRC64;
     MPTRVCCCCS ALRPRYKRLV DNIFPEDPKD GLVKTDMEKL TFYAVSAPEK LDRIGSYLAE
     RLSRDVVRHR SGYVLIAMEA LDQLLMACHS QSIKPFVESF LHMVAKLLES GEPKLQVLGT
     NSFVKFANIE EDTPSYHRRY DFFVSRFSAM CHSCHSDPEI RTEIRIAGIR GIQGVVRKTV
     NDELRATIWE PQHMDKIVPS LLFNMQKIEE VDSRIGPPSS PSATDKEENP AVLAENCFRE
     LLGRATFGNM NNAVRPVFAH LDHHKLWDPN EFAVHCFKII MYSIQAQYSH HVIQEILGHL
     DARKKDAPRV RAGIIQVLLE AVAIAAKGSI GPTVLEVFNT LLKHLRLSVE FEANDLQGGS
     VGSVNLNTSS KDNDEKIVQN AIIQTIGFFG SNLPDYQRSE IMMFIMGKVP VFGTSTHTLD
     ISQLGDLGTR RIQIMLLRSL LMVTSGYKAK TIVTALPGSF LDPLLSPSLM EDYELRQLVL
     EVMHNLMDRH DNRAKLRGIR IIPDVADLKI KREKICRQDT SFMKKNGQQL YRHIYLGCKE
     EDNVQKNYEL LYTSLALITI ELANEEVVID LIRLAIALQD SAIINEDNLP MFHRCGIMAL
     VAAYLNFVSQ MIAVPAFCQH VSKVIEIRTM EAPYFLPEHI FRDKCMLPKS LEKHEKDLYF
     LTNKIAESLG GSGYSVERLS VPYVPQVTDE DRLSRRKSIV DTVSIQVDIL SNNVPSDDVV
     SNTEEITFEA LKKAIDTSGM EEQEKEKRRL VIEKFQKAPF EEIAAQCESK ANLLHDRLAQ
     ILELTIRPPP SPSGTLTITS GHAQYQSVPV YEMKFPDLCV Y
//