EFR3A_HUMAN
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 03-AUG-2022, entry version 159.
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 FAM126 (FAM126A or FAM126B) (PubMed:26571211).
CC {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; 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; 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_001323553.1. [Q14156-2]
DR RefSeq; NP_001310483.1; NM_001323554.1. [Q14156-2]
DR RefSeq; NP_001310484.1; NM_001323555.1. [Q14156-2]
DR RefSeq; NP_001310485.1; NM_001323556.1. [Q14156-2]
DR RefSeq; NP_001310486.1; NM_001323557.1. [Q14156-2]
DR RefSeq; NP_001310487.1; NM_001323558.1.
DR RefSeq; NP_055952.2; NM_015137.5. [Q14156-1]
DR AlphaFoldDB; Q14156; -.
DR SMR; Q14156; -.
DR BioGRID; 116779; 113.
DR IntAct; Q14156; 33.
DR MINT; Q14156; -.
DR STRING; 9606.ENSP00000254624; -.
DR iPTMnet; Q14156; -.
DR PhosphoSitePlus; Q14156; -.
DR SwissPalm; Q14156; -.
DR BioMuta; EFR3A; -.
DR DMDM; 122065174; -.
DR EPD; Q14156; -.
DR jPOST; Q14156; -.
DR MassIVE; Q14156; -.
DR MaxQB; Q14156; -.
DR PaxDb; Q14156; -.
DR PeptideAtlas; Q14156; -.
DR PRIDE; Q14156; -.
DR ProteomicsDB; 59864; -. [Q14156-1]
DR ProteomicsDB; 59865; -. [Q14156-2]
DR ProteomicsDB; 59866; -. [Q14156-3]
DR Antibodypedia; 14097; 124 antibodies from 18 providers.
DR DNASU; 23167; -.
DR Ensembl; ENST00000254624.10; ENSP00000254624.5; ENSG00000132294.15. [Q14156-1]
DR Ensembl; ENST00000519656.1; ENSP00000428086.1; ENSG00000132294.15. [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 CTD; 23167; -.
DR GeneCards; EFR3A; -.
DR HGNC; HGNC:28970; EFR3A.
DR HPA; ENSG00000132294; Tissue enhanced (retina).
DR MIM; 611798; gene.
DR neXtProt; NX_Q14156; -.
DR OpenTargets; ENSG00000132294; -.
DR PharmGKB; PA162384422; -.
DR VEuPathDB; HostDB:ENSG00000132294; -.
DR eggNOG; KOG1877; Eukaryota.
DR GeneTree; ENSGT00390000002143; -.
DR HOGENOM; CLU_012674_1_0_1; -.
DR InParanoid; Q14156; -.
DR OMA; HRHSWVD; -.
DR OrthoDB; 173880at2759; -.
DR PhylomeDB; Q14156; -.
DR TreeFam; TF314098; -.
DR PathwayCommons; Q14156; -.
DR SignaLink; Q14156; -.
DR BioGRID-ORCS; 23167; 259 hits in 1095 CRISPR screens.
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 205 other tissues.
DR ExpressionAtlas; Q14156; baseline and differential.
DR Genevisible; Q14156; HS.
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; TAS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autism; Autism spectrum disorder; Cell membrane;
KW Cytoplasm; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW 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"
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"
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"
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"
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
