CERS3_HUMAN
ID CERS3_HUMAN Reviewed; 383 AA.
AC Q8IU89; Q8NE64; Q8NEN6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ceramide synthase 3 {ECO:0000303|PubMed:17977534};
DE Short=CerS3 {ECO:0000303|PubMed:17977534};
DE AltName: Full=Dihydroceramide synthase 3 {ECO:0000305};
DE AltName: Full=LAG1 longevity assurance homolog 3 {ECO:0000250|UniProtKB:Q1A3B0};
DE AltName: Full=Sphingosine N-acyltransferase CERS3 {ECO:0000305};
DE EC=2.3.1.24 {ECO:0000250|UniProtKB:Q1A3B0};
DE AltName: Full=Ultra-long-chain ceramide synthase CERS3 {ECO:0000305};
DE EC=2.3.1.298 {ECO:0000269|PubMed:22038835};
DE AltName: Full=Very-long-chain ceramide synthase CERS3 {ECO:0000305};
DE EC=2.3.1.297 {ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:22038835, ECO:0000269|PubMed:26887952};
GN Name=CERS3 {ECO:0000303|PubMed:17977534, ECO:0000312|HGNC:HGNC:23752};
GN Synonyms=LASS3 {ECO:0000250|UniProtKB:Q1A3B0};
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 GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-370.
RC TISSUE=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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17977534; DOI=10.1016/j.febslet.2007.10.018;
RA Lahiri S., Lee H., Mesicek J., Fuks Z., Haimovitz-Friedman A.,
RA Kolesnick R.N., Futerman A.H.;
RT "Kinetic characterization of mammalian ceramide synthases: determination of
RT K(m) values towards sphinganine.";
RL FEBS Lett. 581:5289-5294(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=22038835; DOI=10.1093/hmg/ddr494;
RA Jennemann R., Rabionet M., Gorgas K., Epstein S., Dalpke A., Rothermel U.,
RA Bayerle A., van der Hoeven F., Imgrund S., Kirsch J., Nickel W.,
RA Willecke K., Riezman H., Groene H.J., Sandhoff R.;
RT "Loss of ceramide synthase 3 causes lethal skin barrier disruption.";
RL Hum. Mol. Genet. 21:586-608(2012).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN ARCI9.
RX PubMed=23754960; DOI=10.1371/journal.pgen.1003536;
RA Radner F.P., Marrakchi S., Kirchmeier P., Kim G.J., Ribierre F., Kamoun B.,
RA Abid L., Leipoldt M., Turki H., Schempp W., Heilig R., Lathrop M.,
RA Fischer J.;
RT "Mutations in CERS3 cause autosomal recessive congenital ichthyosis in
RT humans.";
RL PLoS Genet. 9:E1003536-E1003536(2013).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TOPOLOGY, PHOSPHORYLATION AT
RP SER-340, AND MUTAGENESIS OF SER-340.
RX PubMed=26887952; DOI=10.1074/jbc.m115.695858;
RA Sassa T., Hirayama T., Kihara A.;
RT "Enzyme activities of the ceramide synthases CERS2-6 are regulated by
RT phosphorylation in the C-terminal region.";
RL J. Biol. Chem. 291:7477-7487(2016).
CC -!- FUNCTION: Ceramide synthase that catalyzes the transfer of the acyl
CC chain from acyl-CoA to a sphingoid base, with high selectivity toward
CC very- and ultra-long-chain fatty acyl-CoA (chain length greater than
CC C22) (PubMed:17977534, PubMed:22038835, PubMed:26887952). N-acylates
CC sphinganine and sphingosine bases to form dihydroceramides and
CC ceramides in de novo synthesis and salvage pathways, respectively
CC (PubMed:17977534, PubMed:22038835, PubMed:26887952). It is crucial for
CC the synthesis of ultra-long-chain ceramides in the epidermis, to
CC maintain epidermal lipid homeostasis and terminal differentiation
CC (PubMed:23754960). {ECO:0000269|PubMed:17977534,
CC ECO:0000269|PubMed:22038835, ECO:0000269|PubMed:23754960,
CC ECO:0000269|PubMed:26887952}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingoid base + a very long-chain fatty acyl-CoA = an N-
CC (very-long-chain fatty acyl)-sphingoid base + CoA + H(+);
CC Xref=Rhea:RHEA:61480, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:84410, ChEBI:CHEBI:138261, ChEBI:CHEBI:144712;
CC EC=2.3.1.297; Evidence={ECO:0000269|PubMed:17977534,
CC ECO:0000269|PubMed:22038835, ECO:0000269|PubMed:26887952};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + sphinganine = CoA + H(+) + N-
CC docosanoylsphinganine; Xref=Rhea:RHEA:36535, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57817, ChEBI:CHEBI:65059,
CC ChEBI:CHEBI:67021; Evidence={ECO:0000250|UniProtKB:Q1A3B0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36536;
CC Evidence={ECO:0000250|UniProtKB:Q1A3B0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphinganine + tetracosanoyl-CoA = CoA + H(+) + N-
CC tetracosanoylsphinganine; Xref=Rhea:RHEA:33591, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:52961, ChEBI:CHEBI:57287, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:65052; Evidence={ECO:0000269|PubMed:17977534,
CC ECO:0000269|PubMed:26887952};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33592;
CC Evidence={ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:26887952};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexacosanoyl-CoA + sphinganine = CoA + H(+) + N-
CC hexacosanoylsphinganine; Xref=Rhea:RHEA:33351, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:52962, ChEBI:CHEBI:57287, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:64868; Evidence={ECO:0000269|PubMed:22038835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33352;
CC Evidence={ECO:0000269|PubMed:22038835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxydocosanoyl-CoA + sphinganine = CoA + H(+) + N-(2-
CC hydroxydocosanoyl)-sphinganine; Xref=Rhea:RHEA:36619,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:67023, ChEBI:CHEBI:74117;
CC Evidence={ECO:0000250|UniProtKB:Q1A3B0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36620;
CC Evidence={ECO:0000250|UniProtKB:Q1A3B0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxytetracosanoyl-CoA + sphinganine = CoA + H(+) + N-(2-
CC hydroxytetracosanoyl)-sphinganine; Xref=Rhea:RHEA:36627,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:52371, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57817, ChEBI:CHEBI:74118;
CC Evidence={ECO:0000250|UniProtKB:Q1A3B0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36628;
CC Evidence={ECO:0000250|UniProtKB:Q1A3B0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingoid base + an ultra-long-chain fatty acyl-CoA = an N-
CC (ultra-long-chain-acyl)-sphingoid base + CoA + H(+);
CC Xref=Rhea:RHEA:61492, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:84410, ChEBI:CHEBI:143018, ChEBI:CHEBI:144713;
CC EC=2.3.1.298; Evidence={ECO:0000269|PubMed:22038835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61493;
CC Evidence={ECO:0000269|PubMed:22038835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=octacosanoyl-CoA + sphinganine = CoA + H(+) + N-
CC (octacosanoyl)-sphinganine; Xref=Rhea:RHEA:36675, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57817, ChEBI:CHEBI:72019,
CC ChEBI:CHEBI:74141; Evidence={ECO:0000269|PubMed:22038835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36676;
CC Evidence={ECO:0000269|PubMed:22038835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + sphing-4-enine = an N-acylsphing-4-enine +
CC CoA + H(+); Xref=Rhea:RHEA:23768, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:57287, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:77636; EC=2.3.1.24;
CC Evidence={ECO:0000250|UniProtKB:Q1A3B0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23769;
CC Evidence={ECO:0000250|UniProtKB:Q1A3B0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=octadecanoyl-CoA + sphinganine = CoA + H(+) + N-
CC (octadecanoyl)-sphinganine; Xref=Rhea:RHEA:36547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:67033; Evidence={ECO:0000250|UniProtKB:Q1A3B0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36548;
CC Evidence={ECO:0000250|UniProtKB:Q1A3B0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyoctadecanoyl-CoA + sphinganine = CoA + H(+) + N-(2-
CC hydroxyoctadecanoyl)-sphinganine; Xref=Rhea:RHEA:36615,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:67034, ChEBI:CHEBI:74116;
CC Evidence={ECO:0000250|UniProtKB:Q1A3B0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36616;
CC Evidence={ECO:0000250|UniProtKB:Q1A3B0};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 uM for sphinganine {ECO:0000269|PubMed:17977534};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:22038835,
CC ECO:0000269|PubMed:26887952}.
CC -!- INTERACTION:
CC Q8IU89; Q99519: NEU1; NbExp=3; IntAct=EBI-18202821, EBI-721517;
CC Q8IU89; Q8N138: ORMDL3; NbExp=3; IntAct=EBI-18202821, EBI-721750;
CC Q8IU89; Q9H0N5: PCBD2; NbExp=3; IntAct=EBI-18202821, EBI-634289;
CC Q8IU89; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-18202821, EBI-2823239;
CC Q8IU89; Q96FB2; NbExp=3; IntAct=EBI-18202821, EBI-2857623;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q1A3B0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the epidermis, where it localizes at
CC the interface between the stratum granulosum and the stratum corneum
CC (at protein level). {ECO:0000269|PubMed:23754960}.
CC -!- DISEASE: Ichthyosis, congenital, autosomal recessive 9 (ARCI9)
CC [MIM:615023]: A form of autosomal recessive congenital ichthyosis, a
CC disorder of keratinization with abnormal differentiation and
CC desquamation of the epidermis, resulting in abnormal skin scaling over
CC the whole body. The main skin phenotypes are lamellar ichthyosis (LI)
CC and non-bullous congenital ichthyosiform erythroderma (NCIE), although
CC phenotypic overlap within the same patient or among patients from the
CC same family can occur. Lamellar ichthyosis is a condition often
CC associated with an embedment in a collodion-like membrane at birth;
CC skin scales later develop, covering the entire body surface. Non-
CC bullous congenital ichthyosiform erythroderma characterized by fine
CC whitish scaling on an erythrodermal background; larger brownish scales
CC are present on the buttocks, neck and legs.
CC {ECO:0000269|PubMed:23754960}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- CAUTION: Contains a predicted homeobox domain which is degenerated,
CC lacking residues important for DNA-binding. Moreover, the protein
CC localizes in the endoplasmic reticulum and not in the nucleus, which
CC also argues against homeobox function (By similarity).
CC {ECO:0000250|UniProtKB:Q1A3B0, ECO:0000305}.
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DR EMBL; AC015723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028703; AAH28703.1; -; mRNA.
DR EMBL; BC034500; AAH34500.1; -; mRNA.
DR EMBL; BC034970; AAH34970.1; -; mRNA.
DR CCDS; CCDS10384.1; -.
DR RefSeq; NP_001277270.1; NM_001290341.2.
DR RefSeq; NP_001277271.1; NM_001290342.2.
DR RefSeq; NP_001277272.1; NM_001290343.1.
DR RefSeq; NP_849164.2; NM_178842.4.
DR RefSeq; XP_016877492.1; XM_017022003.1.
DR RefSeq; XP_016877493.1; XM_017022004.1.
DR AlphaFoldDB; Q8IU89; -.
DR SMR; Q8IU89; -.
DR BioGRID; 128485; 71.
DR IntAct; Q8IU89; 5.
DR STRING; 9606.ENSP00000284382; -.
DR SwissLipids; SLP:000000259; -.
DR iPTMnet; Q8IU89; -.
DR PhosphoSitePlus; Q8IU89; -.
DR BioMuta; CERS3; -.
DR DMDM; 322510043; -.
DR MassIVE; Q8IU89; -.
DR PaxDb; Q8IU89; -.
DR PeptideAtlas; Q8IU89; -.
DR PRIDE; Q8IU89; -.
DR ProteomicsDB; 70524; -.
DR Antibodypedia; 1805; 157 antibodies from 30 providers.
DR DNASU; 204219; -.
DR Ensembl; ENST00000284382.8; ENSP00000284382.4; ENSG00000154227.14.
DR Ensembl; ENST00000394113.5; ENSP00000377672.3; ENSG00000154227.14.
DR Ensembl; ENST00000538112.6; ENSP00000437640.2; ENSG00000154227.14.
DR Ensembl; ENST00000679737.1; ENSP00000506641.1; ENSG00000154227.14.
DR GeneID; 204219; -.
DR KEGG; hsa:204219; -.
DR MANE-Select; ENST00000679737.1; ENSP00000506641.1; NM_001378789.1; NP_001365718.1.
DR UCSC; uc002bvz.4; human.
DR CTD; 204219; -.
DR DisGeNET; 204219; -.
DR GeneCards; CERS3; -.
DR GeneReviews; CERS3; -.
DR HGNC; HGNC:23752; CERS3.
DR HPA; ENSG00000154227; Group enriched (esophagus, lymphoid tissue, skin, testis, vagina).
DR MalaCards; CERS3; -.
DR MIM; 615023; phenotype.
DR MIM; 615276; gene.
DR neXtProt; NX_Q8IU89; -.
DR OpenTargets; ENSG00000154227; -.
DR Orphanet; 79394; Congenital non-bullous ichthyosiform erythroderma.
DR Orphanet; 363992; Ichthyosis-short stature-brachydactyly-microspherophakia syndrome.
DR PharmGKB; PA134873153; -.
DR VEuPathDB; HostDB:ENSG00000154227; -.
DR eggNOG; KOG1607; Eukaryota.
DR GeneTree; ENSGT01030000234515; -.
DR HOGENOM; CLU_028277_1_1_1; -.
DR InParanoid; Q8IU89; -.
DR OMA; DRPCRMK; -.
DR OrthoDB; 987268at2759; -.
DR PhylomeDB; Q8IU89; -.
DR TreeFam; TF314319; -.
DR BioCyc; MetaCyc:ENSG00000154227-MON; -.
DR BRENDA; 2.3.1.24; 2681.
DR BRENDA; 2.3.1.298; 2681.
DR PathwayCommons; Q8IU89; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR SignaLink; Q8IU89; -.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 204219; 8 hits in 1093 CRISPR screens.
DR ChiTaRS; CERS3; human.
DR GenomeRNAi; 204219; -.
DR Pharos; Q8IU89; Tbio.
DR PRO; PR:Q8IU89; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8IU89; protein.
DR Bgee; ENSG00000154227; Expressed in lower esophagus mucosa and 103 other tissues.
DR ExpressionAtlas; Q8IU89; baseline and differential.
DR Genevisible; Q8IU89; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0050291; F:sphingosine N-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0070268; P:cornification; ISS:UniProtKB.
DR GO; GO:0008544; P:epidermis development; ISS:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; IMP:UniProtKB.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR016439; Lag1/Lac1-like.
DR InterPro; IPR006634; TLC-dom.
DR PANTHER; PTHR12560; PTHR12560; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR PIRSF; PIRSF005225; LAG1_LAC1; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00724; TLC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50922; TLC; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Ichthyosis; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..383
FT /note="Ceramide synthase 3"
FT /id="PRO_0000185511"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26887952"
FT DOMAIN 130..331
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 66..127
FT /note="Homeobox-like"
FT /evidence="ECO:0000305"
FT REGION 342..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..357
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:26887952"
FT VARIANT 45
FT /note="Y -> C (in dbSNP:rs60405735)"
FT /id="VAR_061847"
FT VARIANT 342
FT /note="D -> G (in dbSNP:rs1023783)"
FT /id="VAR_057276"
FT VARIANT 370
FT /note="R -> G (in dbSNP:rs2439928)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_019328"
FT MUTAGEN 340
FT /note="S->A: Decreased phosphorylation."
FT /evidence="ECO:0000269|PubMed:26887952"
FT CONFLICT 144
FT /note="Missing (in Ref. 2; AAH34500)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="L -> R (in Ref. 2; AAH28703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 46316 MW; 6711189C189C8469 CRC64;
MFWTFKEWFW LERFWLPPTI KWSDLEDHDG LVFVKPSHLY VTIPYAFLLL IIRRVFEKFV
ASPLAKSFGI KETVRKVTPN TVLENFFKHS TRQPLQTDIY GLAKKCNLTE RQVERWFRSR
RNQERPSRLK KFQEACWRFA FYLMITVAGI AFLYDKPWLY DLWEVWNGYP KQPLLPSQYW
YYILEMSFYW SLLFRLGFDV KRKDFLAHII HHLAAISLMS FSWCANYIRS GTLVMIVHDV
ADIWLESAKM FSYAGWTQTC NTLFFIFSTI FFISRLIVFP FWILYCTLIL PMYHLEPFFS
YIFLNLQLMI LQVLHLYWGY YILKMLNRCI FMKSIQDVRS DDEDYEEEEE EEEEEATKGK
EMDCLKNGLR AERHLIPNGQ HGH
