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 24-JAN-2024, entry version 170. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 72. 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; 9606-ENSP00000284382; -. DR PeptideAtlas; Q8IU89; -. DR ProteomicsDB; 70524; -. DR Antibodypedia; 1805; 184 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 AGR; HGNC:23752; -. DR CTD; 204219; -. DR DisGeNET; 204219; -. DR GeneCards; CERS3; -. DR GeneReviews; CERS3; -. DR HGNC; HGNC:23752; CERS3. DR HPA; ENSG00000154227; Tissue enhanced (esophagus, skin, vagina). DR MalaCards; CERS3; -. DR MIM; 615023; phenotype. DR MIM; 615276; gene. DR neXtProt; NX_Q8IU89; -. DR OpenTargets; ENSG00000154227; -. DR Orphanet; 79394; Congenital 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; DHDGLIF; -. DR OrthoDB; 460400at2759; -. DR PhylomeDB; Q8IU89; -. DR TreeFam; TF314319; -. DR BioCyc; MetaCyc:ENSG00000154227-MONOMER; -. 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; 9 hits in 1176 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 105 other cell types or tissues. DR ExpressionAtlas; Q8IU89; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. 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 Gene3D; 1.10.10.60; Homeodomain-like; 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:SF18; CERAMIDE SYNTHASE 3; 1. DR PANTHER; PTHR12560; LONGEVITY ASSURANCE FACTOR 1 LAG1; 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; Homeodomain-like; 1. DR PROSITE; PS50922; TLC; 1. DR Genevisible; Q8IU89; HS. 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 //