CERS2_BOVIN
ID CERS2_BOVIN Reviewed; 380 AA.
AC Q3ZBF8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ceramide synthase 2 {ECO:0000250|UniProtKB:Q96G23};
DE Short=CerS2 {ECO:0000250|UniProtKB:Q96G23};
DE AltName: Full=LAG1 longevity assurance homolog 2 {ECO:0000250|UniProtKB:Q96G23};
DE AltName: Full=Sphingosine N-acyltransferase CERS2 {ECO:0000305};
DE EC=2.3.1.24 {ECO:0000250|UniProtKB:Q96G23};
DE AltName: Full=Tumor metastasis-suppressor gene 1 protein {ECO:0000250|UniProtKB:Q96G23};
DE AltName: Full=Very-long-chain ceramide synthase CERS2 {ECO:0000305};
DE EC=2.3.1.297 {ECO:0000250|UniProtKB:Q924Z4, ECO:0000250|UniProtKB:Q96G23};
GN Name=CERS2 {ECO:0000250|UniProtKB:Q96G23};
GN Synonyms=LASS2 {ECO:0000250|UniProtKB:Q96G23};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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-long-chain fatty acyl-CoA (chain length C22-C27) (By similarity).
CC N-acylates sphinganine and sphingosine bases to form dihydroceramides
CC and ceramides in de novo synthesis and salvage pathways, respectively
CC (By similarity). Plays a non-redundant role in the synthesis of
CC ceramides with very-long-chain fatty acids in kidney, liver and brain.
CC Regulates the abundance of myelin-specific sphingolipids
CC galactosylceramide and sulfatide that affects myelin sheath
CC architecture and motor neuron functions (By similarity).
CC {ECO:0000250|UniProtKB:Q924Z4, ECO:0000250|UniProtKB:Q96G23}.
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:0000250|UniProtKB:Q924Z4,
CC ECO:0000250|UniProtKB:Q96G23};
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:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36536;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
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:0000250|UniProtKB:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33592;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
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:0000250|UniProtKB:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33352;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(15Z)-tetracosenoyl-CoA + sphinganine = CoA + H(+) + N-(15Z-
CC tetracosenoyl)-sphinganine; Xref=Rhea:RHEA:36667, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57817, ChEBI:CHEBI:74128,
CC ChEBI:CHEBI:74130; Evidence={ECO:0000250|UniProtKB:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36668;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
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:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36628;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
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:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36620;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxytetracosenoyl-CoA + sphinganine = CoA + H(+) + N-(2-
CC hydroxytetracosenoyl)-sphinganine; Xref=Rhea:RHEA:36767,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:74215, ChEBI:CHEBI:74216;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36768;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphinganine + tetracosenoyl-CoA = an N-
CC tetracosenoylsphinganine + CoA + H(+); Xref=Rhea:RHEA:36715,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:74146, ChEBI:CHEBI:74160;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36716;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexacosenoyl-CoA + sphinganine = CoA + H(+) + N-
CC hexacosenoylsphinganine; Xref=Rhea:RHEA:36719, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57817, ChEBI:CHEBI:74161,
CC ChEBI:CHEBI:74162; Evidence={ECO:0000250|UniProtKB:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36720;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphing-4-enine + tetracosanoyl-CoA = CoA + H(+) + N-
CC tetracosanoyl-sphing-4-enine; Xref=Rhea:RHEA:37115,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:72965;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37116;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphing-4-enine + tetracosenoyl-CoA = CoA + H(+) + N-
CC (tetracosenoyl)-sphing-4-enine; Xref=Rhea:RHEA:37123,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:74146, ChEBI:CHEBI:74457;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37124;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=heptadecasphing-4-enine + tetracosanoyl-CoA = CoA + H(+) + N-
CC tetracosanoyl-heptadecasphing-4-enine; Xref=Rhea:RHEA:36739,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052,
CC ChEBI:CHEBI:74166, ChEBI:CHEBI:74167;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36740;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
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:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23769;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sphing-4-enine = CoA + H(+) + N-
CC hexadecanoylsphing-4-enine; Xref=Rhea:RHEA:36687, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:72959; Evidence={ECO:0000250|UniProtKB:Q924Z4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36688;
CC Evidence={ECO:0000250|UniProtKB:Q924Z4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=octadecanoyl-CoA + sphing-4-enine = CoA + H(+) + N-
CC octadecanoylsphing-4-enine; Xref=Rhea:RHEA:36691, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:72961; Evidence={ECO:0000250|UniProtKB:Q924Z4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36692;
CC Evidence={ECO:0000250|UniProtKB:Q924Z4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + sphing-4-enine = CoA + H(+) + N-eicosanoyl-
CC sphing-4-enine; Xref=Rhea:RHEA:45284, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:72962; Evidence={ECO:0000250|UniProtKB:Q924Z4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45285;
CC Evidence={ECO:0000250|UniProtKB:Q924Z4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sphinganine = CoA + H(+) + N-
CC hexadecanoylsphinganine; Xref=Rhea:RHEA:36539, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:67042; Evidence={ECO:0000250|UniProtKB:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36540;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
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:Q924Z4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36548;
CC Evidence={ECO:0000250|UniProtKB:Q924Z4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + sphinganine = CoA + H(+) + N-(9Z-
CC octadecenoyl)-sphinganine; Xref=Rhea:RHEA:36575, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:74100; Evidence={ECO:0000250|UniProtKB:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36576;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + sphinganine = CoA + H(+) + N-
CC eicosanoylsphinganine; Xref=Rhea:RHEA:36555, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:67027; Evidence={ECO:0000250|UniProtKB:Q96G23};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36556;
CC Evidence={ECO:0000250|UniProtKB:Q96G23};
CC -!- ACTIVITY REGULATION: Ceramide synthase activity is inhibited by
CC sphingosine-1-phosphate. {ECO:0000250|UniProtKB:Q96G23}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:Q96G23}.
CC -!- SUBUNIT: Interacts with ATP6V0C, ASGR1, ASGR2 and SLC22A1/OCT1.
CC Interacts with ELOV1, HSD17B12 and TECR (By similarity). Interacts with
CC NDUFS2 (By similarity). {ECO:0000250|UniProtKB:Q924Z4,
CC ECO:0000250|UniProtKB:Q96G23}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96G23}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The last loop motif confers selectivity toward behenoyl-CoA
CC (docosanoyl-CoA; C22:0-CoA) and lignoceroyl-CoA (tetracosanoyl-CoA;
CC C24:0-CoA) as acyl donors. {ECO:0000250|UniProtKB:Q96G23}.
CC -!- PTM: Acetylated. Deacetylation by SIRT3 increases enzyme activity and
CC promotes mitochondrial ceramide accumulation.
CC {ECO:0000250|UniProtKB:Q924Z4}.
CC -!- PTM: Phosphorylated at the C-terminus by CK2, leading to increase the
CC ceramide synthase activity. {ECO:0000250|UniProtKB:Q96G23}.
CC -!- CAUTION: Contains a predicted homeobox domain which is degenerated and
CC lacks residues that are important for DNA-binding. 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:Q96G23, ECO:0000305}.
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DR EMBL; BC103330; AAI03331.1; -; mRNA.
DR RefSeq; NP_001029839.1; NM_001034667.1.
DR RefSeq; XP_005203977.1; XM_005203920.3.
DR RefSeq; XP_005203978.1; XM_005203921.3.
DR AlphaFoldDB; Q3ZBF8; -.
DR SMR; Q3ZBF8; -.
DR STRING; 9913.ENSBTAP00000000109; -.
DR PaxDb; Q3ZBF8; -.
DR PRIDE; Q3ZBF8; -.
DR Ensembl; ENSBTAT00000000109; ENSBTAP00000000109; ENSBTAG00000000099.
DR GeneID; 539223; -.
DR KEGG; bta:539223; -.
DR CTD; 29956; -.
DR VEuPathDB; HostDB:ENSBTAG00000000099; -.
DR VGNC; VGNC:27224; CERS2.
DR eggNOG; KOG1607; Eukaryota.
DR GeneTree; ENSGT01030000234515; -.
DR HOGENOM; CLU_028277_1_1_1; -.
DR InParanoid; Q3ZBF8; -.
DR OMA; CTNCYID; -.
DR OrthoDB; 987268at2759; -.
DR TreeFam; TF314319; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000000099; Expressed in midbrain and 103 other tissues.
DR ExpressionAtlas; Q3ZBF8; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
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; SM00724; TLC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50922; TLC; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..380
FT /note="Ceramide synthase 2"
FT /id="PRO_0000240446"
FT TOPO_DOM 1..40
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96G23"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96G23"
FT DOMAIN 131..332
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 67..128
FT /note="Homeobox-like"
FT /evidence="ECO:0000305"
FT REGION 338..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 291..300
FT /note="Last loop motif"
FT /evidence="ECO:0000250|UniProtKB:Q96G23"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96G23"
FT MOD_RES 346
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96G23"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96G23"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96G23"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 380 AA; 44903 MW; 40AC52B2A153B750 CRC64;
MLQTLHDYFW WERLWLPVNL TWADLEDRDG RVYAKASDLY ITLPLALLFL IIRYFFELYV
ATPLAALLNV KEKTRLRAPP NPTLEHFYMT SGKQPKQADV ELLSRQSGLS GRQVERWFRR
RRNQDRPSLL KKFREASWRF TFYLIAFIAG TAVIVDKPWF YDLRKVWEGY PIQSIIPSQY
WYYMIELSFY WSLLFSIASD VKRKDFKEQI IHHVATIILI SFSWFANYVR AGTLIMALHD
SSDYLLESAK MFNYAGWKNT CNNIFIVFAI VFIITRLVIL PFWILHCTLV YPLELYPAFF
GYYFFNFMMG VLQLLHIFWA YLILRMAHKF ITGKVVEDER SDREETESSE GEEAAAGGGA
KNRPLANGHP ILNNNHRKND
