ELOV5_MOUSE
ID ELOV5_MOUSE Reviewed; 299 AA.
AC Q8BHI7; Q8BLG6; Q8BUE3; Q8R5D3;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Elongation of very long chain fatty acids protein 5 {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000305};
DE EC=2.3.1.199 {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:24184513};
DE AltName: Full=3-keto acyl-CoA synthase Elovl5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE AltName: Full=ELOVL fatty acid elongase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE Short=ELOVL FA elongase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 5 {ECO:0000255|HAMAP-Rule:MF_03205};
GN Name=Elovl5 {ECO:0000255|HAMAP-Rule:MF_03205};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Embryo, Embryoid bodies, Kidney, Mammary gland, Skin, and
RC Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24184513; DOI=10.1016/j.bbalip.2013.10.013;
RA Ichi I., Kono N., Arita Y., Haga S., Arisawa K., Yamano M., Nagase M.,
RA Fujiwara Y., Arai H.;
RT "Identification of genes and pathways involved in the synthesis of Mead
RT acid (20:3n-9), an indicator of essential fatty acid deficiency.";
RL Biochim. Biophys. Acta 1841:204-213(2014).
CC -!- FUNCTION: Catalyzes the first and rate-limiting reaction of the four
CC reactions that constitute the long-chain fatty acids elongation cycle.
CC This endoplasmic reticulum-bound enzymatic process allows the addition
CC of 2 carbons to the chain of long- and very long-chain fatty acids
CC (VLCFAs) per cycle. Condensing enzyme that acts specifically toward
CC polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6)
CC acyl-CoA. May participate in the production of monounsaturated and of
CC polyunsaturated VLCFAs of different chain lengths that are involved in
CC multiple biological processes as precursors of membrane lipids and
CC lipid mediators (By similarity). In conditions where the essential
CC linoleic and alpha linoleic fatty acids are lacking it is also involved
CC in the synthesis of Mead acid from oleic acid (PubMed:24184513).
CC {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:24184513}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC EC=2.3.1.199; Evidence={ECO:0000255|HAMAP-Rule:MF_03205,
CC ECO:0000269|PubMed:24184513};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000269|PubMed:24184513};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA =
CC (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:35379, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57363, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:71481; Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35380;
CC Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA =
CC (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36523, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:74034,
CC ChEBI:CHEBI:74054; Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524;
CC Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(11Z)-
CC octadecenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39675,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:61540, ChEBI:CHEBI:76555;
CC Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676;
CC Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = (11Z)-3-
CC oxoicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36511,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57387, ChEBI:CHEBI:74011;
CC Evidence={ECO:0000269|PubMed:24184513};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512;
CC Evidence={ECO:0000269|PubMed:24184513};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(13Z)-
CC eicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39679, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:75121, ChEBI:CHEBI:76559;
CC Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39680;
CC Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z)-
CC 3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36503,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:57384, ChEBI:CHEBI:74012;
CC Evidence={ECO:0000269|PubMed:24184513};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504;
CC Evidence={ECO:0000269|PubMed:24184513};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + H(+) + malonyl-CoA =
CC (8Z,11Z,14Z,17Z)-3-oxoicosatetraenoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:35391, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:71489,
CC ChEBI:CHEBI:71491; Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35392;
CC Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H(+) + malonyl-CoA =
CC (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36475, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:73852; Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476;
CC Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + H(+) + malonyl-CoA
CC = (7Z,10Z,13Z,16Z,19Z)-3-oxodocosapentaenoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36483, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:73862,
CC ChEBI:CHEBI:73863; Evidence={ECO:0000250|UniProtKB:Q9NYP7};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03205}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03205}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03205}. Cell projection, dendrite
CC {ECO:0000255|HAMAP-Rule:MF_03205}. Note=In Purkinje cells, the protein
CC localizes to the soma and proximal portion of the dendritic tree.
CC {ECO:0000255|HAMAP-Rule:MF_03205}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL5 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03205}.
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DR EMBL; AK028761; BAC26105.1; -; mRNA.
DR EMBL; AK045274; BAC32290.1; -; mRNA.
DR EMBL; AK051580; BAC34682.1; -; mRNA.
DR EMBL; AK085663; BAC39499.1; -; mRNA.
DR EMBL; AK085696; BAC39509.1; -; mRNA.
DR EMBL; AK088153; BAC40176.1; -; mRNA.
DR EMBL; AK162451; BAE36925.1; -; mRNA.
DR EMBL; AK168987; BAE40787.1; -; mRNA.
DR EMBL; BC022911; AAH22911.1; -; mRNA.
DR CCDS; CCDS23355.1; -.
DR RefSeq; NP_599016.2; NM_134255.3.
DR RefSeq; XP_006511463.1; XM_006511400.1.
DR AlphaFoldDB; Q8BHI7; -.
DR SMR; Q8BHI7; -.
DR BioGRID; 213059; 3.
DR STRING; 10090.ENSMUSP00000034904; -.
DR SwissLipids; SLP:000000811; -.
DR iPTMnet; Q8BHI7; -.
DR PhosphoSitePlus; Q8BHI7; -.
DR SwissPalm; Q8BHI7; -.
DR EPD; Q8BHI7; -.
DR jPOST; Q8BHI7; -.
DR MaxQB; Q8BHI7; -.
DR PaxDb; Q8BHI7; -.
DR PeptideAtlas; Q8BHI7; -.
DR PRIDE; Q8BHI7; -.
DR ProteomicsDB; 277822; -.
DR Antibodypedia; 4471; 361 antibodies from 28 providers.
DR DNASU; 68801; -.
DR Ensembl; ENSMUST00000034904; ENSMUSP00000034904; ENSMUSG00000032349.
DR GeneID; 68801; -.
DR KEGG; mmu:68801; -.
DR UCSC; uc009qtn.2; mouse.
DR CTD; 60481; -.
DR MGI; MGI:1916051; Elovl5.
DR VEuPathDB; HostDB:ENSMUSG00000032349; -.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR InParanoid; Q8BHI7; -.
DR OMA; WVVIDIN; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q8BHI7; -.
DR TreeFam; TF323454; -.
DR Reactome; R-MMU-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-MMU-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00658; -.
DR BioGRID-ORCS; 68801; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Elovl5; mouse.
DR PRO; PR:Q8BHI7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BHI7; protein.
DR Bgee; ENSMUSG00000032349; Expressed in vestibular membrane of cochlear duct and 261 other tissues.
DR ExpressionAtlas; Q8BHI7; baseline and differential.
DR Genevisible; Q8BHI7; MM.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0097447; C:dendritic tree; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0009922; F:fatty acid elongase activity; ISS:UniProtKB.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; ISS:UniProtKB.
DR GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; ISS:UniProtKB.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IBA:GO_Central.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; ISS:UniProtKB.
DR HAMAP; MF_03205; VLCF_elongase_5; 1.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033677; ELOVL5.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR PANTHER; PTHR11157:SF18; PTHR11157:SF18; 1.
DR Pfam; PF01151; ELO; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Endoplasmic reticulum;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..299
FT /note="Elongation of very long chain fatty acids protein 5"
FT /id="PRO_0000282840"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03205"
FT REGION 274..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYP7"
FT CONFLICT 36
FT /note="F -> L (in Ref. 1; BAC32290)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="C -> W (in Ref. 1; BAC39499)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="D -> E (in Ref. 1; BAC40176 and 2; AAH22911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 35332 MW; 176B88A3683E813B CRC64;
MEHFDASLST YFKAFLGPRD TRVKGWFLLD NYIPTFVCSV IYLLIVWLGP KYMKNRQPFS
CRGILQLYNL GLTLLSLYMF YELVTGVWEG KYNFFCQGTR SAGESDMKII RVLWWYYFSK
LIEFMDTFFF ILRKNNHQIT VLHVYHHATM LNIWWFVMNW VPCGHSYFGA TLNSFIHVLM
YSYYGLSSIP SMRPYLWWKK YITQGQLVQF VLTIIQTTCG VFWPCSFPLG WLFFQIGYMI
SLIALFTNFY IQTYNKKGAS RRKDHLKGHQ NGSVAAVNGH TNSFPSLENS VKPRKQRKD
