FACR1_HUMAN
ID FACR1_HUMAN Reviewed; 515 AA.
AC Q8WVX9; D3DQW8; Q5CZA3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Fatty acyl-CoA reductase 1 {ECO:0000305|PubMed:15220348};
DE EC=1.2.1.84 {ECO:0000269|PubMed:15220348, ECO:0000269|PubMed:24108123};
DE AltName: Full=Male sterility domain-containing protein 2 {ECO:0000312|HGNC:HGNC:26222};
GN Name=FAR1 {ECO:0000312|HGNC:HGNC:26222};
GN Synonyms=MLSTD2 {ECO:0000312|HGNC:HGNC:26222};
GN ORFNames=UNQ2423/PRO4981 {ECO:0000312|EMBL:AAQ89144.1};
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 [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15220348; DOI=10.1074/jbc.m406225200;
RA Cheng J.B., Russell D.W.;
RT "Mammalian wax biosynthesis: I. Identification of two fatty acyl-coenzyme A
RT reductases with different substrate specificities and tissue
RT distributions.";
RL J. Biol. Chem. 279:37789-37797(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zheng H., Xie Y., Mao Y.;
RT "Cloning and characterization of a putative fatty acyl reductase.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Endometrial tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [7]
RP FUNCTION, INDUCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20071337; DOI=10.1074/jbc.m109.083311;
RA Honsho M., Asaoku S., Fujiki Y.;
RT "Posttranslational regulation of fatty acyl-CoA reductase 1, Far1, controls
RT ether glycerophospholipid synthesis.";
RL J. Biol. Chem. 285:8537-8542(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION
RP WITH PEX19, INDUCTION, AND REGION.
RX PubMed=24108123; DOI=10.1074/jbc.m113.498345;
RA Honsho M., Asaoku S., Fukumoto K., Fujiki Y.;
RT "Topogenesis and homeostasis of fatty acyl-CoA reductase 1.";
RL J. Biol. Chem. 288:34588-34598(2013).
RN [10]
RP INVOLVEMENT IN PFCRD, VARIANTS PFCRD 165-GLU--PRO-169 DELINS ASP;
RP 263-ARG--TYR-515 DEL AND GLY-365, AND CHARACTERIZATION OF VARIANTS PFCRD
RP 165-GLU--PRO-169 DELINS ASP; 263-ARG--TYR-515 DEL AND GLY-365.
RX PubMed=25439727; DOI=10.1016/j.ajhg.2014.10.003;
RA Buchert R., Tawamie H., Smith C., Uebe S., Innes A.M., Al Hallak B.,
RA Ekici A.B., Sticht H., Schwarze B., Lamont R.E., Parboosingh J.S.,
RA Bernier F.P., Abou Jamra R.;
RT "A peroxisomal disorder of severe intellectual disability, epilepsy, and
RT cataracts due to fatty acyl-CoA reductase 1 deficiency.";
RL Am. J. Hum. Genet. 95:602-610(2014).
RN [11]
RP VARIANTS CSPSD CYS-480; HIS-480 AND LEU-480, CHARACTERIZATION OF VARIANTS
RP CSPSD CYS-480 AND HIS-480, INVOLVEMENT IN CSPSD, AND FUNCTION.
RX PubMed=33239752; DOI=10.1038/s41436-020-01027-3;
RG Undiagnosed Diseases Network;
RA Ferdinandusse S., McWalter K., Te Brinke H., Ijlst L., Mooijer P.M.,
RA Ruiter J.P.N., van Lint A.E.M., Pras-Raves M., Wever E., Millan F.,
RA Guillen Sacoto M.J., Begtrup A., Tarnopolsky M., Brady L., Ladda R.L.,
RA Sell S.L., Nowak C.B., Douglas J., Tian C., Ulm E., Perlman S., Drack A.V.,
RA Chong K., Martin N., Brault J., Brokamp E., Toro C., Gahl W.A.,
RA Macnamara E.F., Wolfe L., Waisfisz Q., Zwijnenburg P.J.G., Ziegler A.,
RA Barth M., Smith R., Ellingwood S., Gaebler-Spira D., Bakhtiari S.,
RA Kruer M.C., van Kampen A.H.C., Wanders R.J.A., Waterham H.R., Cassiman D.,
RA Vaz F.M.;
RT "An autosomal dominant neurological disorder caused by de novo variants in
RT FAR1 resulting in uncontrolled synthesis of ether lipids.";
RL Genet. Med. 23:740-750(2021).
CC -!- FUNCTION: Catalyzes the reduction of saturated and unsaturated C16 or
CC C18 fatty acyl-CoA to fatty alcohols (PubMed:15220348,
CC PubMed:24108123). It plays an essential role in the production of ether
CC lipids/plasmalogens which synthesis requires fatty alcohols
CC (PubMed:20071337, PubMed:24108123, PubMed:33239752). In parallel, it is
CC also required for wax monoesters production since fatty alcohols also
CC constitute a substrate for their synthesis (By similarity).
CC {ECO:0000250|UniProtKB:Q922J9, ECO:0000269|PubMed:15220348,
CC ECO:0000269|PubMed:20071337, ECO:0000269|PubMed:24108123,
CC ECO:0000269|PubMed:33239752}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain
CC primary fatty alcohol + CoA + 2 NADP(+); Xref=Rhea:RHEA:52716,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77396, ChEBI:CHEBI:83139; EC=1.2.1.84;
CC Evidence={ECO:0000269|PubMed:15220348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52717;
CC Evidence={ECO:0000305|PubMed:15220348};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoyl-CoA + 2 NADPH = CoA + hexadecan-1-ol + 2
CC NADP(+); Xref=Rhea:RHEA:36315, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.84;
CC Evidence={ECO:0000269|PubMed:15220348, ECO:0000269|PubMed:20071337};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36316;
CC Evidence={ECO:0000305|PubMed:15220348, ECO:0000305|PubMed:20071337};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 NADPH + octadecanoyl-CoA = CoA + 2 NADP(+) +
CC octadecan-1-ol; Xref=Rhea:RHEA:36319, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32154, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.84;
CC Evidence={ECO:0000250|UniProtKB:Q922J9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36320;
CC Evidence={ECO:0000250|UniProtKB:Q922J9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2 H(+) + 2 NADPH = (9Z)-octadecen-1-ol
CC + CoA + 2 NADP(+); Xref=Rhea:RHEA:36323, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:73504;
CC Evidence={ECO:0000250|UniProtKB:Q922J9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36324;
CC Evidence={ECO:0000250|UniProtKB:Q922J9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2 H(+) + 2 NADPH = (9Z,12Z)-
CC octadecadien-1-ol + CoA + 2 NADP(+); Xref=Rhea:RHEA:36363,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:73534;
CC Evidence={ECO:0000250|UniProtKB:Q922J9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36364;
CC Evidence={ECO:0000250|UniProtKB:Q922J9};
CC -!- SUBUNIT: Interacts with PEX19; PEX19 mediates the targeting of FAR1 to
CC peroxisomes. {ECO:0000269|PubMed:24108123}.
CC -!- INTERACTION:
CC Q8WVX9; P46379-2: BAG6; NbExp=3; IntAct=EBI-1045879, EBI-10988864;
CC Q8WVX9; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-1045879, EBI-21553822;
CC Q8WVX9; O14901: KLF11; NbExp=3; IntAct=EBI-1045879, EBI-948266;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:24108123}; Single-pass membrane protein
CC {ECO:0000269|PubMed:24108123}.
CC -!- INDUCTION: Down-regulated by ether lipids/plasmalogen that induce its
CC degradation (at protein level). {ECO:0000269|PubMed:20071337,
CC ECO:0000269|PubMed:24108123}.
CC -!- DISEASE: Peroxisomal fatty acyl-CoA reductase 1 disorder (PFCRD)
CC [MIM:616154]: An autosomal recessive metabolic disorder clinically
CC characterized by severe intellectual disability, early-onset epilepsy,
CC microcephaly, congenital cataracts, growth retardation, and spasticity.
CC {ECO:0000269|PubMed:25439727}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Cataracts, spastic paraparesis, and speech delay (CSPSD)
CC [MIM:619338]: An autosomal dominant disease characterized by bilateral
CC cataracts apparent at birth or in infancy, spastic paraparesis, truncal
CC hypotonia, delayed psychomotor development, and speech delay.
CC {ECO:0000269|PubMed:33239752}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000305}.
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DR EMBL; AY600449; AAT42129.1; -; mRNA.
DR EMBL; AY423606; AAR84086.1; -; mRNA.
DR EMBL; AY358784; AAQ89144.1; -; mRNA.
DR EMBL; CR936619; CAI56762.1; -; mRNA.
DR EMBL; CH471064; EAW68492.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68493.1; -; Genomic_DNA.
DR EMBL; BC017377; AAH17377.1; -; mRNA.
DR CCDS; CCDS7813.1; -.
DR RefSeq; NP_115604.1; NM_032228.5.
DR AlphaFoldDB; Q8WVX9; -.
DR BioGRID; 123936; 78.
DR IntAct; Q8WVX9; 53.
DR MINT; Q8WVX9; -.
DR STRING; 9606.ENSP00000346874; -.
DR SwissLipids; SLP:000000208; -.
DR iPTMnet; Q8WVX9; -.
DR PhosphoSitePlus; Q8WVX9; -.
DR SwissPalm; Q8WVX9; -.
DR BioMuta; FAR1; -.
DR DMDM; 74730902; -.
DR EPD; Q8WVX9; -.
DR jPOST; Q8WVX9; -.
DR MassIVE; Q8WVX9; -.
DR MaxQB; Q8WVX9; -.
DR PaxDb; Q8WVX9; -.
DR PeptideAtlas; Q8WVX9; -.
DR PRIDE; Q8WVX9; -.
DR ProteomicsDB; 74834; -.
DR Antibodypedia; 2735; 45 antibodies from 16 providers.
DR DNASU; 84188; -.
DR Ensembl; ENST00000354817.8; ENSP00000346874.3; ENSG00000197601.13.
DR GeneID; 84188; -.
DR KEGG; hsa:84188; -.
DR MANE-Select; ENST00000354817.8; ENSP00000346874.3; NM_032228.6; NP_115604.1.
DR UCSC; uc001mld.4; human.
DR CTD; 84188; -.
DR DisGeNET; 84188; -.
DR GeneCards; FAR1; -.
DR HGNC; HGNC:26222; FAR1.
DR HPA; ENSG00000197601; Low tissue specificity.
DR MalaCards; FAR1; -.
DR MIM; 616107; gene.
DR MIM; 616154; phenotype.
DR MIM; 619338; phenotype.
DR neXtProt; NX_Q8WVX9; -.
DR OpenTargets; ENSG00000197601; -.
DR Orphanet; 447753; Autosomal dominant spastic paraplegia type 9A.
DR Orphanet; 438178; Fatty acyl-CoA reductase 1 deficiency.
DR PharmGKB; PA162388007; -.
DR VEuPathDB; HostDB:ENSG00000197601; -.
DR eggNOG; KOG1221; Eukaryota.
DR GeneTree; ENSGT00390000006367; -.
DR HOGENOM; CLU_024661_0_0_1; -.
DR InParanoid; Q8WVX9; -.
DR OMA; QPYTFYG; -.
DR PhylomeDB; Q8WVX9; -.
DR TreeFam; TF313011; -.
DR BioCyc; MetaCyc:HS16231-MON; -.
DR BRENDA; 1.2.1.84; 2681.
DR PathwayCommons; Q8WVX9; -.
DR Reactome; R-HSA-9640463; Wax biosynthesis.
DR SignaLink; Q8WVX9; -.
DR BioGRID-ORCS; 84188; 23 hits in 1089 CRISPR screens.
DR ChiTaRS; FAR1; human.
DR GeneWiki; MLSTD2; -.
DR GenomeRNAi; 84188; -.
DR Pharos; Q8WVX9; Tbio.
DR PRO; PR:Q8WVX9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8WVX9; protein.
DR Bgee; ENSG00000197601; Expressed in corpus callosum and 186 other tissues.
DR ExpressionAtlas; Q8WVX9; baseline and differential.
DR Genevisible; Q8WVX9; HS.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; HDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0102965; F:alcohol-forming fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; TAS:Reactome.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IDA:UniProtKB.
DR GO; GO:0010025; P:wax biosynthetic process; ISS:UniProtKB.
DR CDD; cd09071; FAR_C; 1.
DR InterPro; IPR026055; FAR.
DR InterPro; IPR033640; FAR_C.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11011; PTHR11011; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF03015; Sterile; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cataract; Disease variant; Epilepsy; Intellectual disability;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Peroxisome; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..515
FT /note="Fatty acyl-CoA reductase 1"
FT /id="PRO_0000261394"
FT TOPO_DOM 1..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24108123"
FT TRANSMEM 466..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 484..515
FT /note="Peroxisomal"
FT /evidence="ECO:0000269|PubMed:24108123"
FT REGION 451..507
FT /note="Necessary and sufficient for PEX19-mediated
FT localization into peroxisome membrane"
FT /evidence="ECO:0000269|PubMed:24108123"
FT VARIANT 96
FT /note="E -> K (in dbSNP:rs12793516)"
FT /id="VAR_053800"
FT VARIANT 165..169
FT /note="EVVYP -> D (in PFCRD; results in a complete loss of
FT enzyme activity)"
FT /evidence="ECO:0000269|PubMed:25439727"
FT /id="VAR_072692"
FT VARIANT 263..515
FT /note="Missing (in PFCRD; results in a complete loss of
FT enzyme activity)"
FT /evidence="ECO:0000269|PubMed:25439727"
FT /id="VAR_085710"
FT VARIANT 365
FT /note="D -> G (in PFCRD; results in a complete loss of
FT enzyme activity; dbSNP:rs724159963)"
FT /evidence="ECO:0000269|PubMed:25439727"
FT /id="VAR_072693"
FT VARIANT 480
FT /note="R -> C (in CSPSD; increased ether lipid biosynthetic
FT process in patient cells; increased FAR1 protein levels in
FT patient cells due to impaired down-regulation by
FT plasmalogen)"
FT /evidence="ECO:0000269|PubMed:33239752"
FT /id="VAR_085711"
FT VARIANT 480
FT /note="R -> H (in CSPSD; increased ether lipid biosynthetic
FT process in patient cells; increased FAR1 protein levels in
FT patient cells due to impaired down-regulation by
FT plasmalogen; dbSNP:rs1057517926)"
FT /evidence="ECO:0000269|PubMed:33239752"
FT /id="VAR_085712"
FT VARIANT 480
FT /note="R -> L (in CSPSD; dbSNP:rs1057517926)"
FT /evidence="ECO:0000269|PubMed:33239752"
FT /id="VAR_085713"
FT CONFLICT 275..276
FT /note="LV -> PG (in Ref. 4; CAI56762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 59357 MW; EF5CF7CDD161BCD3 CRC64;
MVSIPEYYEG KNVLLTGATG FLGKVLLEKL LRSCPKVNSV YVLVRQKAGQ TPQERVEEVL
SGKLFDRLRD ENPDFREKII AINSELTQPK LALSEEDKEV IIDSTNIIFH CAATVRFNEN
LRDAVQLNVI ATRQLILLAQ QMKNLEVFMH VSTAYAYCNR KHIDEVVYPP PVDPKKLIDS
LEWMDDGLVN DITPKLIGDR PNTYIYTKAL AEYVVQQEGA KLNVAIVRPS IVGASWKEPF
PGWIDNFNGP SGLFIAAGKG ILRTIRASNN ALADLVPVDV VVNMSLAAAW YSGVNRPRNI
MVYNCTTGST NPFHWGEVEY HVISTFKRNP LEQAFRRPNV NLTSNHLLYH YWIAVSHKAP
AFLYDIYLRM TGRSPRMMKT ITRLHKAMVF LEYFTSNSWV WNTENVNMLM NQLNPEDKKT
FNIDVRQLHW AEYIENYCLG TKKYVLNEEM SGLPAARKHL NKLRNIRYGF NTILVILIWR
IFIARSQMAR NIWYFVVSLC YKFLSYFRAS STMRY
