ID   FADS3_HUMAN             Reviewed;         445 AA.
AC   Q9Y5Q0; O60426;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=Fatty acid desaturase 3 {ECO:0000250|UniProtKB:Q8K1P9};
DE            Short=FADS3 {ECO:0000303|PubMed:31862735, ECO:0000303|PubMed:31916624, ECO:0000303|PubMed:37209771};
DE            EC=1.14.19.- {ECO:0000269|PubMed:31862735, ECO:0000269|PubMed:31916624, ECO:0000269|PubMed:37209771};
DE   AltName: Full=Delta(13) fatty acid desaturase {ECO:0000250|UniProtKB:Q8K1P9};
DE            Short=Delta(13) desaturase {ECO:0000250|UniProtKB:Q8K1P9};
GN   Name=FADS3 {ECO:0000303|PubMed:19752397, ECO:0000312|HGNC:HGNC:3576};
GN   Synonyms=CYB5RP;
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].
RX   PubMed=10860662; DOI=10.1006/geno.2000.6196;
RA   Marquardt A., Stoehr H., White K., Weber B.H.;
RT   "cDNA cloning, genomic structure, and chromosomal localization of three
RT   members of the human fatty acid desaturase family.";
RL   Genomics 66:175-183(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li W., Metzker M.L., Caskey C.T., Petrukhin K.;
RT   "Human retina-specific delta 6 fatty acid desaturase.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Muscle;
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=19752397; DOI=10.1194/jlr.m000588;
RA   Pedrono F., Blanchard H., Kloareg M., D'andrea S., Daval S., Rioux V.,
RA   Legrand P.;
RT   "The fatty acid desaturase 3 gene encodes for different FADS3 protein
RT   isoforms in mammalian tissues.";
RL   J. Lipid Res. 51:472-479(2010).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=31916624; DOI=10.1096/fj.201902645r;
RA   Jojima K., Edagawa M., Sawai M., Ohno Y., Kihara A.;
RT   "Biosynthesis of the anti-lipid-microdomain sphingoid base 4,14-
RT   sphingadiene by the ceramide desaturase FADS3.";
RL   FASEB J. 34:3318-3335(2020).
RN   [7]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=31862735; DOI=10.1074/jbc.ac119.011883;
RA   Karsai G., Lone M., Kutalik Z., Brenna J.T., Li H., Pan D.,
RA   von Eckardstein A., Hornemann T.;
RT   "FADS3 is a Delta14Z sphingoid base desaturase that contributes to gender
RT   differences in the human plasma sphingolipidome.";
RL   J. Biol. Chem. 295:1889-1897(2020).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=37209771; DOI=10.1016/j.bbalip.2023.159335;
RA   Jojima K., Kihara A.;
RT   "Metabolism of sphingadiene and characterization of the sphingadiene-
RT   producing enzyme FADS3.";
RL   Biochim. Biophys. Acta 1868:159335-159335(2023).
CC   -!- FUNCTION: Mammals have different sphingoid bases that differ in their
CC       length and/or pattern of desaturation and hydroxyl groups. The
CC       predominant sphingoid base that comprises mammalian ceramides is
CC       sphing-4-enine (sphingosine or SPH) which has a trans (E) desaturation
CC       at carbon 4 (PubMed:31916624, PubMed:31862735). FADS3 is a desaturase
CC       that introduces a cis (Z) double bond between carbon 14 and carbon 15
CC       of the sphingoid base (also known as long chain base, LCB), producing
CC       LCBs such as sphinga-4,14-dienine (SPD, d18:2(4E,14Z)) from SPH
CC       (PubMed:31916624, PubMed:31862735, PubMed:37209771). Prefers SPH-
CC       containing ceramides (N-acylsphing-4-enines) as substrates
CC       (PubMed:31916624, PubMed:31862735, PubMed:37209771). Capable of
CC       metabolizing also the SPH in its free form (PubMed:31862735). SPD
CC       ceramides occur widely in mammalian tissues and cells
CC       (PubMed:31916624). Due to their unusual structure containing a cis
CC       double bond, SPD ceramides may have an opposite, negative role in lipid
CC       microdomain formation relative to conventional ceramides
CC       (PubMed:31916624). Could be involved in the detoxification of 1-deoxy
CC       sphingolipids, by desaturating the cytotoxic 1-deoxysphinganine (1-
CC       deoxySA, m18:0), produced under pathological conditions, to 1-
CC       deoxysphingenine (1-deoxysphingosine, 1-deoxySO, m18:1) (Probable).
CC       Although prefers SPH-containing ceramides (N-acylsphing-4-enines) as
CC       substrates, it also exhibits activity toward dihydrosphingosine-
CC       containing CERs (N-acylsphinganines) and produces 14Z-SPH-containing
CC       sphingolipids,which can be found in patients with DEGS1 mutations
CC       (PubMed:37209771). Its desaturase mechanism involves an electron
CC       transfer facilitated by cytochrome b5 (PubMed:37209771). FADS3 also
CC       acts as a methyl-end fatty acyl coenzyme A (CoA) desaturase that
CC       introduces a cis double bond between the preexisting double bond and
CC       the terminal methyl group of the fatty acyl chain (By similarity).
CC       Desaturates (11E)-octadecenoate (trans-vaccenoate, the predominant
CC       trans fatty acid in human milk) at carbon 13 to generate (11E,13Z)-
CC       octadecadienoate (also known as conjugated linoleic acid 11E,13Z-CLA)
CC       (By similarity). {ECO:0000250|UniProtKB:Q8K1P9,
CC       ECO:0000269|PubMed:31862735, ECO:0000269|PubMed:31916624,
CC       ECO:0000269|PubMed:37209771, ECO:0000305|PubMed:31862735}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC         O2 = an N-acyl-sphinga-4E,14Z-dienine + 2 Fe(III)-[cytochrome b5] + 2
CC         H2O; Xref=Rhea:RHEA:63928, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC         COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:52639,
CC         ChEBI:CHEBI:139573; Evidence={ECO:0000269|PubMed:31862735,
CC         ECO:0000269|PubMed:31916624, ECO:0000269|PubMed:37209771};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63929;
CC         Evidence={ECO:0000269|PubMed:31862735, ECO:0000269|PubMed:31916624,
CC         ECO:0000269|PubMed:37209771};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + N-(hexanoyl)sphing-4-enine
CC         + O2 = 2 Fe(III)-[cytochrome b5] + 2 H2O + N-hexanoyl-sphinga-4E,14Z-
CC         dienine; Xref=Rhea:RHEA:63940, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC         COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:63867,
CC         ChEBI:CHEBI:149631; Evidence={ECO:0000269|PubMed:31916624,
CC         ECO:0000269|PubMed:37209771};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63941;
CC         Evidence={ECO:0000269|PubMed:31916624, ECO:0000269|PubMed:37209771};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + sphing-4-enine = 2
CC         Fe(III)-[cytochrome b5] + 2 H2O + sphinga-4E,14Z-dienine;
CC         Xref=Rhea:RHEA:76483, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57756,
CC         ChEBI:CHEBI:83568; Evidence={ECO:0000269|PubMed:31862735};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76484;
CC         Evidence={ECO:0000305|PubMed:31862735};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(11E)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC         O2 = (11E,13Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC         H2O; Xref=Rhea:RHEA:46056, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC         COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74296,
CC         ChEBI:CHEBI:85650; Evidence={ECO:0000250|UniProtKB:Q8K1P9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46057;
CC         Evidence={ECO:0000250|UniProtKB:Q8K1P9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + N-acyl-1-deoxysphinganine
CC         + O2 = 2 Fe(III)-[cytochrome b5] + 2 H2O + N-acyl-1-deoxysphing-14Z-
CC         enine; Xref=Rhea:RHEA:76487, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC         COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:67111,
CC         ChEBI:CHEBI:195246; Evidence={ECO:0000269|PubMed:31862735};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76488;
CC         Evidence={ECO:0000305|PubMed:31862735};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC         = an N-acylsphing-14Z-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC         Xref=Rhea:RHEA:76563, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31488,
CC         ChEBI:CHEBI:195278; Evidence={ECO:0000269|PubMed:37209771};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76564;
CC         Evidence={ECO:0000305|PubMed:37209771};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000305|PubMed:31862735, ECO:0000305|PubMed:31916624,
CC       ECO:0000305|PubMed:37209771}.
CC   -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC       {ECO:0000250|UniProtKB:Q8K1P9}.
CC   -!- INTERACTION:
CC       Q9Y5Q0; Q8N5I4: DHRSX; NbExp=3; IntAct=EBI-17548630, EBI-3923585;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:31916624}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in various organs and tissues
CC       including liver, kidney, brain, lung, pancreas, testis, ovary and
CC       skeletal muscle (at protein level). {ECO:0000269|PubMed:19752397}.
CC   -!- DOMAIN: The protein sequence includes a number of characteristic
CC       features of microsomal fatty acid desaturases including the three
CC       histidine boxes (these domains may contain the active site and/or be
CC       involved in metal ion binding), and the N-terminal cytochrome b5 domain
CC       containing the heme-binding motif, HPGG, similar to that of other fatty
CC       acid desaturases. {ECO:0000303|PubMed:10860662}.
CC   -!- MISCELLANEOUS: A 28 kDa isoform is expressed in lung, kidney, pancreas
CC       and ovary (at protein level). {ECO:0000269|PubMed:19752397}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000305|PubMed:37209771}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC23396.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF084560; AAG23122.1; -; mRNA.
DR   EMBL; AF134404; AAD31282.1; -; mRNA.
DR   EMBL; AC004770; AAC23396.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP006260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004901; AAH04901.1; -; mRNA.
DR   CCDS; CCDS8013.1; -.
DR   RefSeq; NP_068373.1; NM_021727.4.
DR   AlphaFoldDB; Q9Y5Q0; -.
DR   SMR; Q9Y5Q0; -.
DR   BioGRID; 110182; 48.
DR   IntAct; Q9Y5Q0; 19.
DR   STRING; 9606.ENSP00000278829; -.
DR   SwissLipids; SLP:000000278; -.
DR   iPTMnet; Q9Y5Q0; -.
DR   PhosphoSitePlus; Q9Y5Q0; -.
DR   BioMuta; FADS3; -.
DR   DMDM; 74762790; -.
DR   EPD; Q9Y5Q0; -.
DR   jPOST; Q9Y5Q0; -.
DR   MassIVE; Q9Y5Q0; -.
DR   MaxQB; Q9Y5Q0; -.
DR   PaxDb; 9606-ENSP00000278829; -.
DR   PeptideAtlas; Q9Y5Q0; -.
DR   ProteomicsDB; 86470; -.
DR   Pumba; Q9Y5Q0; -.
DR   Antibodypedia; 28347; 172 antibodies from 22 providers.
DR   DNASU; 3995; -.
DR   Ensembl; ENST00000278829.7; ENSP00000278829.2; ENSG00000221968.9.
DR   GeneID; 3995; -.
DR   KEGG; hsa:3995; -.
DR   MANE-Select; ENST00000278829.7; ENSP00000278829.2; NM_021727.5; NP_068373.1.
DR   UCSC; uc001nsm.5; human.
DR   AGR; HGNC:3576; -.
DR   CTD; 3995; -.
DR   DisGeNET; 3995; -.
DR   GeneCards; FADS3; -.
DR   HGNC; HGNC:3576; FADS3.
DR   HPA; ENSG00000221968; Low tissue specificity.
DR   MIM; 606150; gene.
DR   neXtProt; NX_Q9Y5Q0; -.
DR   OpenTargets; ENSG00000221968; -.
DR   PharmGKB; PA27975; -.
DR   VEuPathDB; HostDB:ENSG00000221968; -.
DR   eggNOG; KOG4232; Eukaryota.
DR   GeneTree; ENSGT00950000182990; -.
DR   InParanoid; Q9Y5Q0; -.
DR   OMA; WMHEAGH; -.
DR   OrthoDB; 294339at2759; -.
DR   PhylomeDB; Q9Y5Q0; -.
DR   TreeFam; TF313604; -.
DR   BRENDA; 1.14.19.30; 2681.
DR   PathwayCommons; Q9Y5Q0; -.
DR   SignaLink; Q9Y5Q0; -.
DR   SIGNOR; Q9Y5Q0; -.
DR   UniPathway; UPA00222; -.
DR   UniPathway; UPA00658; -.
DR   BioGRID-ORCS; 3995; 11 hits in 1156 CRISPR screens.
DR   ChiTaRS; FADS3; human.
DR   GenomeRNAi; 3995; -.
DR   Pharos; Q9Y5Q0; Tbio.
DR   PRO; PR:Q9Y5Q0; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9Y5Q0; Protein.
DR   Bgee; ENSG00000221968; Expressed in tibial nerve and 215 other cell types or tissues.
DR   ExpressionAtlas; Q9Y5Q0; baseline and differential.
DR   Genevisible; Q9Y5Q0; HS.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; NAS:UniProtKB.
DR   CDD; cd03506; Delta6-FADS-like; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR012171; Fatty_acid_desaturase.
DR   PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 1.
DR   PANTHER; PTHR19353:SF11; FATTY ACID DESATURASE 3; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   1: Evidence at protein level;
KW   Electron transport; Endoplasmic reticulum; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..445
FT                   /note="Fatty acid desaturase 3"
FT                   /id="PRO_0000307108"
FT   TOPO_DOM        1..133
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        155..159
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..263
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        285..306
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        328..445
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          20..97
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           182..186
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000303|PubMed:10860662"
FT   MOTIF           219..223
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000303|PubMed:10860662"
FT   MOTIF           383..387
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000303|PubMed:10860662"
FT   VARIANT         192
FT                   /note="K -> N (in dbSNP:rs35479241)"
FT                   /id="VAR_035341"
FT   VARIANT         216
FT                   /note="N -> K (in dbSNP:rs34511441)"
FT                   /id="VAR_035342"
SQ   SEQUENCE   445 AA;  51145 MW;  7840EF6BE055111D CRC64;
     MGGVGEPGPR EGPAQPGAPL PTFCWEQIRA HDQPGDKWLV IERRVYDISR WAQRHPGGSR
     LIGHHGAEDA TDAFRAFHQD LNFVRKFLQP LLIGELAPEE PSQDGPLNAQ LVEDFRALHQ
     AAEDMKLFDA SPTFFAFLLG HILAMEVLAW LLIYLLGPGW VPSALAAFIL AISQAQSWCL
     QHDLGHASIF KKSWWNHVAQ KFVMGQLKGF SAHWWNFRHF QHHAKPNIFH KDPDVTVAPV
     FLLGESSVEY GKKKRRYLPY NQQHLYFFLI GPPLLTLVNF EVENLAYMLV CMQWADLLWA
     ASFYARFFLS YLPFYGVPGV LLFFVAVRVL ESHWFVWITQ MNHIPKEIGH EKHRDWVSSQ
     LAATCNVEPS LFTNWFSGHL NFQIEHHLFP RMPRHNYSRV APLVKSLCAK HGLSYEVKPF
     LTALVDIVRS LKKSGDIWLD AYLHQ
//