ID   ETFD_PIG                Reviewed;         617 AA.
AC   P55931; A0A8W4FK45;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2026, sequence version 3.
DT   04-NOV-2026, entry version 136.
DE   RecName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial;
DE            Short=ETF-QO;
DE            Short=ETF-ubiquinone oxidoreductase;
DE            EC=1.5.5.1 {ECO:0000250|UniProtKB:Q16134};
DE   AltName: Full=Electron-transferring-flavoprotein dehydrogenase;
DE            Short=ETF dehydrogenase;
DE   Flags: Precursor;
GN   Name=ETFDH;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-617, AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Fetal liver;
RX   PubMed=8306995; DOI=10.1111/j.1432-1033.1994.tb19939.x;
RA   Goodman S.I., Axtell K.M., Bindoff L.A., Beard S.E., Gill R.E.,
RA   Frerman F.E.;
RT   "Molecular cloning and expression of a cDNA encoding human electron
RT   transfer flavoprotein-ubiquinone oxidoreductase.";
RL   Eur. J. Biochem. 219:277-286(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-103.
RX   PubMed=17407547; DOI=10.1186/gb-2007-8-4-r45;
RA   Gorodkin J., Cirera S., Hedegaard J., Gilchrist M.J., Panitz F.,
RA   Jorgensen C.B., Scheibye-Knudsen K., Arvin T., Lumholdt S., Sawera M.,
RA   Green T., Nielsen B.J., Havgaard J.H., Rosenkilde C., Wang J., Li H.,
RA   Li R., Liu B., Hu S., Dong W., Li W., Yu J., Wang J., Staerfeldt H.H.,
RA   Wernersson R., Madsen L.B., Thomsen B., Hornshoj H., Bujie Z., Wang X.,
RA   Wang X., Bolund L., Brunak S., Yang H., Bendixen C., Fredholm M.;
RT   "Porcine transcriptome analysis based on 97 non-normalized cDNA libraries
RT   and assembly of 1,021,891 expressed sequence tags.";
RL   Genome Biol. 8:R45.1-R45.16(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc;
RX   PubMed=32543654; DOI=10.1093/gigascience/giaa051;
RA   Warr A., Affara N., Aken B., Beiki H., Bickhart D.M., Billis K., Chow W.,
RA   Eory L., Finlayson H.A., Flicek P., Giron C.G., Griffin D.K., Hall R.,
RA   Hannum G., Hourlier T., Howe K., Hume D.A., Izuogu O., Kim K., Koren S.,
RA   Liu H., Manchanda N., Martin F.J., Nonneman D.J., O'Connor R.E.,
RA   Phillippy A.M., Rohrer G.A., Rosen B.D., Rund L.A., Sargent C.A.,
RA   Schook L.B., Schroeder S.G., Schwartz A.S., Skinner B.M., Talbot R.,
RA   Tseng E., Tuggle C.K., Watson M., Smith T.P.L., Archibald A.L.;
RT   "An improved pig reference genome sequence to enable pig genetics and
RT   genomics research.";
RL   Gigascience 9:giaa051-giaa051(2020).
RN   [4] {ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH FAD AND UBIQUINONE, SUBUNIT, AND
RP   IRON-SULFUR BINDING SITES.
RX   PubMed=17050691; DOI=10.1073/pnas.0604567103;
RA   Zhang J., Frerman F.E., Kim J.J.;
RT   "Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and
RT   electron transfer to the mitochondrial ubiquinone pool.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:16212-16217(2006).
CC   -!- FUNCTION: Links fatty acid beta-oxidation and amino acid catabolism to
CC       the respiratory chain by transferring electrons from the electron
CC       transfer flavoprotein (ETF) to ubiquinone.
CC       {ECO:0000250|UniProtKB:Q16134}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + reduced [electron-transfer flavoprotein] = a
CC         ubiquinol + oxidized [electron-transfer flavoprotein] + H(+);
CC         Xref=Rhea:RHEA:24052, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC         Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307; EC=1.5.5.1;
CC         Evidence={ECO:0000250|UniProtKB:Q16134};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24053;
CC         Evidence={ECO:0000250|UniProtKB:Q16134};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster.;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17050691}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q16134}.
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DR   EMBL; EW134518; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001431439.1; NM_001444510.1.
DR   PDB; 2GMH; X-ray; 2.50 A; A/B=34-617.
DR   PDB; 2GMJ; X-ray; 2.60 A; A/B=34-617.
DR   AlphaFoldDB; P55931; -.
DR   FunCoup; P55931; 1837.
DR   STRING; 9823.ENSSSCP00000058340; -.
DR   PaxDb; 9823-ENSSSCP00000058340; -.
DR   PeptideAtlas; P55931; -.
DR   GeneID; 100515785; -.
DR   KEGG; ssc:100515785; -.
DR   CTD; 2110; -.
DR   eggNOG; KOG2415; Eukaryota.
DR   InParanoid; P55931; -.
DR   OMA; AACHENF; -.
DR   OrthoDB; 437331at2759; -.
DR   Reactome; R-SSC-611105; Respiratory electron transport.
DR   EvolutionaryTrace; P55931; -.
DR   Proteomes; UP000008227; Chromosome 8.
DR   ExpressionAtlas; P55931; baseline and differential.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR   GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR   GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR   GO; GO:0048039; F:ubiquinone binding; IDA:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR   FunFam; 3.30.70.20:FF:000088; Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.30.9.90; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR040156; ETF-QO.
DR   InterPro; IPR049398; ETF-QO/FixC_UQ-bd.
DR   InterPro; IPR007859; ETF-QO/FixX_C.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR10617; ELECTRON TRANSFER FLAVOPROTEIN-UBIQUINONE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR10617:SF107; ELECTRON TRANSFER FLAVOPROTEIN-UBIQUINONE OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR   Pfam; PF21162; ETFQO_UQ-bd; 1.
DR   Pfam; PF05187; Fer4_ETF_QO; 1.
DR   Pfam; PF01946; Thi4; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Acetylation; Direct protein sequencing;
KW   Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur;
KW   Lipid degradation; Lipid metabolism; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Transit peptide; Transport; Ubiquinone.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..617
FT                   /note="Electron transfer flavoprotein-ubiquinone
FT                   oxidoreductase, mitochondrial"
FT                   /id="PRO_0000008663"
FT   INTRAMEM        147..164
FT                   /evidence="ECO:0000305|PubMed:17050691"
FT   INTRAMEM        460..484
FT                   /evidence="ECO:0000305|PubMed:17050691"
FT   DOMAIN          577..606
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         79
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   BINDING         104
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   BINDING         105
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   BINDING         116
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   BINDING         117
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   BINDING         118
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   BINDING         200
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   BINDING         246
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   BINDING         305
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000269|PubMed:17050691"
FT   BINDING         306
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000269|PubMed:17050691"
FT   BINDING         310
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMJ"
FT   BINDING         364
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   BINDING         387
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   BINDING         399
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH"
FT   BINDING         400
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH"
FT   BINDING         561
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   BINDING         586
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   BINDING         589
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   BINDING         592
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:17050691,
FT                   ECO:0007744|PDB:2GMH, ECO:0007744|PDB:2GMJ"
FT   MOD_RES         96
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921G7"
FT   MOD_RES         132
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921G7"
FT   MOD_RES         223
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921G7"
FT   MOD_RES         357
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921G7"
FT   MOD_RES         551
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16134"
FT   CONFLICT        37
FT                   /note="C -> S (in Ref. 2; EW134518)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="Q -> H (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        408
FT                   /note="I -> T (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           55..57
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           78..93
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          100..103
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          105..108
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   TURN            109..112
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           122..127
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           131..134
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          144..150
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          162..164
FT                   /evidence="ECO:0007829|PDB:2GMJ"
FT   HELIX           176..189
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          200..205
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          209..216
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          219..221
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          227..232
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          236..238
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          240..244
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           251..259
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   TURN            260..265
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          271..280
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           283..285
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          290..296
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          305..311
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          314..316
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          318..326
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           336..343
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   TURN            347..349
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           350..353
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          357..367
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           370..373
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          382..384
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   TURN            386..389
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   TURN            394..397
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           400..418
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          426..429
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           434..440
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           443..450
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   TURN            451..455
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           456..459
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   TURN            461..463
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           464..471
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           472..477
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   TURN            478..480
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           492..494
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           499..501
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           507..510
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          512..515
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           518..523
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   TURN            524..526
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          531..533
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          536..541
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           545..553
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           557..560
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          566..570
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          577..581
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           583..585
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   HELIX           591..595
FT                   /evidence="ECO:0007829|PDB:2GMH"
FT   STRAND          601..603
FT                   /evidence="ECO:0007829|PDB:2GMH"
SQ   SEQUENCE   617 AA;  68635 MW;  50F1744AC596A6CD CRC64;
     MMVPLAKLAS PAYQCFHALK IKKNYLPLCA TRWSSTCKVP RITTHYTIYP RDQDKRWEGV
     NMERFAEEAD VVIVGAGPAG LSAATRLKQL AAQHEKDLRV CLVEKAAQIG AHTLSGACLD
     PRAFEELFPD WKEKGAPLNT PVTEDRFGIL TEKYRIPVPI LPGLPMNNHG NYVVRLGHLV
     SWMGEQAEAL GVEVYPGYAA AEILFHEDGS VKGIATNDVG IQKDGAPKTT FERGLELHAK
     VTIFAEGCHG HLAKQLYKKF DLRANCEPQT YGIGLKELWV IDEKKWKPGR VDHTVGWPLD
     RHTYGGSFLY HLNEGEPLLA LGFVVGLDYQ NPYLSPFREF QRWKHHPSIK PTLEGGKRIA
     YGARALNEGG FQSIPKLTFP GGLLIGCSPG FMNVPKIKGT HTAMKSGILA AESIFNQLTS
     ENLQSKTIGL HVTEYEDNLK NSWVWKELYS VRNIRPSCHG ILGVYGGMIY TGIFYWIFRG
     MEPWTLKHKG SDSDQLKPAK DCTPIEYPKP DGQISFDLLS SVALSGTNHE HDQPAHLTLK
     DDSVPVNRNL SIYDGPEQRF CPAGVYEFVP LEQGDGFRLQ INAQNCVHCK TCDIKDPSQN
     INWVVPEGGG GPAYNGM
//