ID   ACSM3_HUMAN             Reviewed;         586 AA.
AC   Q53FZ2; O60363; Q13732; Q15425; Q7KYM6; Q9BUA2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Acyl-coenzyme A synthetase ACSM3, mitochondrial;
DE            EC=6.2.1.2 {ECO:0000269|PubMed:11772874};
DE   AltName: Full=Acyl-CoA synthetase medium-chain family member 3;
DE   AltName: Full=Butyrate--CoA ligase 3;
DE   AltName: Full=Butyryl-coenzyme A synthetase 3;
DE   AltName: Full=Middle-chain acyl-CoA synthetase 3;
DE   AltName: Full=Propionate--CoA ligase;
DE            EC=6.2.1.17 {ECO:0000250|UniProtKB:Q3UNX5};
DE   AltName: Full=Protein SA homolog;
DE   Flags: Precursor;
GN   Name=ACSM3; Synonyms=SAH;
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] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=7907320; DOI=10.1161/01.hyp.23.3.375;
RA   Iwai N., Ohmichi N., Hanai K., Nakamura Y., Kinoshita M.;
RT   "Human SA gene locus as a candidate locus for essential hypertension.";
RL   Hypertension 23:375-380(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND LACK OF INVOLVEMENT IN
RP   HEREDITARY HYPERTENSION.
RX   PubMed=7843754; DOI=10.1161/01.hyp.25.1.6;
RA   Nabika T., Bonnardeaux A., James M., Julier C., Jeunemaitre X., Corvol P.,
RA   Lathrop M., Soubrier F.;
RT   "Evaluation of the SA locus in human hypertension.";
RL   Hypertension 25:6-13(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA   Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA   Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA   Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA   Adams M.D.;
RT   "Genome duplications and other features in 12 Mb of DNA sequence from human
RT   chromosome 16p and 16q.";
RL   Genomics 60:295-308(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-367.
RC   TISSUE=Kidney;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Skin;
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   [6]
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   REVIEW.
RX   PubMed=27351777; DOI=10.1080/17425255.2016.1206888;
RA   van der Sluis R., Erasmus E.;
RT   "Xenobiotic/medium chain fatty acid: CoA ligase - a critical review on its
RT   role in fatty acid metabolism and the detoxification of benzoic acid and
RT   aspirin.";
RL   Expert Opin. Drug Metab. Toxicol. 12:1169-1179(2016).
RN   [9]
RP   VARIANT ASN-367, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11772874; DOI=10.1161/hc0102.101780;
RA   Iwai N., Katsuya T., Mannami T., Higaki J., Ogihara T., Kokame K.,
RA   Ogata J., Baba S.;
RT   "Association between SAH, an acyl-CoA synthetase gene, and
RT   hypertriglyceridemia, obesity, and hypertension.";
RL   Circulation 105:41-47(2002).
RN   [10]
RP   VARIANT ASN-367.
RX   PubMed=17278971; DOI=10.1097/hjh.0b013e3280144779;
RA   Telgmann R., Brand E., Nicaud V., Hagedorn C., Beining K., Schoenfelder J.,
RA   Brink-Spalink V., Schmidt-Petersen K., Matanis T., Vischer P., Nofer J.-R.,
RA   Hasenkamp S., Plouin P.-F., Drouet L., Cambien F., Paul M., Tiret L.,
RA   Brand-Herrmann S.-M.;
RT   "SAH gene variants are associated with obesity-related hypertension in
RT   Caucasians: the PEGASE Study.";
RL   J. Hypertens. 25:557-564(2007).
CC   -!- FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an
CC       acyl-CoA, the first step in fatty acid metabolism (PubMed:11772874).
CC       Capable of activating medium-chain fatty acids with a preference for
CC       isobutyrate among fatty acids with 2-6 carbon atoms (By similarity).
CC       {ECO:0000250|UniProtKB:Q3UNX5, ECO:0000269|PubMed:11772874}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC         acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC         Evidence={ECO:0000269|PubMed:11772874};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC         Evidence={ECO:0000305|PubMed:11772874};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA;
CC         Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC         ChEBI:CHEBI:456215; EC=6.2.1.17;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate;
CC         Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methylpropanoate + ATP + CoA = 2-methylpropanoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:46176, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:48944, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57338, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46177;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methylbutanoate + ATP + CoA = 2-methylbutanoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:46180, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:48946, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57336, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46181;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC         Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11772874};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC         Evidence={ECO:0000305|PubMed:11772874};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC   -!- INTERACTION:
CC       Q53FZ2-2; Q92876: KLK6; NbExp=3; IntAct=EBI-25887341, EBI-2432309;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11772874}.
CC       Mitochondrion matrix {ECO:0000250|UniProtKB:Q3UNX5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q53FZ2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q53FZ2-2; Sequence=VSP_028395, VSP_028396;
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC31667.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA03853.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA56369.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D16350; BAA03853.1; ALT_INIT; mRNA.
DR   EMBL; X80062; CAA56369.1; ALT_INIT; mRNA.
DR   EMBL; AC004381; AAC31667.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK223139; BAD96859.1; -; mRNA.
DR   EMBL; BC002790; AAH02790.3; -; mRNA.
DR   CCDS; CCDS10589.1; -. [Q53FZ2-1]
DR   CCDS; CCDS45435.1; -. [Q53FZ2-2]
DR   PIR; I54401; I54401.
DR   PIR; S69913; S69913.
DR   RefSeq; NP_005613.2; NM_005622.3. [Q53FZ2-1]
DR   RefSeq; NP_973729.1; NM_202000.2. [Q53FZ2-2]
DR   AlphaFoldDB; Q53FZ2; -.
DR   SMR; Q53FZ2; -.
DR   BioGRID; 112203; 20.
DR   IntAct; Q53FZ2; 2.
DR   STRING; 9606.ENSP00000289416; -.
DR   SwissLipids; SLP:000001189; -.
DR   iPTMnet; Q53FZ2; -.
DR   PhosphoSitePlus; Q53FZ2; -.
DR   SwissPalm; Q53FZ2; -.
DR   BioMuta; ACSM3; -.
DR   DMDM; 158706483; -.
DR   EPD; Q53FZ2; -.
DR   jPOST; Q53FZ2; -.
DR   MassIVE; Q53FZ2; -.
DR   MaxQB; Q53FZ2; -.
DR   PaxDb; 9606-ENSP00000289416; -.
DR   PeptideAtlas; Q53FZ2; -.
DR   ProteomicsDB; 62470; -. [Q53FZ2-1]
DR   ProteomicsDB; 62471; -. [Q53FZ2-2]
DR   Pumba; Q53FZ2; -.
DR   Antibodypedia; 25607; 180 antibodies from 25 providers.
DR   DNASU; 6296; -.
DR   Ensembl; ENST00000289416.10; ENSP00000289416.5; ENSG00000005187.12. [Q53FZ2-1]
DR   Ensembl; ENST00000440284.6; ENSP00000394565.2; ENSG00000005187.12. [Q53FZ2-2]
DR   GeneID; 6296; -.
DR   KEGG; hsa:6296; -.
DR   MANE-Select; ENST00000289416.10; ENSP00000289416.5; NM_005622.4; NP_005613.2.
DR   UCSC; uc002dhq.4; human. [Q53FZ2-1]
DR   AGR; HGNC:10522; -.
DR   CTD; 6296; -.
DR   DisGeNET; 6296; -.
DR   GeneCards; ACSM3; -.
DR   HGNC; HGNC:10522; ACSM3.
DR   HPA; ENSG00000005187; Tissue enhanced (kidney, liver).
DR   MalaCards; ACSM3; -.
DR   MIM; 145505; gene.
DR   neXtProt; NX_Q53FZ2; -.
DR   OpenTargets; ENSG00000005187; -.
DR   PharmGKB; PA34930; -.
DR   VEuPathDB; HostDB:ENSG00000005187; -.
DR   eggNOG; KOG1175; Eukaryota.
DR   GeneTree; ENSGT00940000157930; -.
DR   InParanoid; Q53FZ2; -.
DR   OMA; HAWSNLF; -.
DR   OrthoDB; 5474118at2759; -.
DR   PhylomeDB; Q53FZ2; -.
DR   TreeFam; TF354287; -.
DR   PathwayCommons; Q53FZ2; -.
DR   Reactome; R-HSA-77352; Beta oxidation of butanoyl-CoA to acetyl-CoA.
DR   SignaLink; Q53FZ2; -.
DR   BioGRID-ORCS; 6296; 7 hits in 1153 CRISPR screens.
DR   ChiTaRS; ACSM3; human.
DR   GeneWiki; ACSM3; -.
DR   GenomeRNAi; 6296; -.
DR   Pharos; Q53FZ2; Tbio.
DR   PRO; PR:Q53FZ2; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q53FZ2; Protein.
DR   Bgee; ENSG00000005187; Expressed in left ovary and 122 other cell types or tissues.
DR   ExpressionAtlas; Q53FZ2; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047760; F:butyrate-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0015645; F:fatty acid ligase activity; IBA:GO_Central.
DR   GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043759; F:methylbutanoate-CoA ligase activity; IEA:RHEA.
DR   GO; GO:0018729; F:propionate CoA-transferase activity; IEA:Ensembl.
DR   GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR   GO; GO:0042632; P:cholesterol homeostasis; NAS:BHF-UCL.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008217; P:regulation of blood pressure; TAS:ProtInc.
DR   CDD; cd05928; MACS_euk; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR   PANTHER; PTHR43605:SF7; ACYL-COENZYME A SYNTHETASE ACSM3, MITOCHONDRIAL; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   Genevisible; Q53FZ2; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Fatty acid metabolism;
KW   Ligase; Lipid metabolism; Magnesium; Metal-binding; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Transit peptide.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..586
FT                   /note="Acyl-coenzyme A synthetase ACSM3, mitochondrial"
FT                   /id="PRO_0000306097"
FT   BINDING         235..243
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         374..379
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         461
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         476
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         572
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UNX5"
FT   MOD_RES         106
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UNX5"
FT   MOD_RES         157
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UNX5"
FT   VAR_SEQ         409..438
FT                   /note="IVDVNGNVLPPGQEGDIGIQVLPNRPFGLF -> VCTSPSRRMFNNPICTLP
FT                   TYRLPPYKLSLL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:7843754"
FT                   /id="VSP_028395"
FT   VAR_SEQ         439..586
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:7843754"
FT                   /id="VSP_028396"
FT   VARIANT         100
FT                   /note="L -> P (in dbSNP:rs5713)"
FT                   /id="VAR_035249"
FT   VARIANT         270
FT                   /note="D -> H (in dbSNP:rs13306603)"
FT                   /id="VAR_048239"
FT   VARIANT         308
FT                   /note="P -> T (in dbSNP:rs7196188)"
FT                   /id="VAR_035250"
FT   VARIANT         367
FT                   /note="K -> N (in dbSNP:rs5716)"
FT                   /evidence="ECO:0000269|PubMed:11772874,
FT                   ECO:0000269|PubMed:17278971, ECO:0000269|Ref.4"
FT                   /id="VAR_035251"
FT   CONFLICT        132
FT                   /note="E -> R (in Ref. 1; BAA03853)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237
FT                   /note="G -> A (in Ref. 1; BAA03853)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="T -> S (in Ref. 1; BAA03853)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        407
FT                   /note="V -> D (in Ref. 4; BAD96859)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        463
FT                   /note="G -> A (in Ref. 1; BAA03853)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        569
FT                   /note="I -> V (in Ref. 1; BAA03853)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   586 AA;  66153 MW;  329967C751F11F1D CRC64;
     MLARVTRKML RHAKCFQRLA IFGSVRALHK DNRTATPQNF SNYESMKQDF KLGIPEYFNF
     AKDVLDQWTD KEKAGKKPSN PAFWWINRNG EEMRWSFEEL GSLSRKFANI LSEACSLQRG
     DRVILILPRV PEWWLANVAC LRTGTVLIPG TTQLTQKDIL YRLQSSKANC IITNDVLAPA
     VDAVASKCEN LHSKLIVSEN SREGWGNLKE LMKHASDSHT CVKTKHNEIM AIFFTSGTSG
     YPKMTAHTHS SFGLGLSVNG RFWLDLTPSD VMWNTSDTGW AKSAWSSVFS PWIQGACVFT
     HHLPRFEPTS ILQTLSKYPI TVFCSAPTVY RMLVQNDITS YKFKSLKHCV SAGEPITPDV
     TEKWRNKTGL DIYEGYGQTE TVLICGNFKG MKIKPGSMGK PSPAFDVKIV DVNGNVLPPG
     QEGDIGIQVL PNRPFGLFTH YVDNPSKTAS TLRGNFYITG DRGYMDKDGY FWFVARADDV
     ILSSGYRIGP FEVENALNEH PSVAESAVVS SPDPIRGEVV KAFVVLNPDY KSHDQEQLIK
     EIQEHVKKTT APYKYPRKVE FIQELPKTIS GKTKRNELRK KEWKTI
//