ACSM3_MOUSE
ID ACSM3_MOUSE Reviewed; 580 AA.
AC Q3UNX5; Q8BRY2; Q91WI1; Q9Z2F3; Q9Z2X0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Acyl-coenzyme A synthetase ACSM3, mitochondrial;
DE EC=6.2.1.2 {ECO:0000269|PubMed:11470804};
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:0000269|PubMed:11470804};
DE AltName: Full=Protein SA homolog;
DE Flags: Precursor;
GN Name=Acsm3; Synonyms=Sa, Sah;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=C57BL/6J;
RX PubMed=9449642; DOI=10.1210/endo.139.2.5763;
RA Melia M.J., Bofill N., Hubank M., Meseguer A.;
RT "Identification of androgen-regulated genes in mouse kidney by
RT representational difference analysis and random arbitrarily primed
RT polymerase chain reaction.";
RL Endocrinology 139:688-695(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=9507200; DOI=10.1046/j.1523-1755.1998.00808.x;
RA Takenaka M., Imai E., Kaneko T., Ito T., Moriyama T., Yamauchi A., Hori M.,
RA Kawamoto S., Okubo K.;
RT "Isolation of genes identified in mouse renal proximal tubule by comparing
RT different gene expression profiles.";
RL Kidney Int. 53:562-572(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INDUCTION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ; TISSUE=Kidney;
RX PubMed=15525578; DOI=10.1677/joe.1.05649;
RA Areste C., Melia M.J., Isern J., Tovar J.L., Meseguer A.;
RT "Sex steroid regulation and identification of different transcription units
RT of the SA gene in mouse kidney.";
RL J. Endocrinol. 183:101-114(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Aorta, Kidney, and Vein;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11470804; DOI=10.1074/jbc.m106651200;
RA Fujino T., Takei Y.A., Sone H., Ioka R.X., Kamataki A., Magoori K.,
RA Takahashi S., Sakai J., Yamamoto T.T.;
RT "Molecular identification and characterization of two medium-chain acyl-CoA
RT synthetases, MACS1 and the Sa gene product.";
RL J. Biol. Chem. 276:35961-35966(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-100, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-151, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an
CC acyl-CoA, the first step in fatty acid metabolism (PubMed:11470804).
CC Capable of activating medium-chain fatty acids with a preference for
CC isobutyrate among fatty acids with 2-6 carbon atoms (PubMed:11470804).
CC {ECO:0000269|PubMed:11470804}.
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:11470804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000305|PubMed:11470804};
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:0000269|PubMed:11470804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC Evidence={ECO:0000305|PubMed:11470804};
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:0000269|PubMed:11470804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC Evidence={ECO:0000305|PubMed:11470804};
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:0000269|PubMed:11470804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46177;
CC Evidence={ECO:0000305|PubMed:11470804};
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:0000269|PubMed:11470804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46181;
CC Evidence={ECO:0000305|PubMed:11470804};
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:0000250|UniProtKB:Q53FZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC Evidence={ECO:0000250|UniProtKB:Q53FZ2};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.92 mM for butyrate {ECO:0000269|PubMed:11470804};
CC KM=0.05 mM for isobutyrate {ECO:0000269|PubMed:11470804};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15525578}.
CC Mitochondrion matrix {ECO:0000269|PubMed:11470804}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UNX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UNX5-2; Sequence=VSP_028397;
CC -!- TISSUE SPECIFICITY: Detected in kidney (at protein level). Detected in
CC kidney proximal tubules and in liver. Detected at low levels in testis,
CC stomach, heart and lung. {ECO:0000269|PubMed:11470804,
CC ECO:0000269|PubMed:15525578, ECO:0000269|PubMed:9449642,
CC ECO:0000269|PubMed:9507200}.
CC -!- INDUCTION: Up-regulated in kidney by androgens. Down-regulated in
CC kidney by estrogens. Levels in kidney are very low in female C57BL/6
CC mice and in castrated male C57BL/6, 129/SvJ and BALB/c mice.
CC Constitutively expressed in liver. {ECO:0000269|PubMed:15525578,
CC ECO:0000269|PubMed:9449642}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79656.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH15248.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL40880.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA37141.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE38232.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY064696; AAL40880.1; ALT_INIT; mRNA.
DR EMBL; AB022340; BAA37141.1; ALT_FRAME; mRNA.
DR EMBL; AF068246; AAC79656.1; ALT_INIT; mRNA.
DR EMBL; AK041060; BAC30805.1; -; mRNA.
DR EMBL; AK143946; BAE25622.1; -; mRNA.
DR EMBL; AK165516; BAE38232.1; ALT_INIT; mRNA.
DR EMBL; BC015248; AAH15248.1; ALT_INIT; mRNA.
DR CCDS; CCDS21786.1; -. [Q3UNX5-1]
DR RefSeq; NP_058566.3; NM_016870.3. [Q3UNX5-1]
DR RefSeq; NP_997606.2; NM_212441.2. [Q3UNX5-1]
DR RefSeq; NP_997607.2; NM_212442.2. [Q3UNX5-1]
DR AlphaFoldDB; Q3UNX5; -.
DR SMR; Q3UNX5; -.
DR STRING; 10090.ENSMUSP00000068803; -.
DR SwissLipids; SLP:000001206; -.
DR iPTMnet; Q3UNX5; -.
DR PhosphoSitePlus; Q3UNX5; -.
DR SwissPalm; Q3UNX5; -.
DR jPOST; Q3UNX5; -.
DR MaxQB; Q3UNX5; -.
DR PaxDb; Q3UNX5; -.
DR PeptideAtlas; Q3UNX5; -.
DR PRIDE; Q3UNX5; -.
DR ProteomicsDB; 285713; -. [Q3UNX5-1]
DR ProteomicsDB; 285714; -. [Q3UNX5-2]
DR Antibodypedia; 25607; 159 antibodies from 24 providers.
DR DNASU; 20216; -.
DR Ensembl; ENSMUST00000063770; ENSMUSP00000068803; ENSMUSG00000030935. [Q3UNX5-1]
DR Ensembl; ENSMUST00000106526; ENSMUSP00000102136; ENSMUSG00000030935. [Q3UNX5-1]
DR Ensembl; ENSMUST00000106527; ENSMUSP00000102137; ENSMUSG00000030935. [Q3UNX5-1]
DR Ensembl; ENSMUST00000106528; ENSMUSP00000102138; ENSMUSG00000030935. [Q3UNX5-1]
DR Ensembl; ENSMUST00000106529; ENSMUSP00000102139; ENSMUSG00000030935. [Q3UNX5-2]
DR GeneID; 20216; -.
DR KEGG; mmu:20216; -.
DR UCSC; uc009jlq.1; mouse. [Q3UNX5-1]
DR CTD; 6296; -.
DR MGI; MGI:99538; Acsm3.
DR VEuPathDB; HostDB:ENSMUSG00000030935; -.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000157930; -.
DR HOGENOM; CLU_000022_59_10_1; -.
DR InParanoid; Q3UNX5; -.
DR OMA; HAWSNLF; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q3UNX5; -.
DR TreeFam; TF354287; -.
DR BioGRID-ORCS; 20216; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Acsm3; mouse.
DR PRO; PR:Q3UNX5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3UNX5; protein.
DR Bgee; ENSMUSG00000030935; Expressed in right kidney and 106 other tissues.
DR Genevisible; Q3UNX5; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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; IDA:MGI.
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; IDA:UniProtKB.
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:0006633; P:fatty acid biosynthetic process; IDA:MGI.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
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..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..580
FT /note="Acyl-coenzyme A synthetase ACSM3, mitochondrial"
FT /id="PRO_0000306098"
FT BINDING 229..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 368..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 67
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 100
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 151
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 578..580
FT /note="VTT -> EQGLLHEQMTVDRLLGKSARHERHVPSVCMNCSGVAAVLRYAEAA
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028397"
FT CONFLICT 137
FT /note="T -> P (in Ref. 3; AAC79656)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 65623 MW; CAF3D06A0B4A2778 CRC64;
MVMLLRARCF QRLAIPDPMR VLYKDYRTAT PQNFSNYESM KQDFKIEIPE YFNFAKDVLD
QWTNMEKAGK RLSNPAFWWI DGNGEELRWS FEELGLLSRK FANILTEACS LQRGDRVMVI
LPKIPEWWLA NVACLRTGTV LIPGTTQLTQ KDILYRLQSS KAKCIITDDT LAPAVDAVAA
KCENLHSKLI VSQHSREGWG NLKEMMKYAS DSHTCVDTKH DEMMAIYFTS GTTGPPKMIG
HTHSSFGLGL SVNGRFWLDL IASDVMWNTS DTGWAKSAWS SVFSPWTQGA CVFAHYLPRF
ESTSILQTLS KFPITVFCSA PTAYRMLVQN DMSSYKFNSL KHCVSAGEPI NPEVMEQWRK
KTGLDIYEGY GQTETVLICG NFKGMKIKPG SMGKPSPAFD VKILDENGAT LPPGQEGDIA
LQVLPERPFG LFTHYVDNPS KTASTLRGSF YITGDRGYMD EDGYFWFVAR SDDIILSSGY
RIGPFEVESA LIEHPSIAES AVVSSPDPIR GEVVKAFIVL NPDYKSHDQE QLKKEIQEHV
KKTTAPYKYP RKVEFIEELP KTVSGKVKRN ELRKKEWVTT
