ECHB_MOUSE
ID ECHB_MOUSE Reviewed; 475 AA.
AC Q99JY0; Q3TEH9; Q8BJI5; Q8BJM0; Q8BK52;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Trifunctional enzyme subunit beta, mitochondrial;
DE AltName: Full=TP-beta;
DE Includes:
DE RecName: Full=3-ketoacyl-CoA thiolase;
DE EC=2.3.1.155 {ECO:0000250|UniProtKB:P55084};
DE EC=2.3.1.16 {ECO:0000250|UniProtKB:P55084};
DE AltName: Full=Acetyl-CoA acyltransferase;
DE AltName: Full=Beta-ketothiolase;
DE Flags: Precursor;
GN Name=Hadhb;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Colon, Hippocampus, Spinal ganglion, Testis, and
RC Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-53; LYS-73; LYS-189; LYS-191;
RP LYS-273; LYS-292; LYS-294 AND LYS-333, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-189; LYS-294; LYS-299;
RP LYS-333; LYS-349 AND LYS-362, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [6]
RP INTERACTION WITH MTLN.
RX PubMed=29949755; DOI=10.1016/j.celrep.2018.05.058;
RA Makarewich C.A., Baskin K.K., Munir A.Z., Bezprozvannaya S., Sharma G.,
RA Khemtong C., Shah A.M., McAnally J.R., Malloy C.R., Szweda L.I.,
RA Bassel-Duby R., Olson E.N.;
RT "MOXI Is a Mitochondrial Micropeptide That Enhances Fatty Acid beta-
RT Oxidation.";
RL Cell Rep. 23:3701-3709(2018).
CC -!- FUNCTION: Mitochondrial trifunctional enzyme catalyzes the last three
CC of the four reactions of the mitochondrial beta-oxidation pathway. The
CC mitochondrial beta-oxidation pathway is the major energy-producing
CC process in tissues and is performed through four consecutive reactions
CC breaking down fatty acids into acetyl-CoA. Among the enzymes involved
CC in this pathway, the trifunctional enzyme exhibits specificity for
CC long-chain fatty acids. Mitochondrial trifunctional enzyme is a
CC heterotetrameric complex composed of two proteins, the trifunctional
CC enzyme subunit alpha/HADHA carries the 2,3-enoyl-CoA hydratase and the
CC 3-hydroxyacyl-CoA dehydrogenase activities, while the trifunctional
CC enzyme subunit beta/HADHB described here bears the 3-ketoacyl-CoA
CC thiolase activity. {ECO:0000250|UniProtKB:P55084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + butanoyl-CoA = 3-oxohexanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:31111, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:62418;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + hexanoyl-CoA = 3-oxooctanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:31203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:62619, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + octanoyl-CoA = 3-oxodecanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:31087, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57386, ChEBI:CHEBI:62548;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + decanoyl-CoA = 3-oxododecanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:31183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:61430, ChEBI:CHEBI:62615;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + dodecanoyl-CoA = 3-oxotetradecanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:31091, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:62543;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:18161, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57385; EC=2.3.1.155;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163;
CC Evidence={ECO:0000250|UniProtKB:P55084};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P55084}.
CC -!- SUBUNIT: Heterotetramer of 2 alpha/HADHA and 2 beta/HADHB subunits;
CC forms the mitochondrial trifunctional enzyme (By similarity). Also
CC purified as higher order heterooligomers including a 4 alpha/HADHA and
CC 4 beta/HADHB heterooligomer which physiological significance remains
CC unclear (By similarity). The mitochondrial trifunctional enzyme
CC interacts with MTLN (PubMed:29949755). Interacts with RSAD2/viperin (By
CC similarity). {ECO:0000250|UniProtKB:P55084,
CC ECO:0000269|PubMed:29949755}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P55084}.
CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:P55084}.
CC Mitochondrion outer membrane {ECO:0000250|UniProtKB:P55084}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P55084}. Note=Protein
CC stability and association with membranes require HADHA.
CC {ECO:0000250|UniProtKB:P55084}.
CC -!- PTM: Acetylation of Lys-202 is observed in liver mitochondria from
CC fasted mice but not from fed mice.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; AK033462; BAC28300.1; -; mRNA.
DR EMBL; AK076814; BAC36493.1; -; mRNA.
DR EMBL; AK083164; BAC38790.1; -; mRNA.
DR EMBL; AK083767; BAC39015.1; -; mRNA.
DR EMBL; AK150889; BAE29936.1; -; mRNA.
DR EMBL; AK169637; BAE41269.1; -; mRNA.
DR EMBL; BC005585; AAH05585.1; -; mRNA.
DR CCDS; CCDS39045.1; -.
DR RefSeq; NP_001276727.1; NM_001289798.1.
DR RefSeq; NP_001276728.1; NM_001289799.1.
DR RefSeq; NP_663533.1; NM_145558.2.
DR RefSeq; XP_017176317.1; XM_017320828.1.
DR RefSeq; XP_017176318.1; XM_017320829.1.
DR AlphaFoldDB; Q99JY0; -.
DR SMR; Q99JY0; -.
DR BioGRID; 231080; 30.
DR IntAct; Q99JY0; 7.
DR MINT; Q99JY0; -.
DR STRING; 10090.ENSMUSP00000110434; -.
DR iPTMnet; Q99JY0; -.
DR PhosphoSitePlus; Q99JY0; -.
DR SwissPalm; Q99JY0; -.
DR EPD; Q99JY0; -.
DR jPOST; Q99JY0; -.
DR MaxQB; Q99JY0; -.
DR PaxDb; Q99JY0; -.
DR PeptideAtlas; Q99JY0; -.
DR PRIDE; Q99JY0; -.
DR ProteomicsDB; 277669; -.
DR Antibodypedia; 27848; 249 antibodies from 30 providers.
DR DNASU; 231086; -.
DR Ensembl; ENSMUST00000026841; ENSMUSP00000026841; ENSMUSG00000059447.
DR Ensembl; ENSMUST00000114783; ENSMUSP00000110431; ENSMUSG00000059447.
DR Ensembl; ENSMUST00000114786; ENSMUSP00000110434; ENSMUSG00000059447.
DR GeneID; 231086; -.
DR KEGG; mmu:231086; -.
DR UCSC; uc008wve.2; mouse.
DR CTD; 3032; -.
DR MGI; MGI:2136381; Hadhb.
DR VEuPathDB; HostDB:ENSMUSG00000059447; -.
DR eggNOG; KOG1392; Eukaryota.
DR GeneTree; ENSGT01030000234626; -.
DR HOGENOM; CLU_031026_2_0_1; -.
DR InParanoid; Q99JY0; -.
DR OMA; MTAFPEP; -.
DR OrthoDB; 1129049at2759; -.
DR PhylomeDB; Q99JY0; -.
DR TreeFam; TF315243; -.
DR Reactome; R-MMU-1482798; Acyl chain remodeling of CL.
DR Reactome; R-MMU-77285; Beta oxidation of myristoyl-CoA to lauroyl-CoA.
DR Reactome; R-MMU-77305; Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
DR Reactome; R-MMU-77310; Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
DR Reactome; R-MMU-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR Reactome; R-MMU-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
DR Reactome; R-MMU-77350; Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 231086; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Hadhb; mouse.
DR PRO; PR:Q99JY0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99JY0; protein.
DR Bgee; ENSMUSG00000059447; Expressed in spermatocyte and 170 other tissues.
DR ExpressionAtlas; Q99JY0; baseline and differential.
DR Genevisible; Q99JY0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016507; C:mitochondrial fatty acid beta-oxidation multienzyme complex; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:MGI.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IDA:MGI.
DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0106222; F:lncRNA binding; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Endoplasmic reticulum; Fatty acid metabolism;
KW Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Mitochondrion outer membrane; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 35..475
FT /note="Trifunctional enzyme subunit beta, mitochondrial"
FT /id="PRO_0000034082"
FT INTRAMEM 174..221
FT /evidence="ECO:0000250|UniProtKB:P55084"
FT ACT_SITE 139
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P55084"
FT ACT_SITE 459
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P55084"
FT SITE 429
FT /note="Increases nucleophilicity of active site Cys"
FT /evidence="ECO:0000250|UniProtKB:P55084"
FT MOD_RES 53
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 73
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 73
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 189
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 189
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 191
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 273
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 292
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 294
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 294
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 333
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 333
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 349
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 362
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 24..25
FT /note="IR -> HK (in Ref. 1; BAC36493)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="L -> M (in Ref. 1; BAC38790)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="G -> R (in Ref. 1; BAC38790)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="G -> V (in Ref. 1; BAC39015)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 51386 MW; F131B497C4F5FAF4 CRC64;
MTTILTSTFR NLSTTSKWAL RSSIRPLSCS SQLHSAPAVQ TKSKKTLAKP NMKNIVVVEG
VRIPFLLSGT SYKDLMPHDL ARAALSGLLH RTNIPKDVVD YIIFGTVIQE VKTSNVAREA
ALGAGFSDKT PAHTVTMACI SSNQAMTTAV GLIASGQCDV VVAGGVELMS DVPIRHSRNM
RKMMLDLNKA KTLGQRLSLL SKFRLNFLSP ELPAVAEFST NETMGHSADR LAAAFAVSRM
EQDEYALRSH SLAKKAQDEG HLSDIVPFKV PGKDTVTKDN GIRPSSLEQM AKLKPAFIKP
YGTVTAANSS FLTDGASAML IMSEDRALAM GYKPKAYLRD FIYVSQDPKD QLLLGPTYAT
PKVLEKAGLT MNDIDAFEFH EAFSGQILAN FKAMDSDWFA QNYMGRKTKV GSPPLEKFNI
WGGSLSLGHP FGATGCRLVM AAANRLRKDG GQYALVAACA AGGQGHAMIV EAYPK
