ACSM1_HUMAN
ID ACSM1_HUMAN Reviewed; 577 AA.
AC Q08AH1; Q08AH2; Q96A20;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Acyl-coenzyme A synthetase ACSM1, mitochondrial;
DE EC=6.2.1.2 {ECO:0000269|PubMed:10434065};
DE AltName: Full=Acyl-CoA synthetase medium-chain family member 1;
DE AltName: Full=Benzoate--CoA ligase;
DE EC=6.2.1.25 {ECO:0000269|PubMed:10434065};
DE AltName: Full=Butyrate--CoA ligase 1;
DE AltName: Full=Butyryl-coenzyme A synthetase 1;
DE AltName: Full=Lipoate-activating enzyme {ECO:0000250|UniProtKB:Q9BEA2};
DE AltName: Full=Middle-chain acyl-CoA synthetase 1;
DE AltName: Full=Xenobiotic/medium-chain fatty acid-CoA ligase HXM-B {ECO:0000303|PubMed:10434065};
DE Flags: Precursor;
GN Name=ACSM1; Synonyms=BUCS1, LAE {ECO:0000250|UniProtKB:Q9BEA2}, MACS1;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10434065; DOI=10.1016/s0304-4165(99)00088-4;
RA Vessey D.A., Kelley M., Warren R.S.;
RT "Characterization of the CoA ligases of human liver mitochondria catalyzing
RT the activation of short- and medium-chain fatty acids and xenobiotic
RT carboxylic acids.";
RL Biochim. Biophys. Acta 1428:455-462(1999).
RN [4]
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 [5]
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).
CC -!- FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an
CC acyl-CoA, the first step in fatty acid metabolism (PubMed:10434065).
CC Capable of activating medium-chain fatty acids (e.g. butyric (C4) to
CC decanoic (C10) acids), and certain carboxylate-containing xenobiotics,
CC e.g. benzoate (PubMed:10434065). Also catalyzes the activation of
CC lipoate to lipoyl-nucleoside monophosphate (By similarity). Activates
CC lipoate with GTP at a 1000-fold higher rate than with ATP and activates
CC both (R)- and (S)-lipoate to the respective lipoyl-GMP, with a
CC preference for (R)-lipoate (By similarity).
CC {ECO:0000250|UniProtKB:Q9BEA2, ECO:0000269|PubMed:10434065}.
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:10434065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000305|PubMed:10434065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + benzoate + CoA = AMP + benzoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:10132, ChEBI:CHEBI:16150, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57369,
CC ChEBI:CHEBI:456215; EC=6.2.1.25;
CC Evidence={ECO:0000269|PubMed:10434065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10133;
CC Evidence={ECO:0000269|PubMed:10434065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lipoate + GTP + H(+) = (R)-lipoyl-GMP + diphosphate;
CC Xref=Rhea:RHEA:46700, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:83088, ChEBI:CHEBI:86460;
CC Evidence={ECO:0000250|UniProtKB:Q9BEA2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46701;
CC Evidence={ECO:0000250|UniProtKB:Q9BEA2};
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:Q91VA0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + decanoate = AMP + decanoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:33627, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:10434065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628;
CC Evidence={ECO:0000305|PubMed:10434065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA;
CC Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetradecanoate = AMP + diphosphate +
CC tetradecanoyl-CoA; Xref=Rhea:RHEA:33619, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA;
CC Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000305|PubMed:10434065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
CC Evidence={ECO:0000305|PubMed:10434065};
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:0000305|PubMed:10434065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC Evidence={ECO:0000305|PubMed:10434065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10434065};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10434065};
CC -!- ACTIVITY REGULATION: Activated by monovalent cations, such as
CC potassium, rubidium or ammonium. {ECO:0000269|PubMed:10434065}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for benzoate {ECO:0000269|PubMed:10434065};
CC KM=570 uM for butyrate {ECO:0000269|PubMed:10434065};
CC KM=20 uM for decanoate {ECO:0000269|PubMed:10434065};
CC KM=34 uM for hexanoate {ECO:0000269|PubMed:10434065};
CC KM=24 uM for laurate {ECO:0000269|PubMed:10434065};
CC KM=143 uM for phenylacetate {ECO:0000269|PubMed:10434065};
CC KM=25 uM for salicylate {ECO:0000269|PubMed:10434065};
CC Vmax=9 nmol/min/mg enzyme for benzoate {ECO:0000269|PubMed:10434065};
CC Vmax=24 nmol/min/mg enzyme for butyrate
CC {ECO:0000269|PubMed:10434065};
CC Vmax=8 nmol/min/mg enzyme for decanoate
CC {ECO:0000269|PubMed:10434065};
CC Vmax=118 nmol/min/mg enzyme for hexanoate
CC {ECO:0000269|PubMed:10434065};
CC Vmax=0.15 nmol/min/mg enzyme for laurate
CC {ECO:0000269|PubMed:10434065};
CC Vmax=2 nmol/min/mg enzyme for phenylacetate
CC {ECO:0000269|PubMed:10434065};
CC pH dependence:
CC Optimum pH is 8.8. {ECO:0000269|PubMed:10434065};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9BEA2}.
CC -!- INTERACTION:
CC Q08AH1; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-2818055, EBI-11522780;
CC Q08AH1; P43356: MAGEA2B; NbExp=3; IntAct=EBI-2818055, EBI-5650739;
CC Q08AH1; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2818055, EBI-11522433;
CC Q08AH1; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-2818055, EBI-1051317;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q91VA0}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q91VA0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q08AH1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08AH1-2; Sequence=VSP_028391;
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AB059429; BAB64535.1; -; mRNA.
DR EMBL; AB062503; BAB68363.1; -; Genomic_DNA.
DR EMBL; BC125177; AAI25178.1; -; mRNA.
DR EMBL; BC125178; AAI25179.1; -; mRNA.
DR CCDS; CCDS10587.1; -. [Q08AH1-1]
DR RefSeq; NP_001305819.1; NM_001318890.1. [Q08AH1-1]
DR RefSeq; NP_443188.2; NM_052956.2. [Q08AH1-1]
DR AlphaFoldDB; Q08AH1; -.
DR SMR; Q08AH1; -.
DR BioGRID; 125496; 10.
DR IntAct; Q08AH1; 9.
DR STRING; 9606.ENSP00000301956; -.
DR SwissLipids; SLP:000000449; -.
DR iPTMnet; Q08AH1; -.
DR PhosphoSitePlus; Q08AH1; -.
DR BioMuta; ACSM1; -.
DR DMDM; 121940002; -.
DR MassIVE; Q08AH1; -.
DR PaxDb; Q08AH1; -.
DR PeptideAtlas; Q08AH1; -.
DR PRIDE; Q08AH1; -.
DR ProteomicsDB; 58670; -. [Q08AH1-1]
DR ProteomicsDB; 58671; -. [Q08AH1-2]
DR TopDownProteomics; Q08AH1-1; -. [Q08AH1-1]
DR Antibodypedia; 49877; 70 antibodies from 18 providers.
DR DNASU; 116285; -.
DR Ensembl; ENST00000307493.8; ENSP00000301956.3; ENSG00000166743.10. [Q08AH1-1]
DR Ensembl; ENST00000519745.5; ENSP00000428650.1; ENSG00000166743.10. [Q08AH1-2]
DR Ensembl; ENST00000520010.6; ENSP00000428047.1; ENSG00000166743.10. [Q08AH1-1]
DR GeneID; 116285; -.
DR KEGG; hsa:116285; -.
DR MANE-Select; ENST00000520010.6; ENSP00000428047.1; NM_001318890.3; NP_001305819.1.
DR UCSC; uc002dhm.1; human. [Q08AH1-1]
DR CTD; 116285; -.
DR DisGeNET; 116285; -.
DR GeneCards; ACSM1; -.
DR HGNC; HGNC:18049; ACSM1.
DR HPA; ENSG00000166743; Tissue enriched (breast).
DR MIM; 614357; gene.
DR neXtProt; NX_Q08AH1; -.
DR OpenTargets; ENSG00000166743; -.
DR PharmGKB; PA25468; -.
DR VEuPathDB; HostDB:ENSG00000166743; -.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000161138; -.
DR HOGENOM; CLU_000022_59_10_1; -.
DR InParanoid; Q08AH1; -.
DR OMA; ECTAPCA; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q08AH1; -.
DR TreeFam; TF354287; -.
DR BioCyc; MetaCyc:HS09445-MON; -.
DR PathwayCommons; Q08AH1; -.
DR Reactome; R-HSA-177135; Conjugation of benzoate with glycine.
DR Reactome; R-HSA-177162; Conjugation of phenylacetate with glutamine.
DR SignaLink; Q08AH1; -.
DR BioGRID-ORCS; 116285; 14 hits in 1071 CRISPR screens.
DR ChiTaRS; ACSM1; human.
DR GenomeRNAi; 116285; -.
DR Pharos; Q08AH1; Tbio.
DR PRO; PR:Q08AH1; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q08AH1; protein.
DR Bgee; ENSG00000166743; Expressed in left ovary and 93 other tissues.
DR ExpressionAtlas; Q08AH1; baseline and differential.
DR Genevisible; Q08AH1; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0018858; F:benzoate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0016405; F:CoA-ligase activity; TAS:Reactome.
DR GO; GO:0102391; F:decanoate-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:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0018874; P:benzoate metabolic process; NAS:UniProtKB.
DR GO; GO:0019605; P:butyrate metabolic process; NAS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; NAS:BHF-UCL.
DR GO; GO:0015980; P:energy derivation by oxidation of organic compounds; NAS:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0019395; P:fatty acid oxidation; NAS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
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 GTP-binding; Ligase; Lipid metabolism; Magnesium; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 32..577
FT /note="Acyl-coenzyme A synthetase ACSM1, mitochondrial"
FT /id="PRO_0000306091"
FT BINDING 226..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 146
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 146
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 183
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 204
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 204
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 214
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 237
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 356
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 356
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 391
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 391
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 531
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 538
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 538
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT MOD_RES 549
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT VAR_SEQ 205..577
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028391"
FT VARIANT 272
FT /note="I -> M (in dbSNP:rs16970511)"
FT /id="VAR_048238"
FT VARIANT 479
FT /note="I -> V (in dbSNP:rs8056709)"
FT /id="VAR_035245"
FT VARIANT 515
FT /note="I -> T (in dbSNP:rs16970453)"
FT /id="VAR_035246"
FT CONFLICT 549
FT /note="K -> N (in Ref. 1; BAB64535/BAB68363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 65273 MW; 380BF4B8944B0E34 CRC64;
MQWLMRFRTL WGIHKSFHNI HPAPSQLRCR SLSEFGAPRW NDYEVPEEFN FASYVLDYWA
QKEKEGKRGP NPAFWWVNGQ GDEVKWSFRE MGDLTRRVAN VFTQTCGLQQ GDHLALMLPR
VPEWWLVAVG CMRTGIIFIP ATILLKAKDI LYRLQLSKAK GIVTIDALAS EVDSIASQCP
SLKTKLLVSD HSREGWLDFR SLVKSASPEH TCVKSKTLDP MVIFFTSGTT GFPKMAKHSH
GLALQPSFPG SRKLRSLKTS DVSWCLSDSG WIVATIWTLV EPWTAGCTVF IHHLPQFDTK
VIIQTLLKYP INHFWGVSSI YRMILQQDFT SIRFPALEHC YTGGEVVLPK DQEEWKRRTG
LLLYENYGQS ETGLICATYW GMKIKPGFMG KATPPYDVQV IDDKGSILPP NTEGNIGIRI
KPVRPVSLFM CYEGDPEKTA KVECGDFYNT GDRGKMDEEG YICFLGRSDD IINASGYRIG
PAEVESALVE HPAVAESAVV GSPDPIRGEV VKAFIVLTPQ FLSHDKDQLT KELQQHVKSV
TAPYKYPRKV EFVSELPKTI TGKIERKELR KKETGQM
