ID   HEM1_HUMAN              Reviewed;         640 AA.
AC   P13196;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 2.
DT   27-MAR-2024, entry version 222.
DE   RecName: Full=5-aminolevulinate synthase, non-specific, mitochondrial;
DE            Short=ALAS-H;
DE            EC=2.3.1.37 {ECO:0000269|PubMed:16234850, ECO:0000269|PubMed:17975826};
DE   AltName: Full=5-aminolevulinic acid synthase 1;
DE   AltName: Full=Delta-ALA synthase 1;
DE   AltName: Full=Delta-aminolevulinate synthase 1;
DE   Flags: Precursor;
GN   Name=ALAS1; Synonyms=ALAS3, ALASH; ORFNames=OK/SW-cl.121;
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=2263504; DOI=10.1093/nar/18.23.7187;
RA   Bishop D.F.;
RT   "Two different genes encode delta-aminolevulinate synthase in humans:
RT   nucleotide sequences of cDNAs for the housekeeping and erythroid genes.";
RL   Nucleic Acids Res. 18:7187-7188(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Liver;
RX   PubMed=3671094; DOI=10.1093/nar/15.20.8563;
RA   Bawden M.J., Borthwick I.A., Healy H.M., Morris C.P., May B.K.,
RA   Elliott W.H.;
RT   "Sequence of human 5-aminolevulinate synthase cDNA.";
RL   Nucleic Acids Res. 15:8563-8563(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon adenocarcinoma;
RA   Shichijo S., Itoh K.;
RT   "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT   CTL generated from TIL of colon cancer patients.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
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   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, HYDROXYLATION
RP   AT PRO-576, MUTAGENESIS OF PRO-576, UBIQUITINATION, PROTEASOMAL
RP   DEGRADATION, AND INTERACTION WITH VHL.
RX   PubMed=16234850; DOI=10.1139/o05-045;
RA   Abu-Farha M., Niles J., Willmore W.G.;
RT   "Erythroid-specific 5-aminolevulinate synthase protein is stabilized by low
RT   oxygen and proteasomal inhibition.";
RL   Biochem. Cell Biol. 83:620-630(2005).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND ACTIVITY REGULATION.
RX   PubMed=17975826; DOI=10.1002/hep.21879;
RA   Peyer A.K., Jung D., Beer M., Gnerre C., Keogh A., Stroka D., Zavolan M.,
RA   Meyer U.A.;
RT   "Regulation of human liver delta-aminolevulinic acid synthase by bile
RT   acids.";
RL   Hepatology 46:1960-1970(2007).
CC   -!- FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent
CC       condensation of succinyl-CoA and glycine to form aminolevulinic acid
CC       (ALA), with CoA and CO2 as by-products. {ECO:0000269|PubMed:16234850,
CC       ECO:0000269|PubMed:17975826}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA;
CC         Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:356416; EC=2.3.1.37;
CC         Evidence={ECO:0000269|PubMed:16234850, ECO:0000269|PubMed:17975826};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12922;
CC         Evidence={ECO:0000305|PubMed:16234850};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000305|PubMed:16234850};
CC   -!- ACTIVITY REGULATION: Activity increases about 2-fold over 72 hours of
CC       hypoxia compared with normoxia (PubMed:16234850). Activity increases in
CC       the presence of phenobarbital, chenodeoxycholic and NR1H4/FXR-specific
CC       agonist GW4064 (PubMed:17975826). {ECO:0000269|PubMed:16234850,
CC       ECO:0000269|PubMed:17975826}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from glycine: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts (hydroxylated form) with
CC       VHL (PubMed:16234850). {ECO:0000250|UniProtKB:P22557,
CC       ECO:0000269|PubMed:16234850}.
CC   -!- INTERACTION:
CC       P13196; P13196: ALAS1; NbExp=4; IntAct=EBI-3905054, EBI-3905054;
CC       P13196; Q4VC05: BCL7A; NbExp=3; IntAct=EBI-3905054, EBI-359917;
CC       P13196; Q9NWW7: C2orf42; NbExp=3; IntAct=EBI-3905054, EBI-2812028;
CC       P13196; P40123: CAP2; NbExp=3; IntAct=EBI-3905054, EBI-1051165;
CC       P13196; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-3905054, EBI-10175300;
CC       P13196; Q6P1J9: CDC73; NbExp=9; IntAct=EBI-3905054, EBI-930143;
CC       P13196; Q8TCT0: CERK; NbExp=3; IntAct=EBI-3905054, EBI-10274247;
CC       P13196; O75128: COBL; NbExp=3; IntAct=EBI-3905054, EBI-3446582;
CC       P13196; O14645: DNALI1; NbExp=3; IntAct=EBI-3905054, EBI-395638;
CC       P13196; Q8WTR2: DUSP19; NbExp=8; IntAct=EBI-3905054, EBI-8654968;
CC       P13196; A0A0A0MR80: EP400; NbExp=3; IntAct=EBI-3905054, EBI-12089140;
CC       P13196; Q96L91: EP400; NbExp=4; IntAct=EBI-3905054, EBI-399163;
CC       P13196; Q96CD0: FBXL8; NbExp=3; IntAct=EBI-3905054, EBI-2321097;
CC       P13196; Q9NVN8: GNL3L; NbExp=3; IntAct=EBI-3905054, EBI-746682;
CC       P13196; A8MXD5: GRXCR1; NbExp=3; IntAct=EBI-3905054, EBI-5235612;
CC       P13196; C9JCN9: HSBP1L1; NbExp=3; IntAct=EBI-3905054, EBI-2685549;
CC       P13196; Q9UMF0: ICAM5; NbExp=3; IntAct=EBI-3905054, EBI-6398041;
CC       P13196; O75564-2: JRK; NbExp=3; IntAct=EBI-3905054, EBI-17181882;
CC       P13196; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-3905054, EBI-8472129;
CC       P13196; Q6PF15: KLHL35; NbExp=4; IntAct=EBI-3905054, EBI-9477654;
CC       P13196; Q17RB8: LONRF1; NbExp=6; IntAct=EBI-3905054, EBI-2341787;
CC       P13196; Q96CN5: LRRC45; NbExp=3; IntAct=EBI-3905054, EBI-2805176;
CC       P13196; Q6P444: MTFR2; NbExp=5; IntAct=EBI-3905054, EBI-10252703;
CC       P13196; Q765P7: MTSS2; NbExp=3; IntAct=EBI-3905054, EBI-2815102;
CC       P13196; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-3905054, EBI-14066006;
CC       P13196; Q9Y2S7: POLDIP2; NbExp=4; IntAct=EBI-3905054, EBI-713000;
CC       P13196; O60437: PPL; NbExp=6; IntAct=EBI-3905054, EBI-368321;
CC       P13196; Q8IYW5: RNF168; NbExp=3; IntAct=EBI-3905054, EBI-914207;
CC       P13196; Q17RB0: RTL8B; NbExp=6; IntAct=EBI-3905054, EBI-10238588;
CC       P13196; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-3905054, EBI-747035;
CC       P13196; P08579: SNRPB2; NbExp=3; IntAct=EBI-3905054, EBI-1053651;
CC       P13196; Q7Z614: SNX20; NbExp=3; IntAct=EBI-3905054, EBI-744896;
CC       P13196; Q15560: TCEA2; NbExp=3; IntAct=EBI-3905054, EBI-710310;
CC       P13196; Q8WW24: TEKT4; NbExp=6; IntAct=EBI-3905054, EBI-750487;
CC       P13196; P63313: TMSB10; NbExp=6; IntAct=EBI-3905054, EBI-2688673;
CC       P13196; Q0P5Q0: TMSB4X; NbExp=3; IntAct=EBI-3905054, EBI-10226570;
CC       P13196; Q5W5X9: TTC23; NbExp=3; IntAct=EBI-3905054, EBI-6447954;
CC       P13196; Q9Y2K6: USP20; NbExp=3; IntAct=EBI-3905054, EBI-2511991;
CC       P13196; Q5TAP6: UTP14C; NbExp=3; IntAct=EBI-3905054, EBI-11737646;
CC       P13196; O43516: WIPF1; NbExp=3; IntAct=EBI-3905054, EBI-346356;
CC       P13196; Q68DK2-5: ZFYVE26; NbExp=3; IntAct=EBI-3905054, EBI-8656416;
CC       P13196; Q9Y473: ZNF175; NbExp=6; IntAct=EBI-3905054, EBI-3438881;
CC       P13196; Q8TBZ8: ZNF564; NbExp=6; IntAct=EBI-3905054, EBI-10273713;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P22557}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P22557}. Note=Localizes to the matrix side of
CC       the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P22557}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P13196-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P13196-2; Sequence=VSP_025925, VSP_025924;
CC   -!- INDUCTION: Up-regulated by bile acids; chenodeoxycholic acid,
CC       ursodeoxycholic acid and lithocholic acid and by the NR1H4/FXR-specific
CC       agonist GW4064. {ECO:0000269|PubMed:17975826}.
CC   -!- PTM: In normoxia, is hydroxylated at Pro-576, promoting interaction
CC       with VHL, initiating ubiquitination and subsequent degradation via the
CC       proteasome. {ECO:0000269|PubMed:16234850}.
CC   -!- PTM: Ubiquitinated; in normoxia following hydroxylation and interaction
CC       with VHL, leading to its subsequent degradation via the proteasome.
CC       {ECO:0000269|PubMed:16234850}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA68506.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X56351; CAA39794.1; -; mRNA.
DR   EMBL; Y00451; CAA68506.1; ALT_FRAME; mRNA.
DR   EMBL; AB063322; BAB93514.1; -; mRNA.
DR   EMBL; BC011798; AAH11798.1; -; mRNA.
DR   CCDS; CCDS2847.1; -. [P13196-1]
DR   PIR; S13682; SYHUAL.
DR   RefSeq; NP_000679.1; NM_000688.5. [P13196-1]
DR   RefSeq; NP_001291372.1; NM_001304443.1. [P13196-1]
DR   RefSeq; NP_001291373.1; NM_001304444.1.
DR   RefSeq; NP_954635.1; NM_199166.2. [P13196-1]
DR   AlphaFoldDB; P13196; -.
DR   SMR; P13196; -.
DR   BioGRID; 106713; 150.
DR   IntAct; P13196; 73.
DR   MINT; P13196; -.
DR   STRING; 9606.ENSP00000378416; -.
DR   DrugBank; DB00145; Glycine.
DR   DrugBank; DB00114; Pyridoxal phosphate.
DR   DrugCentral; P13196; -.
DR   iPTMnet; P13196; -.
DR   MetOSite; P13196; -.
DR   PhosphoSitePlus; P13196; -.
DR   BioMuta; ALAS1; -.
DR   DMDM; 122824; -.
DR   EPD; P13196; -.
DR   jPOST; P13196; -.
DR   MassIVE; P13196; -.
DR   MaxQB; P13196; -.
DR   PaxDb; 9606-ENSP00000378416; -.
DR   PeptideAtlas; P13196; -.
DR   ProteomicsDB; 52898; -. [P13196-1]
DR   Pumba; P13196; -.
DR   Antibodypedia; 4303; 372 antibodies from 34 providers.
DR   DNASU; 211; -.
DR   Ensembl; ENST00000310271.6; ENSP00000309259.2; ENSG00000023330.15. [P13196-1]
DR   Ensembl; ENST00000394965.6; ENSP00000378416.2; ENSG00000023330.15. [P13196-1]
DR   Ensembl; ENST00000469224.5; ENSP00000417719.1; ENSG00000023330.15. [P13196-1]
DR   Ensembl; ENST00000484952.6; ENSP00000418779.1; ENSG00000023330.15. [P13196-1]
DR   GeneID; 211; -.
DR   KEGG; hsa:211; -.
DR   MANE-Select; ENST00000484952.6; ENSP00000418779.1; NM_000688.6; NP_000679.1.
DR   AGR; HGNC:396; -.
DR   CTD; 211; -.
DR   DisGeNET; 211; -.
DR   GeneCards; ALAS1; -.
DR   HGNC; HGNC:396; ALAS1.
DR   HPA; ENSG00000023330; Group enriched (adrenal gland, bone marrow, liver).
DR   MIM; 125290; gene.
DR   neXtProt; NX_P13196; -.
DR   OpenTargets; ENSG00000023330; -.
DR   PharmGKB; PA24688; -.
DR   VEuPathDB; HostDB:ENSG00000023330; -.
DR   eggNOG; KOG1360; Eukaryota.
DR   GeneTree; ENSGT00940000156030; -.
DR   HOGENOM; CLU_015846_6_1_1; -.
DR   InParanoid; P13196; -.
DR   OMA; RAYFSGM; -.
DR   OrthoDB; 9643at2759; -.
DR   PhylomeDB; P13196; -.
DR   TreeFam; TF300724; -.
DR   BioCyc; MetaCyc:HS00424-MONOMER; -.
DR   BRENDA; 2.3.1.37; 2681.
DR   PathwayCommons; P13196; -.
DR   Reactome; R-HSA-189451; Heme biosynthesis.
DR   Reactome; R-HSA-1989781; PPARA activates gene expression.
DR   Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR   SignaLink; P13196; -.
DR   UniPathway; UPA00251; UER00375.
DR   BioGRID-ORCS; 211; 56 hits in 1166 CRISPR screens.
DR   ChiTaRS; ALAS1; human.
DR   GeneWiki; ALAS1; -.
DR   GenomeRNAi; 211; -.
DR   Pharos; P13196; Tclin.
DR   PRO; PR:P13196; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; P13196; Protein.
DR   Bgee; ENSG00000023330; Expressed in right adrenal gland cortex and 200 other cell types or tissues.
DR   ExpressionAtlas; P13196; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003870; F:5-aminolevulinate synthase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0048821; P:erythrocyte development; IBA:GO_Central.
DR   GO; GO:0006784; P:heme A biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006785; P:heme B biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR   GO; GO:0048034; P:heme O biosynthetic process; IEA:Ensembl.
DR   GO; GO:0042541; P:hemoglobin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:1903412; P:response to bile acid; IDA:UniProtKB.
DR   CDD; cd06454; KBL_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010961; 4pyrrol_synth_NH2levulA_synth.
DR   InterPro; IPR015118; 5aminolev_synth_preseq.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01821; 5aminolev_synth; 1.
DR   PANTHER; PTHR13693:SF50; 5-AMINOLEVULINATE SYNTHASE, NON-SPECIFIC, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF09029; Preseq_ALAS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
DR   Genevisible; P13196; HS.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative splicing; Heme biosynthesis; Hydroxylation;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Pyridoxal phosphate;
KW   Reference proteome; Transferase; Transit peptide; Ubl conjugation.
FT   TRANSIT         1..56
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P07997"
FT   CHAIN           57..640
FT                   /note="5-aminolevulinate synthase, non-specific,
FT                   mitochondrial"
FT                   /id="PRO_0000001230"
FT   REGION          60..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        445
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         386
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         414
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         442
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         474
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         475
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         562
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   MOD_RES         445
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   MOD_RES         576
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:16234850"
FT   VAR_SEQ         95..118
FT                   /note="HPLPATSQGTASKCPFLAAQMNQR -> FRLDTPCLPQARALQANALSWQHR
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:3671094"
FT                   /id="VSP_025925"
FT   VAR_SEQ         119..640
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:3671094"
FT                   /id="VSP_025924"
FT   MUTAGEN         576
FT                   /note="P->A: Loss of interaction with VHL."
FT                   /evidence="ECO:0000269|PubMed:16234850"
FT   CONFLICT        2
FT                   /note="E -> D (in Ref. 2; CAA68506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        6
FT                   /note="R -> G (in Ref. 2; CAA68506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="P -> Q (in Ref. 2; CAA68506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        47
FT                   /note="A -> G (in Ref. 2; CAA68506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        56..57
FT                   /note="QQ -> HK (in Ref. 2; CAA68506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="K -> Q (in Ref. 2; CAA68506)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   640 AA;  70581 MW;  5E952DCCFFD6873F CRC64;
     MESVVRRCPF LSRVPQAFLQ KAGKSLLFYA QNCPKMMEVG AKPAPRALST AAVHYQQIKE
     TPPASEKDKT AKAKVQQTPD GSQQSPDGTQ LPSGHPLPAT SQGTASKCPF LAAQMNQRGS
     SVFCKASLEL QEDVQEMNAV RKEVAETSAG PSVVSVKTDG GDPSGLLKNF QDIMQKQRPE
     RVSHLLQDNL PKSVSTFQYD RFFEKKIDEK KNDHTYRVFK TVNRRAHIFP MADDYSDSLI
     TKKQVSVWCS NDYLGMSRHP RVCGAVMDTL KQHGAGAGGT RNISGTSKFH VDLERELADL
     HGKDAALLFS SCFVANDSTL FTLAKMMPGC EIYSDSGNHA SMIQGIRNSR VPKYIFRHND
     VSHLRELLQR SDPSVPKIVA FETVHSMDGA VCPLEELCDV AHEFGAITFV DEVHAVGLYG
     ARGGGIGDRD GVMPKMDIIS GTLGKAFGCV GGYIASTSSL IDTVRSYAAG FIFTTSLPPM
     LLAGALESVR ILKSAEGRVL RRQHQRNVKL MRQMLMDAGL PVVHCPSHII PVRVADAAKN
     TEVCDELMSR HNIYVQAINY PTVPRGEELL RIAPTPHHTP QMMNYFLENL LVTWKQVGLE
     LKPHSSAECN FCRRPLHFEV MSEREKSYFS GLSKLVSAQA
//