HEM1_HUMAN
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 03-AUG-2022, entry version 214.
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 h 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; 145.
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; P13196; -.
DR PeptideAtlas; P13196; -.
DR PRIDE; P13196; -.
DR ProteomicsDB; 52898; -. [P13196-1]
DR ProteomicsDB; 52899; -. [P13196-2]
DR Antibodypedia; 4303; 306 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 CTD; 211; -.
DR DisGeNET; 211; -.
DR GeneCards; ALAS1; -.
DR HGNC; HGNC:396; ALAS1.
DR HPA; ENSG00000023330; Tissue enhanced (adrenal gland, 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; 930001at2759; -.
DR PhylomeDB; P13196; -.
DR TreeFam; TF300724; -.
DR BioCyc; MetaCyc:HS00424-MON; -.
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; 47 hits in 1085 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 199 other tissues.
DR ExpressionAtlas; P13196; baseline and differential.
DR Genevisible; P13196; HS.
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:0006783; P:heme biosynthetic process; IBA:GO_Central.
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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF09029; Preseq_ALAS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01821; 5aminolev_synth; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
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
