DPH5_HUMAN
ID DPH5_HUMAN Reviewed; 285 AA.
AC Q9H2P9; A8JZY6; D3DT62; Q9P017; Q9P0I4; Q9Y319;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Diphthine methyl ester synthase;
DE EC=2.1.1.314;
DE AltName: Full=Diphthamide biosynthesis methyltransferase;
GN Name=DPH5; ORFNames=AD-018, CGI-30, HSPC143, NPD015;
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 [LARGE SCALE MRNA] (ISOFORM 5).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Pituitary;
RA Yang Y., Xu X., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION IN DIPHTHAMIDE BIOSYNTHESIS.
RX PubMed=23486472; DOI=10.1074/jbc.m113.461343;
RA Wei H., Bera T.K., Wayne A.S., Xiang L., Colantonio S., Chertov O.,
RA Pastan I.;
RT "A modified form of diphthamide causes immunotoxin resistance in a lymphoma
RT cell line with a deletion of the WDR85 gene.";
RL J. Biol. Chem. 288:12305-12312(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC catalyzes four methylations of the modified target histidine residue in
CC translation elongation factor 2 (EF-2), to form an intermediate called
CC diphthine methyl ester. The four successive methylation reactions
CC represent the second step of diphthamide biosynthesis.
CC {ECO:0000250|UniProtKB:P32469, ECO:0000269|PubMed:23486472}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation
CC elongation factor 2] + 4 S-adenosyl-L-methionine = diphthine methyl
CC ester-[translation elongation factor 2] + 3 H(+) + 4 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:42652, Rhea:RHEA-COMP:9749, Rhea:RHEA-
CC COMP:10173, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73995, ChEBI:CHEBI:79005; EC=2.1.1.314;
CC Evidence={ECO:0000250|UniProtKB:P32469};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9H2P9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H2P9-2; Sequence=VSP_008508;
CC Name=3;
CC IsoId=Q9H2P9-3; Sequence=VSP_008509;
CC Name=4;
CC IsoId=Q9H2P9-4; Sequence=VSP_008510;
CC Name=5;
CC IsoId=Q9H2P9-5; Sequence=VSP_008511;
CC Name=6;
CC IsoId=Q9H2P9-6; Sequence=VSP_043444;
CC -!- SIMILARITY: Belongs to the diphthine synthase family. {ECO:0000305}.
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DR EMBL; AF132964; AAD27739.1; -; mRNA.
DR EMBL; AF157319; AAF67485.1; -; mRNA.
DR EMBL; AF161492; AAF29107.1; -; mRNA.
DR EMBL; AF248965; AAG44563.1; -; mRNA.
DR EMBL; AK289351; BAF82040.1; -; mRNA.
DR EMBL; AC093157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW72933.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72937.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72938.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72940.1; -; Genomic_DNA.
DR EMBL; BC053857; AAH53857.1; -; mRNA.
DR CCDS; CCDS41358.1; -. [Q9H2P9-1]
DR CCDS; CCDS41359.1; -. [Q9H2P9-6]
DR RefSeq; NP_001070862.1; NM_001077394.1. [Q9H2P9-1]
DR RefSeq; NP_001070863.1; NM_001077395.1. [Q9H2P9-6]
DR RefSeq; NP_057042.2; NM_015958.2. [Q9H2P9-1]
DR RefSeq; XP_016856949.1; XM_017001460.1. [Q9H2P9-1]
DR AlphaFoldDB; Q9H2P9; -.
DR SMR; Q9H2P9; -.
DR BioGRID; 119637; 18.
DR IntAct; Q9H2P9; 2.
DR STRING; 9606.ENSP00000359127; -.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR GlyGen; Q9H2P9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H2P9; -.
DR PhosphoSitePlus; Q9H2P9; -.
DR BioMuta; DPH5; -.
DR DMDM; 46397414; -.
DR EPD; Q9H2P9; -.
DR jPOST; Q9H2P9; -.
DR MassIVE; Q9H2P9; -.
DR MaxQB; Q9H2P9; -.
DR PaxDb; Q9H2P9; -.
DR PeptideAtlas; Q9H2P9; -.
DR PRIDE; Q9H2P9; -.
DR ProteomicsDB; 80572; -. [Q9H2P9-1]
DR ProteomicsDB; 80573; -. [Q9H2P9-2]
DR ProteomicsDB; 80574; -. [Q9H2P9-3]
DR ProteomicsDB; 80575; -. [Q9H2P9-4]
DR ProteomicsDB; 80576; -. [Q9H2P9-5]
DR ProteomicsDB; 80577; -. [Q9H2P9-6]
DR Antibodypedia; 33698; 31 antibodies from 9 providers.
DR DNASU; 51611; -.
DR Ensembl; ENST00000342173.11; ENSP00000339630.7; ENSG00000117543.22. [Q9H2P9-6]
DR Ensembl; ENST00000370109.8; ENSP00000359127.3; ENSG00000117543.22. [Q9H2P9-1]
DR Ensembl; ENST00000427040.3; ENSP00000394364.3; ENSG00000117543.22. [Q9H2P9-1]
DR Ensembl; ENST00000488176.1; ENSP00000418282.1; ENSG00000117543.22. [Q9H2P9-1]
DR GeneID; 51611; -.
DR KEGG; hsa:51611; -.
DR MANE-Select; ENST00000370109.8; ENSP00000359127.3; NM_015958.3; NP_057042.2.
DR UCSC; uc001dtr.4; human. [Q9H2P9-1]
DR CTD; 51611; -.
DR DisGeNET; 51611; -.
DR GeneCards; DPH5; -.
DR HGNC; HGNC:24270; DPH5.
DR HPA; ENSG00000117543; Low tissue specificity.
DR MIM; 611075; gene.
DR neXtProt; NX_Q9H2P9; -.
DR OpenTargets; ENSG00000117543; -.
DR PharmGKB; PA142671956; -.
DR VEuPathDB; HostDB:ENSG00000117543; -.
DR eggNOG; KOG3123; Eukaryota.
DR GeneTree; ENSGT00390000010568; -.
DR HOGENOM; CLU_066040_1_0_1; -.
DR InParanoid; Q9H2P9; -.
DR OMA; TAGDPMV; -.
DR OrthoDB; 1018517at2759; -.
DR PhylomeDB; Q9H2P9; -.
DR TreeFam; TF105603; -.
DR BRENDA; 2.1.1.314; 2681.
DR PathwayCommons; Q9H2P9; -.
DR Reactome; R-HSA-5358493; Synthesis of diphthamide-EEF2.
DR SignaLink; Q9H2P9; -.
DR SIGNOR; Q9H2P9; -.
DR UniPathway; UPA00559; -.
DR BioGRID-ORCS; 51611; 142 hits in 1099 CRISPR screens.
DR ChiTaRS; DPH5; human.
DR GeneWiki; DPH5; -.
DR GenomeRNAi; 51611; -.
DR Pharos; Q9H2P9; Tbio.
DR PRO; PR:Q9H2P9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H2P9; protein.
DR Bgee; ENSG00000117543; Expressed in body of pancreas and 208 other tissues.
DR ExpressionAtlas; Q9H2P9; baseline and differential.
DR Genevisible; Q9H2P9; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004164; F:diphthine synthase activity; EXP:Reactome.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR CDD; cd11647; DHP5_DphB; 1.
DR Gene3D; 3.30.950.10; -; 1.
DR Gene3D; 3.40.1010.10; -; 1.
DR HAMAP; MF_01084; Diphthine_synth; 1.
DR InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR InterPro; IPR004551; Dphthn_synthase.
DR PANTHER; PTHR10882; PTHR10882; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF036432; Diphthine_synth; 1.
DR SUPFAM; SSF53790; SSF53790; 1.
DR TIGRFAMs; TIGR00522; dph5; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..285
FT /note="Diphthine methyl ester synthase"
FT /id="PRO_0000156133"
FT BINDING 9
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 112..113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 85..137
FT /note="PFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFW
FT T -> HL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10931946"
FT /id="VSP_008508"
FT VAR_SEQ 88..143
FT /note="ATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWTDT
FT WRPE -> HLETR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11042152"
FT /id="VSP_008509"
FT VAR_SEQ 117..141
FT /note="VGCCGLQLYKFGETVSIVFWTDTWR -> EAAGGYRYISLERQVLLVFGQTL
FT GG (in isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_008510"
FT VAR_SEQ 134..137
FT /note="VFWT -> MLISVMLHSLWLVIHL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10810093"
FT /id="VSP_008511"
FT VAR_SEQ 212
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043444"
FT CONFLICT 107
FT /note="V -> G (in Ref. 4; AAG44563)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="L -> FEHRYFHCLM (in Ref. 2; AAF67485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 31651 MW; 1348631C25BC624E CRC64;
MLYLIGLGLG DAKDITVKGL EVVRRCSRVY LEAYTSVLTV GKEALEEFYG RKLVVADREE
VEQEADNILK DADISDVAFL VVGDPFGATT HSDLVLRATK LGIPYRVIHN ASIMNAVGCC
GLQLYKFGET VSIVFWTDTW RPESFFDKVK KNRQNGMHTL CLLDIKVKEQ SLENLIKGRK
IYEPPRYMSV NQAAQQLLEI VQNQRIRGEE PAVTEETLCV GLARVGADDQ KIAAGTLRQM
CTVDLGEPLH SLIITGGSIH PMEMEMLSLF SIPENSSESQ SINGL
