PRDC1_HUMAN
ID PRDC1_HUMAN Reviewed; 225 AA.
AC Q9NRG1; B7Z1Z3; Q53HA7; Q59EL9; Q5VV18; Q5VV20;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Phosphoribosyltransferase domain-containing protein 1;
GN Name=PRTFDC1; Synonyms=HHGP;
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 1).
RC TISSUE=Liver cancer;
RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human liver cancer tissue.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORMS 2 AND 3).
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH GMP; PHOSPHATE AND
RP CALCIUM IONS, SUBUNIT, AND ABSENCE OF PHOSPHORIBOSYLTRANSFERASE ACTIVITY.
RX PubMed=21054786; DOI=10.1111/j.1742-4658.2010.07897.x;
RA Welin M., Egeblad L., Johansson A., Stenmark P., Wang L., Flodin S.,
RA Nyman T., Tresaugues L., Kotenyova T., Johansson I., Eriksson S.,
RA Eklund H., Nordlund P.;
RT "Structural and functional studies of the human phosphoribosyltransferase
RT domain containing protein 1.";
RL FEBS J. 277:4920-4930(2010).
CC -!- FUNCTION: Has low, barely detectable phosphoribosyltransferase activity
CC (in vitro). Binds GMP, IMP and alpha-D-5-phosphoribosyl 1-pyrophosphate
CC (PRPP). Is not expected to contribute to purine metabolism or GMP
CC salvage.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21054786}.
CC -!- INTERACTION:
CC Q9NRG1; Q96F85: CNRIP1; NbExp=3; IntAct=EBI-739759, EBI-958255;
CC Q9NRG1; Q96G04: EEF2KMT; NbExp=8; IntAct=EBI-739759, EBI-747840;
CC Q9NRG1; Q7L775: EPM2AIP1; NbExp=6; IntAct=EBI-739759, EBI-6255981;
CC Q9NRG1; Q8NFF5-2: FLAD1; NbExp=3; IntAct=EBI-739759, EBI-11526128;
CC Q9NRG1; P46926: GNPDA1; NbExp=3; IntAct=EBI-739759, EBI-749356;
CC Q9NRG1; P00492: HPRT1; NbExp=11; IntAct=EBI-739759, EBI-748210;
CC Q9NRG1; Q3B8N2: LGALS9B; NbExp=3; IntAct=EBI-739759, EBI-10240775;
CC Q9NRG1; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-739759, EBI-739832;
CC Q9NRG1; Q9BTE3: MCMBP; NbExp=3; IntAct=EBI-739759, EBI-749378;
CC Q9NRG1; Q9BTE3-2: MCMBP; NbExp=6; IntAct=EBI-739759, EBI-9384556;
CC Q9NRG1; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-739759, EBI-741158;
CC Q9NRG1; A0A0B4J2F2: SIK1B; NbExp=3; IntAct=EBI-739759, EBI-22345187;
CC Q9NRG1; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-739759, EBI-742688;
CC Q9NRG1; P56279: TCL1A; NbExp=6; IntAct=EBI-739759, EBI-749995;
CC Q9NRG1; O00534: VWA5A; NbExp=3; IntAct=EBI-739759, EBI-12246480;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NRG1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRG1-2; Sequence=VSP_031180;
CC Name=3;
CC IsoId=Q9NRG1-3; Sequence=VSP_031179;
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved active site Asp and has no significant
CC phosphoribosyltransferase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93029.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF226056; AAF86956.1; -; mRNA.
DR EMBL; AK021950; BAB13944.1; -; mRNA.
DR EMBL; AB209792; BAD93029.1; ALT_INIT; mRNA.
DR EMBL; AK222674; BAD96394.1; -; mRNA.
DR EMBL; AK294130; BAH11679.1; -; mRNA.
DR EMBL; AL157385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86120.1; -; Genomic_DNA.
DR EMBL; BC008662; AAH08662.1; -; mRNA.
DR CCDS; CCDS60506.1; -. [Q9NRG1-2]
DR CCDS; CCDS7145.1; -. [Q9NRG1-1]
DR RefSeq; NP_001269715.1; NM_001282786.1. [Q9NRG1-2]
DR RefSeq; NP_064585.1; NM_020200.6. [Q9NRG1-1]
DR PDB; 2JBH; X-ray; 1.70 A; A/B=1-225.
DR PDBsum; 2JBH; -.
DR AlphaFoldDB; Q9NRG1; -.
DR SMR; Q9NRG1; -.
DR BioGRID; 121276; 38.
DR IntAct; Q9NRG1; 31.
DR MINT; Q9NRG1; -.
DR STRING; 9606.ENSP00000318602; -.
DR iPTMnet; Q9NRG1; -.
DR PhosphoSitePlus; Q9NRG1; -.
DR BioMuta; PRTFDC1; -.
DR DMDM; 74752920; -.
DR EPD; Q9NRG1; -.
DR jPOST; Q9NRG1; -.
DR MassIVE; Q9NRG1; -.
DR MaxQB; Q9NRG1; -.
DR PaxDb; Q9NRG1; -.
DR PeptideAtlas; Q9NRG1; -.
DR PRIDE; Q9NRG1; -.
DR ProteomicsDB; 82352; -. [Q9NRG1-1]
DR ProteomicsDB; 82353; -. [Q9NRG1-2]
DR ProteomicsDB; 82354; -. [Q9NRG1-3]
DR Antibodypedia; 12431; 269 antibodies from 30 providers.
DR DNASU; 56952; -.
DR Ensembl; ENST00000320152.11; ENSP00000318602.5; ENSG00000099256.19. [Q9NRG1-1]
DR Ensembl; ENST00000376376.3; ENSP00000365556.3; ENSG00000099256.19. [Q9NRG1-3]
DR Ensembl; ENST00000376378.5; ENSP00000365558.1; ENSG00000099256.19. [Q9NRG1-2]
DR GeneID; 56952; -.
DR KEGG; hsa:56952; -.
DR MANE-Select; ENST00000320152.11; ENSP00000318602.5; NM_020200.7; NP_064585.1.
DR UCSC; uc001ise.3; human. [Q9NRG1-1]
DR CTD; 56952; -.
DR DisGeNET; 56952; -.
DR GeneCards; PRTFDC1; -.
DR HGNC; HGNC:23333; PRTFDC1.
DR HPA; ENSG00000099256; Low tissue specificity.
DR MIM; 610751; gene.
DR neXtProt; NX_Q9NRG1; -.
DR OpenTargets; ENSG00000099256; -.
DR PharmGKB; PA134888009; -.
DR VEuPathDB; HostDB:ENSG00000099256; -.
DR eggNOG; KOG3367; Eukaryota.
DR GeneTree; ENSGT00940000162225; -.
DR HOGENOM; CLU_073615_3_0_1; -.
DR InParanoid; Q9NRG1; -.
DR OMA; IEFMAVS; -.
DR OrthoDB; 1537610at2759; -.
DR PhylomeDB; Q9NRG1; -.
DR TreeFam; TF313367; -.
DR PathwayCommons; Q9NRG1; -.
DR SignaLink; Q9NRG1; -.
DR BioGRID-ORCS; 56952; 6 hits in 1072 CRISPR screens.
DR ChiTaRS; PRTFDC1; human.
DR EvolutionaryTrace; Q9NRG1; -.
DR GenomeRNAi; 56952; -.
DR Pharos; Q9NRG1; Tbio.
DR PRO; PR:Q9NRG1; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NRG1; protein.
DR Bgee; ENSG00000099256; Expressed in corpus callosum and 172 other tissues.
DR Genevisible; Q9NRG1; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; TAS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:InterPro.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR InterPro; IPR005904; Hxn_phspho_trans.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01203; HGPRTase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..225
FT /note="Phosphoribosyltransferase domain-containing protein
FT 1"
FT /id="PRO_0000318176"
FT BINDING 141..149
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|PubMed:21054786"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 173
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|PubMed:21054786"
FT BINDING 194..195
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|PubMed:21054786"
FT BINDING 201
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|PubMed:21054786"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT VAR_SEQ 114..225
FT /note="NDQSMGEMQIIGGDDLSTLAGKNVLIVEDVVGTGRTMKALLSNIEKYKPNMI
FT KVASLLVKRTSRSDGFRPDYAGFEIPNLFVVGYALDYNEYFRDLNHICVINEHGKEKYR
FT V -> LRARLKRTTICDRGGLAFSQGYMSSCAPLQESPNTLWRGYLQVLIPCFHIRFQL
FT PRSEQN (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_031179"
FT VAR_SEQ 185..225
FT /note="YAGFEIPNLFVVGYALDYNEYFRDLNHICVINEHGKEKYRV -> SHMRHQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031180"
FT CONFLICT 39
FT /note="L -> W (in Ref. 3; BAD93029)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="G -> R (in Ref. 3; BAD96394)"
FT /evidence="ECO:0000305"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2JBH"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:2JBH"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2JBH"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:2JBH"
FT HELIX 46..64
FT /evidence="ECO:0007829|PDB:2JBH"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:2JBH"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:2JBH"
FT HELIX 79..95
FT /evidence="ECO:0007829|PDB:2JBH"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:2JBH"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2JBH"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:2JBH"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:2JBH"
FT STRAND 135..147
FT /evidence="ECO:0007829|PDB:2JBH"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:2JBH"
FT STRAND 163..173
FT /evidence="ECO:0007829|PDB:2JBH"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:2JBH"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:2JBH"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:2JBH"
SQ SEQUENCE 225 AA; 25674 MW; CD612C2783AC3071 CRC64;
MAGSSEEAPD YGRGVVIMDD WPGYDLNLFT YPQHYYGDLE YVLIPHGIIV DRIERLAKDI
MKDIGYSDIM VLCVLKGGYK FCADLVEHLK NISRNSDRFV SMKVDFIRLK SYRNDQSMGE
MQIIGGDDLS TLAGKNVLIV EDVVGTGRTM KALLSNIEKY KPNMIKVASL LVKRTSRSDG
FRPDYAGFEI PNLFVVGYAL DYNEYFRDLN HICVINEHGK EKYRV
