EGLN2_MOUSE
ID EGLN2_MOUSE Reviewed; 419 AA.
AC Q91YE2; Q8C6I4; Q8CIL9; Q8VHJ1; Q99MI0;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Prolyl hydroxylase EGLN2 {ECO:0000305};
DE EC=1.14.11.- {ECO:0000305|PubMed:24809345};
DE AltName: Full=Egl nine homolog 2 {ECO:0000305};
DE EC=1.14.11.29 {ECO:0000250|UniProtKB:Q96KS0, ECO:0000255|PROSITE-ProRule:PRU00805};
DE AltName: Full=Falkor {ECO:0000303|PubMed:12360397};
DE AltName: Full=Hypoxia-inducible factor prolyl hydroxylase 1;
DE Short=HIF-PH1;
DE Short=HIF-prolyl hydroxylase 1;
DE Short=HPH-1;
DE AltName: Full=Prolyl hydroxylase domain-containing protein 1 {ECO:0000303|PubMed:18176562};
DE Short=PHD1 {ECO:0000303|PubMed:18176562};
GN Name=Egln2 {ECO:0000312|MGI:MGI:1932287};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11574160; DOI=10.1016/s0378-1119(01)00633-3;
RA Taylor M.S.;
RT "Characterization and comparative analysis of the EGLN gene family.";
RL Gene 275:125-132(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6 X DBA/2;
RX PubMed=12234095; DOI=10.1139/o02-115;
RA Lieb M.E., Menzies K., Moschella M.C., Ni R., Taubman M.B.;
RT "Mammalian EGLN genes have distinct patterns of mRNA expression and
RT regulation.";
RL Biochem. Cell Biol. 80:421-426(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ;
RX PubMed=12360397; DOI=10.1038/sj.onc.1205867;
RA Erez N., Milyavsky M., Goldfinger N., Peles E., Gudkov A.V., Rotter V.;
RT "Falkor, a novel cell growth regulator isolated by a functional genetic
RT screen.";
RL Oncogene 21:6713-6721(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18176562; DOI=10.1038/ng.2007.62;
RA Aragones J., Schneider M., Van Geyte K., Fraisl P., Dresselaers T.,
RA Mazzone M., Dirkx R., Zacchigna S., Lemieux H., Jeoung N.H., Lambrechts D.,
RA Bishop T., Lafuste P., Diez-Juan A., Harten S.K., Van Noten P., De Bock K.,
RA Willam C., Tjwa M., Grosfeld A., Navet R., Moons L., Vandendriessche T.,
RA Deroose C., Wijeyekoon B., Nuyts J., Jordan B., Silasi-Mansat R., Lupu F.,
RA Dewerchin M., Pugh C., Salmon P., Mortelmans L., Gallez B., Gorus F.,
RA Buyse J., Sluse F., Harris R.A., Gnaiger E., Hespel P., Van Hecke P.,
RA Schuit F., Van Veldhoven P., Ratcliffe P., Baes M., Maxwell P.,
RA Carmeliet P.;
RT "Deficiency or inhibition of oxygen sensor Phd1 induces hypoxia tolerance
RT by reprogramming basal metabolism.";
RL Nat. Genet. 40:170-180(2008).
RN [7]
RP FUNCTION.
RX PubMed=19587290; DOI=10.1523/jneurosci.1779-09.2009;
RA Siddiq A., Aminova L.R., Troy C.M., Suh K., Messer Z., Semenza G.L.,
RA Ratan R.R.;
RT "Selective inhibition of hypoxia-inducible factor (HIF) prolyl-hydroxylase
RT 1 mediates neuroprotection against normoxic oxidative death via HIF- and
RT CREB-independent pathways.";
RL J. Neurosci. 29:8828-8838(2009).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21083501; DOI=10.1089/ars.2010.3769;
RA Adluri R.S., Thirunavukkarasu M., Dunna N.R., Zhan L., Oriowo B.,
RA Takeda K., Sanchez J.A., Otani H., Maulik G., Fong G.H., Maulik N.;
RT "Disruption of hypoxia-inducible transcription factor-prolyl hydroxylase
RT domain-1 (PHD-1-/-) attenuates ex vivo myocardial ischemia/reperfusion
RT injury through hypoxia-inducible factor-1alpha transcription factor and its
RT target genes in mice.";
RL Antioxid. Redox Signal. 15:1789-1797(2011).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND UBIQUITINATION.
RX PubMed=24809345; DOI=10.1371/journal.pgen.1004348;
RA Scortegagna M., Kim H., Li J.L., Yao H., Brill L.M., Han J., Lau E.,
RA Bowtell D., Haddad G., Kaufman R.J., Ronai Z.A.;
RT "Fine tuning of the UPR by the ubiquitin ligases Siah1/2.";
RL PLoS Genet. 10:e1004348-e1004348(2014).
CC -!- FUNCTION: Prolyl hydroxylase that mediates hydroxylation of proline
CC residues in target proteins, such as ATF4, IKBKB, CEP192 and HIF1A
CC (PubMed:24809345). Target proteins are preferentially recognized via a
CC LXXLAP motif (By similarity). Cellular oxygen sensor that catalyzes,
CC under normoxic conditions, the post-translational formation of 4-
CC hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins
CC (PubMed:18176562, PubMed:19587290, PubMed:21083501). Hydroxylates a
CC specific proline found in each of the oxygen-dependent degradation
CC (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A
CC (PubMed:18176562, PubMed:19587290, PubMed:21083501). Also hydroxylates
CC HIF2A (PubMed:18176562, PubMed:19587290, PubMed:21083501). Has a
CC preference for the CODD site for both HIF1A and HIF2A (PubMed:18176562,
CC PubMed:19587290, PubMed:21083501). Hydroxylated HIFs are then targeted
CC for proteasomal degradation via the von Hippel-Lindau ubiquitination
CC complex (PubMed:18176562, PubMed:19587290, PubMed:21083501). Under
CC hypoxic conditions, the hydroxylation reaction is attenuated allowing
CC HIFs to escape degradation resulting in their translocation to the
CC nucleus, heterodimerization with HIF1B, and increased expression of
CC hypoxy-inducible genes (PubMed:18176562, PubMed:19587290,
CC PubMed:21083501). EGLN2 is involved in regulating hypoxia tolerance and
CC apoptosis in cardiac and skeletal muscle (PubMed:18176562,
CC PubMed:19587290, PubMed:21083501). Also regulates susceptibility to
CC normoxic oxidative neuronal death (PubMed:18176562, PubMed:19587290,
CC PubMed:21083501). Links oxygen sensing to cell cycle and primary cilia
CC formation by hydroxylating the critical centrosome component CEP192
CC which promotes its ubiquitination and subsequent proteasomal
CC degradation (By similarity). Hydroxylates IKBKB, mediating NF-kappa-B
CC activation in hypoxic conditions (By similarity). Also mediates
CC hydroxylation of ATF4, leading to decreased protein stability of ATF4
CC (PubMed:24809345). {ECO:0000250|UniProtKB:Q96KS0,
CC ECO:0000269|PubMed:18176562, ECO:0000269|PubMed:19587290,
CC ECO:0000269|PubMed:21083501, ECO:0000269|PubMed:24809345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[protein] + O2 = CO2 + succinate +
CC trans-4-hydroxy-L-prolyl-[protein]; Xref=Rhea:RHEA:63484, Rhea:RHEA-
CC COMP:12408, Rhea:RHEA-COMP:16354, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:50342, ChEBI:CHEBI:61965;
CC Evidence={ECO:0000305|PubMed:24809345};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63485;
CC Evidence={ECO:0000305|PubMed:24809345};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[hypoxia-inducible factor alpha
CC subunit] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[hypoxia-
CC inducible factor alpha subunit]; Xref=Rhea:RHEA:48400, Rhea:RHEA-
CC COMP:12093, Rhea:RHEA-COMP:12094, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.29;
CC Evidence={ECO:0000250|UniProtKB:Q96KS0};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q96KS0,
CC ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q96KS0,
CC ECO:0000255|PROSITE-ProRule:PRU00805};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q96KS0};
CC -!- SUBUNIT: Interacts with E3 ligase SIAH2. Interacts with LIMD1, WTIP and
CC AJUBA. {ECO:0000250|UniProtKB:Q96KS0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12360397}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, expression was also
CC detected in the heart brain, liver kidney and lung. Expression was
CC lowest in spleen and skeletal muscle. Constitutively expressed during
CC differentiation of C2C12 skeletal myocytes.
CC {ECO:0000269|PubMed:12234095}.
CC -!- DOMAIN: The Beta(2)beta(3) 'finger-like' loop domain is important for
CC substrate (HIFs' CODD/NODD) selectivity.
CC {ECO:0000250|UniProtKB:Q9GZT9}.
CC -!- PTM: Ubiquitinated by SIAH1 and/or SIAH2 in response to the unfolded
CC protein response (UPR), leading to its degradation.
CC {ECO:0000269|PubMed:24809345}.
CC -!- DISRUPTION PHENOTYPE: Null mice exhibit a lowering of oxygen
CC consumption in skeletal muscle. Glucose oxidation is reduced to around
CC 35%. Hypoxia tolerance is induced in myofibers.
CC {ECO:0000269|PubMed:18176562, ECO:0000269|PubMed:21083501}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC42516.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ310547; CAC42516.1; ALT_FRAME; mRNA.
DR EMBL; AF453879; AAL65166.1; -; mRNA.
DR EMBL; AF340231; AAK37525.1; -; mRNA.
DR EMBL; AK075582; BAC35835.1; -; mRNA.
DR EMBL; BC023299; AAH23299.2; -; mRNA.
DR CCDS; CCDS21011.1; -.
DR RefSeq; NP_444438.2; NM_053208.4.
DR AlphaFoldDB; Q91YE2; -.
DR SMR; Q91YE2; -.
DR BioGRID; 227482; 3.
DR STRING; 10090.ENSMUSP00000078966; -.
DR iPTMnet; Q91YE2; -.
DR PhosphoSitePlus; Q91YE2; -.
DR MaxQB; Q91YE2; -.
DR PaxDb; Q91YE2; -.
DR PRIDE; Q91YE2; -.
DR ProteomicsDB; 277803; -.
DR Antibodypedia; 66726; 445 antibodies from 32 providers.
DR DNASU; 112406; -.
DR Ensembl; ENSMUST00000080058; ENSMUSP00000078966; ENSMUSG00000058709.
DR Ensembl; ENSMUST00000108382; ENSMUSP00000104019; ENSMUSG00000058709.
DR GeneID; 112406; -.
DR KEGG; mmu:112406; -.
DR UCSC; uc009fva.2; mouse.
DR CTD; 112398; -.
DR MGI; MGI:1932287; Egln2.
DR VEuPathDB; HostDB:ENSMUSG00000058709; -.
DR eggNOG; KOG3710; Eukaryota.
DR GeneTree; ENSGT00940000160655; -.
DR HOGENOM; CLU_063064_0_0_1; -.
DR InParanoid; Q91YE2; -.
DR OMA; WSIGALM; -.
DR OrthoDB; 1604981at2759; -.
DR PhylomeDB; Q91YE2; -.
DR TreeFam; TF314595; -.
DR BRENDA; 1.14.11.29; 3474.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR BioGRID-ORCS; 112406; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Egln2; mouse.
DR PRO; PR:Q91YE2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q91YE2; protein.
DR Bgee; ENSMUSG00000058709; Expressed in seminiferous tubule of testis and 259 other tissues.
DR ExpressionAtlas; Q91YE2; baseline and differential.
DR Genevisible; Q91YE2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0019826; F:oxygen sensor activity; ISS:UniProtKB.
DR GO; GO:0031545; F:peptidyl-proline 4-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IBA:GO_Central.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; ISS:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Vitamin C.
FT CHAIN 1..419
FT /note="Prolyl hydroxylase EGLN2"
FT /id="PRO_0000206665"
FT DOMAIN 290..388
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..247
FT /note="Beta(2)beta(3) 'finger-like' loop"
FT /evidence="ECO:0000250|UniProtKB:Q9GZT9"
FT MOTIF 89..134
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q96KS0"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 309
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q96KS0,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 311
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q96KS0,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 370
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q96KS0,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 379
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KS0"
FT CONFLICT 8
FT /note="Q -> H (in Ref. 4; BAC35835)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="L -> C (in Ref. 4; BAC35835)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="Q -> K (in Ref. 3; AAK37525)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 45109 MW; 13BAA52A0709CE98 CRC64;
MDSPCQPQAL NQALPQLPGS VSESLESSRA RMGVESYLPC PLLPAYHRPG ASGEASAGNG
TPRTTATATT TTASPLREGF GGQDGGELWP LQSEGAAALV TKECQRLAAQ GARPEAPKRK
WAKDGGDAPS PSKRPWARQE NQEAKGESGM GCDSGASNSS SSSSNTTSSS GEASARLREE
VQPSAPERLA LDYIVPCMRY YGICVKDNFL GAVLGGRVLA EVEALKWGGR LRDGQLVSQR
AIPPRSIRGD QIAWVEGHEP GCRSIGALMA HVDAVIRHCA GRLGNYVING RTKAMVACYP
GNGLGYVRHV DNPHGDGRCI TCIYYLNQNW DVKVHGGLLQ IFPEGRPVVA NIEPLFDRLL
IFWSDRRNPH EVKPAYATRY AITVWYFDAK ERAAARDKYQ LASGQKGVQV PVSQPTTPT
