FKRP_MOUSE
ID FKRP_MOUSE Reviewed; 494 AA.
AC Q8CG64; Q8BJR3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ribitol 5-phosphate transferase FKRP {ECO:0000305};
DE EC=2.7.8.- {ECO:0000269|PubMed:26923585};
DE AltName: Full=Fukutin-related protein {ECO:0000303|PubMed:12471058};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9H9S5};
DE AltName: Full=Ribitol-5-phosphate transferase {ECO:0000250|UniProtKB:Q9H9S5};
GN Name=Fkrp {ECO:0000312|MGI:MGI:2447586};
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP MUTAGENESIS OF 2-ARG--ARG-5; 362-ASP--ASP-364 AND PRO-448, AND POSSIBLE
RP FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=12471058; DOI=10.1093/hmg/11.26.3319;
RA Esapa C.T., Benson M.A., Schroeder J.E., Martin-Rendon E., Brockington M.,
RA Brown S.C., Muntoni F., Kroeger S., Blake D.J.;
RT "Functional requirements for fukutin-related protein in the Golgi
RT apparatus.";
RL Hum. Mol. Genet. 11:3319-3331(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-494.
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
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 [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH DGC COMPLEX.
RX PubMed=17452335; DOI=10.1074/jbc.c700061200;
RA Beedle A.M., Nienaber P.M., Campbell K.P.;
RT "Fukutin-related protein associates with the sarcolemmal dystrophin-
RT glycoprotein complex.";
RL J. Biol. Chem. 282:16713-16717(2007).
RN [5]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-276; VAL-405 AND PRO-448.
RX PubMed=17554798; DOI=10.1002/mus.20833;
RA Keramaris-Vrantsis E., Lu P.J., Doran T., Zillmer A., Ashar J., Esapa C.T.,
RA Benson M.A., Blake D.J., Rosenfeld J., Lu Q.L.;
RT "Fukutin-related protein localizes to the Golgi apparatus and mutations
RT lead to mislocalization in muscle in vivo.";
RL Muscle Nerve 36:455-465(2007).
RN [6]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-276; CYS-318 AND PRO-448.
RX PubMed=19900540; DOI=10.1016/j.bbadis.2009.10.016;
RA Lu P.J., Zillmer A., Wu X., Lochmuller H., Vachris J., Blake D., Chan Y.M.,
RA Lu Q.L.;
RT "Mutations alter secretion of fukutin-related protein.";
RL Biochim. Biophys. Acta 1802:253-258(2010).
RN [7]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-448.
RX PubMed=20675713; DOI=10.1093/hmg/ddq314;
RA Chan Y.M., Keramaris-Vrantsis E., Lidov H.G., Norton J.H., Zinchenko N.,
RA Gruber H.E., Thresher R., Blake D.J., Ashar J., Rosenfeld J., Lu Q.L.;
RT "Fukutin-related protein is essential for mouse muscle, brain and eye
RT development and mutation recapitulates the wide clinical spectrums of
RT dystroglycanopathies.";
RL Hum. Mol. Genet. 19:3995-4006(2010).
RN [8]
RP MUTAGENESIS OF LEU-276 AND PRO-448.
RX PubMed=23591631; DOI=10.1007/s00439-013-1302-7;
RA Blaeser A., Keramaris E., Chan Y.M., Sparks S., Cowley D., Xiao X.,
RA Lu Q.L.;
RT "Mouse models of fukutin-related protein mutations show a wide range of
RT disease phenotypes.";
RL Hum. Genet. 132:923-934(2013).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=26923585; DOI=10.1016/j.celrep.2016.02.017;
RA Kanagawa M., Kobayashi K., Tajiri M., Manya H., Kuga A., Yamaguchi Y.,
RA Akasaka-Manya K., Furukawa J.I., Mizuno M., Kawakami H., Shinohara Y.,
RA Wada Y., Endo T., Toda T.;
RT "Identification of a Post-translational Modification with Ribitol-Phosphate
RT and Its Defect in Muscular Dystrophy.";
RL Cell Rep. 14:2209-2223(2016).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29416295;
RA Haro C., Uribe M.L., Quereda C., Cruces J., Martin-Nieto J.;
RT "Expression in retinal neurons of fukutin and FKRP, the protein products of
RT two dystroglycanopathy-causative genes.";
RL Mol. Vis. 24:43-58(2018).
CC -!- FUNCTION: Catalyzes the transfer of CDP-ribitol to ribitol 5-phosphate
CC previously attached by FKTN/fukutin of to the phosphorylated O-mannosyl
CC trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-
CC (phosphate-6-)mannose), a carbohydrate structure present in alpha-
CC dystroglycan (DAG1) (PubMed:26923585). This constitutes the second step
CC in the formation of the ribose 5-phosphate tandem repeat which links
CC the phosphorylated O-mannosyl trisaccharide to the ligand binding
CC moiety composed of repeats of 3-xylosyl-alpha-1,3-glucuronic acid-beta-
CC 1 (PubMed:26923585). {ECO:0000269|PubMed:26923585}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-
CC 6-P-alpha-D-Man)]-Thr-[protein] + CDP-L-ribitol = 3-O-[Rib-ol-P-Rib-
CC ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-
CC Man)]-Thr-[protein] + CMP + H(+); Xref=Rhea:RHEA:39867, Rhea:RHEA-
CC COMP:15021, Rhea:RHEA-COMP:17480, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57608, ChEBI:CHEBI:60377, ChEBI:CHEBI:142403,
CC ChEBI:CHEBI:177331; Evidence={ECO:0000269|PubMed:26923585};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39868;
CC Evidence={ECO:0000269|PubMed:26923585};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:26923585}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Forms a complex
CC composed of FKRP, FKTN/fukutin, and RXYLT1/TMEM5 (By similarity).
CC Exists also as large multimeric protein complexes (By similarity). May
CC interact with the dystrophin-glycoprotein complex (DGC)
CC (PubMed:17452335). {ECO:0000250|UniProtKB:Q9H9S5,
CC ECO:0000269|PubMed:17452335}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12471058, ECO:0000269|PubMed:17554798,
CC ECO:0000269|PubMed:26923585}; Single-pass type II membrane protein
CC {ECO:0000305}. Secreted {ECO:0000269|PubMed:19900540}. Cell membrane,
CC sarcolemma {ECO:0000269|PubMed:17452335}. Rough endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9H9S5}. Cytoplasm
CC {ECO:0000269|PubMed:29416295}. Note=The N-terminal hydrophobic domain
CC is cleaved after translocation to the Golgi apparatus and the protein
CC is secreted (PubMed:19900540). Localization at the cell membrane may
CC require the presence of dystroglycan (PubMed:17452335). At the Golgi
CC apparatus localizes to the middle-to-trans-cisternae (PubMed:12471058,
CC PubMed:17554798). Detected in rough endoplasmic reticulum in myocytes
CC (By similarity). {ECO:0000250|UniProtKB:Q9H9S5,
CC ECO:0000269|PubMed:12471058, ECO:0000269|PubMed:17452335,
CC ECO:0000269|PubMed:17554798, ECO:0000269|PubMed:19900540}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina, specifically in the inner
CC segments of the photoreceptors, the outer plexiform layers, inner
CC nuclear layers, and ganglion cell layers (at protein level)
CC (PubMed:29416295). Expressed at highest levels in brain, lung, heart,
CC kidney and liver (PubMed:12471058). {ECO:0000269|PubMed:12471058,
CC ECO:0000269|PubMed:29416295}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality before 12.5 dpc.
CC {ECO:0000269|PubMed:20675713}.
CC -!- SIMILARITY: Belongs to the LicD transferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37963.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ511806; CAD54301.1; -; mRNA.
DR EMBL; BC053072; AAH53072.1; -; mRNA.
DR EMBL; AK080624; BAC37963.1; ALT_INIT; mRNA.
DR CCDS; CCDS20853.1; -.
DR RefSeq; NP_775606.1; NM_173430.2.
DR RefSeq; XP_006539991.1; XM_006539928.3.
DR RefSeq; XP_006539992.1; XM_006539929.3.
DR RefSeq; XP_006539993.1; XM_006539930.3.
DR RefSeq; XP_011248864.1; XM_011250562.1.
DR AlphaFoldDB; Q8CG64; -.
DR SMR; Q8CG64; -.
DR BioGRID; 232568; 1.
DR STRING; 10090.ENSMUSP00000059091; -.
DR GlyGen; Q8CG64; 2 sites.
DR PhosphoSitePlus; Q8CG64; -.
DR MaxQB; Q8CG64; -.
DR PaxDb; Q8CG64; -.
DR PRIDE; Q8CG64; -.
DR ProteomicsDB; 271771; -.
DR Antibodypedia; 57230; 256 antibodies from 26 providers.
DR DNASU; 243853; -.
DR Ensembl; ENSMUST00000061390; ENSMUSP00000059091; ENSMUSG00000048920.
DR GeneID; 243853; -.
DR KEGG; mmu:243853; -.
DR UCSC; uc009fic.1; mouse.
DR CTD; 79147; -.
DR MGI; MGI:2447586; Fkrp.
DR VEuPathDB; HostDB:ENSMUSG00000048920; -.
DR eggNOG; ENOG502QV4Y; Eukaryota.
DR GeneTree; ENSGT00390000017583; -.
DR HOGENOM; CLU_041755_1_0_1; -.
DR InParanoid; Q8CG64; -.
DR OMA; DNEGFYW; -.
DR OrthoDB; 1115738at2759; -.
DR PhylomeDB; Q8CG64; -.
DR TreeFam; TF324064; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 243853; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Fkrp; mouse.
DR PRO; PR:Q8CG64; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8CG64; protein.
DR Bgee; ENSMUSG00000048920; Expressed in knee joint and 215 other tissues.
DR ExpressionAtlas; Q8CG64; baseline and differential.
DR Genevisible; Q8CG64; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0002162; F:dystroglycan binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IDA:UniProtKB.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; IDA:MGI.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR GO; GO:0016485; P:protein processing; IDA:MGI.
DR GO; GO:0051262; P:protein tetramerization; ISO:MGI.
DR InterPro; IPR007074; LicD_fam.
DR Pfam; PF04991; LicD; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Magnesium; Membrane; Metal-binding;
KW Reference proteome; Secreted; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..494
FT /note="Ribitol 5-phosphate transferase FKRP"
FT /id="PRO_0000204724"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..494
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 289..318
FT /note="Zinc finger loop"
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT REGION 359..364
FT /note="CDP-L-ribitol"
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT REGION 437..438
FT /note="CDP-L-ribitol"
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT REGION 480..482
FT /note="CDP-L-ribitol"
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT BINDING 345
FT /ligand="CDP-L-ribitol"
FT /ligand_id="ChEBI:CHEBI:57608"
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT BINDING 352
FT /ligand="CDP-L-ribitol"
FT /ligand_id="ChEBI:CHEBI:57608"
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 6
FT /note="Interchain"
FT DISULFID 168..191
FT /evidence="ECO:0000250|UniProtKB:Q9H9S5"
FT MUTAGEN 2..5
FT /note="RLTR->ELTE: Localized to the perinuclear region but
FT not retained in or targeted to the medial part of the Golgi
FT apparatus."
FT /evidence="ECO:0000269|PubMed:12471058"
FT MUTAGEN 276
FT /note="L->I: Reduced secretion to the medium; localizes
FT mainly to the Golgi apparatus. Mild dystrophy with reduced
FT alpha-dystroglycan glycosylation and no apparent brain
FT defects."
FT /evidence="ECO:0000269|PubMed:17554798,
FT ECO:0000269|PubMed:19900540, ECO:0000269|PubMed:23591631"
FT MUTAGEN 318
FT /note="C->Y: Reduced secretion to the medium."
FT /evidence="ECO:0000269|PubMed:19900540"
FT MUTAGEN 362..364
FT /note="DVD->NNN: Does not alter dystroglycan processing in
FT vitro."
FT /evidence="ECO:0000269|PubMed:12471058"
FT MUTAGEN 405
FT /note="V->L: Localizes mainly to the ER compartment."
FT /evidence="ECO:0000269|PubMed:17554798"
FT MUTAGEN 448
FT /note="P->L: Not properly targeted to the Golgi apparatus;
FT strongly reduced secretion to the medium; localizes mainly
FT to the ER compartment. Strongly impaired glycosylation of
FT alpha-dystroglycan in muscles and brain."
FT /evidence="ECO:0000269|PubMed:12471058,
FT ECO:0000269|PubMed:17554798, ECO:0000269|PubMed:19900540,
FT ECO:0000269|PubMed:20675713, ECO:0000269|PubMed:23591631"
FT CONFLICT 243
FT /note="A -> E (in Ref. 3; BAC37963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 54852 MW; 470499DDEA7CB73F CRC64;
MRLTRCWAAL AAAIILNLLV FFYVSWLQHQ PRNSRARGPR RTSAIGPRVT VLIREFEAFD
NAVPELVDSF LQQDPAQPVV VAADTLPYPP LALPRIPNVR LALLQPALDR PAAASRPETY
VATEFVALVP DGARAESPGH LERMVEALRG SSARLVAAPV ATANPARCLA LNVSLREWTA
RYDPAPSAPR CDALDGDAVL LMRSRDLFNL SVPLARPLAT SLFLQTALRG WAVQLLDLTF
AAARQPPLAT AHARWKAERE GRSRRAALLR SLGIRLVSWE GGRLEWFGCS KESARCFGTV
AGDTPAYLYE GRWTPPCCLR ALRETARYVV GVLEAAGVRY WLEGGSLLGA ARHGDIIPWD
YDVDLGIYLE DVGNCEQLRG AEAGSVVDER GFVWEKAVEG DFFRVQYSEN NHLHVDLWPF
YPRNGVMTKD TWLDHRQDVE FPEHFLQPLV PLPFAGFMAQ APNNYRRFLE LKFGPGVIEN
PEYPNPALLS LTGG
