VIR_MOUSE
ID VIR_MOUSE Reviewed; 1811 AA.
AC A2AIV2; A2AIV1; Q3TDQ3; Q3TRR9; Q3U1Z2; Q80TD6; Q8C758; Q8K151; Q9CSI3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Protein virilizer homolog {ECO:0000305};
GN Name=Virma {ECO:0000312|MGI:MGI:1913435};
GN Synonyms=Kiaa1429 {ECO:0000303|PubMed:12693553};
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 [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1210 AND 1737-1811 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung, and Urinary bladder;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1811 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1421-1811 (ISOFORM 1).
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1578, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-173, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-1578, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1722; ARG-1740; ARG-1772;
RP ARG-1774 AND ARG-1792, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [9]
RP IDENTIFICATION IN THE WMM COMPLEX.
RX PubMed=29535189; DOI=10.1101/gad.309146.117;
RA Knuckles P., Lence T., Haussmann I.U., Jacob D., Kreim N., Carl S.H.,
RA Masiello I., Hares T., Villasenor R., Hess D., Andrade-Navarro M.A.,
RA Biggiogera M., Helm M., Soller M., Buehler M., Roignant J.Y.;
RT "Zc3h13/Flacc is required for adenosine methylation by bridging the mRNA-
RT binding factor Rbm15/Spenito to the m6A machinery component Wtap/Fl(2)d.";
RL Genes Dev. 32:415-429(2018).
RN [10]
RP IDENTIFICATION IN THE WMM COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=29547716; DOI=10.1016/j.molcel.2018.02.015;
RA Wen J., Lv R., Ma H., Shen H., He C., Wang J., Jiao F., Liu H., Yang P.,
RA Tan L., Lan F., Shi Y.G., He C., Shi Y., Diao J.;
RT "Zc3h13 regulates nuclear RNA m6A methylation and mouse embryonic stem cell
RT self-renewal.";
RL Mol. Cell 69:1028-1038(2018).
CC -!- FUNCTION: Associated component of the WMM complex, a complex that
CC mediates N6-methyladenosine (m6A) methylation of RNAs, a modification
CC that plays a role in the efficiency of mRNA splicing and RNA
CC processing. Acts as a key regulator of m6A methylation by promoting m6A
CC methylation of mRNAs in the 3'-UTR near the stop codon: recruits the
CC catalytic core components METTL3 and METTL14, thereby guiding m6A
CC methylation at specific sites. Required for mRNA polyadenylation via
CC its role in selective m6A methylation: m6A methylation of mRNAs in the
CC 3'-UTR near the stop codon correlating with alternative polyadenylation
CC (APA). {ECO:0000250|UniProtKB:Q69YN4}.
CC -!- SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex
CC composed of a catalytic subcomplex, named MAC, and of an associated
CC subcomplex, named MACOM (PubMed:29535189, PubMed:29547716). The MAC
CC subcomplex is composed of METTL3 and METTL14 (PubMed:29535189,
CC PubMed:29547716). The MACOM subcomplex is composed of WTAP, ZC3H13,
CC CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B)
CC (PubMed:29535189, PubMed:29547716). Interacts with WTAP (By
CC similarity). Also a component of a MACOM-like complex, named WTAP
CC complex, composed of WTAP, ZC3H13, CBLL1, VIRMA, RBM15, BCLAF1 and
CC THRAP3 (By similarity). Interacts with NUDT21 and CPSF6 (By
CC similarity). {ECO:0000250|UniProtKB:Q69YN4,
CC ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29547716}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q69YN4}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:29547716}. Cytoplasm
CC {ECO:0000269|PubMed:29547716}. Note=Mainly nuclear with some fraction
CC located in the cytoplasm (PubMed:29547716). ZC3H13 is required to
CC anchor component of the MACOM subcomplex, such as VIRMA, in the nucleus
CC (PubMed:29547716). {ECO:0000269|PubMed:29547716}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AIV2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AIV2-2; Sequence=VSP_029022, VSP_029023;
CC -!- SIMILARITY: Belongs to the vir family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH28830.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK012768; BAB28456.1; -; mRNA.
DR EMBL; AK052499; BAC35017.2; -; mRNA.
DR EMBL; AK155623; BAE33351.1; -; mRNA.
DR EMBL; AK162531; BAE36958.1; -; mRNA.
DR EMBL; AK170075; BAE41548.1; -; mRNA.
DR EMBL; AL732538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL772170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122509; BAC65791.1; -; mRNA.
DR EMBL; BC028830; AAH28830.1; ALT_INIT; mRNA.
DR CCDS; CCDS84705.1; -. [A2AIV2-1]
DR RefSeq; NP_001333984.1; NM_001347055.1. [A2AIV2-1]
DR AlphaFoldDB; A2AIV2; -.
DR BioGRID; 211281; 26.
DR ComplexPortal; CPX-1609; WMM N6-adenosine-methyltransferase complex.
DR IntAct; A2AIV2; 2.
DR STRING; 10090.ENSMUSP00000103943; -.
DR iPTMnet; A2AIV2; -.
DR PhosphoSitePlus; A2AIV2; -.
DR EPD; A2AIV2; -.
DR jPOST; A2AIV2; -.
DR MaxQB; A2AIV2; -.
DR PaxDb; A2AIV2; -.
DR PeptideAtlas; A2AIV2; -.
DR PRIDE; A2AIV2; -.
DR ProteomicsDB; 297600; -. [A2AIV2-1]
DR ProteomicsDB; 297601; -. [A2AIV2-2]
DR Antibodypedia; 25815; 52 antibodies from 16 providers.
DR Ensembl; ENSMUST00000055372; ENSMUSP00000063188; ENSMUSG00000040720. [A2AIV2-2]
DR Ensembl; ENSMUST00000059914; ENSMUSP00000058078; ENSMUSG00000040720. [A2AIV2-1]
DR GeneID; 66185; -.
DR KEGG; mmu:66185; -.
DR UCSC; uc008rzo.1; mouse. [A2AIV2-2]
DR UCSC; uc008rzq.1; mouse. [A2AIV2-1]
DR CTD; 25962; -.
DR MGI; MGI:1913435; Virma.
DR VEuPathDB; HostDB:ENSMUSG00000040720; -.
DR eggNOG; KOG4822; Eukaryota.
DR GeneTree; ENSGT00390000002833; -.
DR HOGENOM; CLU_254686_0_0_1; -.
DR InParanoid; A2AIV2; -.
DR OMA; CERKQIP; -.
DR PhylomeDB; A2AIV2; -.
DR BioGRID-ORCS; 66185; 27 hits in 74 CRISPR screens.
DR ChiTaRS; 1110037F02Rik; mouse.
DR PRO; PR:A2AIV2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AIV2; protein.
DR Bgee; ENSMUSG00000040720; Expressed in humerus cartilage element and 257 other tissues.
DR ExpressionAtlas; A2AIV2; baseline and differential.
DR Genevisible; A2AIV2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0110104; P:mRNA alternative polyadenylation; ISS:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR031801; VIR_N.
DR InterPro; IPR026736; Virilizer.
DR PANTHER; PTHR23185; PTHR23185; 1.
DR Pfam; PF15912; VIR_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Developmental protein;
KW Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q69YN4"
FT CHAIN 2..1811
FT /note="Protein virilizer homolog"
FT /id="PRO_0000308606"
FT REGION 132..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1615..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1662..1811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..302
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1717..1746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1778..1793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q69YN4"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YN4"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 184
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q69YN4"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69YN4"
FT MOD_RES 913
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q69YN4"
FT MOD_RES 1578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1707
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q69YN4"
FT MOD_RES 1722
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1740
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1740
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1772
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1774
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1792
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1131..1139
FT /note="IEPHDISVA -> PLHITCILS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029022"
FT VAR_SEQ 1140..1811
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029023"
FT CONFLICT 97
FT /note="S -> Y (in Ref. 1; BAE41548)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="K -> E (in Ref. 1; BAC35017)"
FT /evidence="ECO:0000305"
FT CONFLICT 1520
FT /note="A -> T (in Ref. 4; AAH28830)"
FT /evidence="ECO:0000305"
FT CONFLICT 1582
FT /note="S -> T (in Ref. 4; AAH28830)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1811 AA; 201439 MW; 5F505FADEC3211E3 CRC64;
MAVDSSMELL FLDTFKHPSA EQSSHIDVVR FPCVVYINEV RVIPPGVRAH SGLPDNRAYG
ETSPHTFQLD LFFNNVSKPS APVFDRLGSL EYDENTSIIF RPNSKVNTDG LVLRGWYNCL
TLAIYGSVDR VISHDRDSPP PPPPPPPPPQ PQPTLKRNLK HADGEKEDQF NGSPPRPQPR
GPRTPPGPPP PDDDEDDPMS LPVSGDKEED VPHREDYFEP ISPDRNSVPQ EGQYSDEGEV
EEEPQEEGED DEDDVDVEEE EDEDEDDCHT VDSIPDDEEE DEEEEGEEDE EGEGDDGYEQ
ISSDEDGIAD LERETFKYPN FDVEYTPEDL ASVPPMTYDP YDRELAPLLY FSCPYKTTFE
IEISRMKDQG PDKENSGAVE ASVKLTELLD LYQEDRGAKW VTALEEIPSL IIKGLSYLQL
KNTEQDSLGQ LVDWTMQALN LQVAFRQPIA LNVRQLKAGT KLVTSLAECG APGVTELLQA
GVINVLFDLL FADHVSSSLK LNAFKALDSV ISMTEGMEAF LRSTQNEKSG YQRLLELILL
DQTVRVVTAG SAILQKCHFY EILSEIKRLG DHIAEKTSAV PNHSEPDQDT DAVLERANPD
YENEVEASMD MDLLESSIIS EGEIEKLTNL LEEVFHVMET APHTMTQPPV KSFPTIARIT
GPPERDDPYP VLFRYLHSHH FLELVTLLLS IPITSAHQGV LQATKDVLKF LAQSQKGLLF
FMSEYEATNL LIRALCHLYD QDEEEGLQSD GADDAFALWL QDSTQTLQCI TELFSHFQRC
TASEETDHSD LLGTLHNLYL ITFNPVGRSA VGHVFSLDKN LQSLITLMEY YSKEALGDSK
SKKSVAYNYA CVLTLVVAQS SSGVQMLEQH AASLLKLCKA DENNAKLQEL GKWLEPLKNL
RFEINCIPNL IEYVKQNIDN LMTAEGVGLT TALRVLCNVA CPPPPVEGQQ KDLKWNLAVI
QLFSAEGMDT FIRVLQKLNS ILTQPWRLHV NMGTTLHRVT TISMARCTLT LLKTMLTELL
RGGSFEFKDM RVPSALVTLH MLLCSIPLSG RLDSDEQKIQ NDIIDILLTF TQGVNEKLTI
SEETLANNTW SLMLKEVLSS ILKVPEGFFS GLILLSELLP LPLPMQTTQV IEPHDISVAL
NTRKLWSMHL HVQAKLLQEI VRSFSGTTCQ PIQHMLRRIC VQLCDLASPT ALLIMRTVLD
LIVEDLQSTS EDKEKQYTSQ TTRLLALLDA LASHKACKLA ILHLINGTIK GDERYAEIFQ
DLLALVRSPG DSVTRQQCVE YVTSILQSLC DQDIALILPS PSEGPASELE QLSNSLPSKE
LMTAICDCLL ATLANSESSY NCLLTCVRTM MFLAEHDYGL FHLKSSLRKN SSALHSLLKR
VVSTFSKDTG ELASASLDFM RQILNADAMG CCGDDSGLME VEGAHPPRTM SLNAAELKQL
LQSKEESPES LFLELEKLVL EHSKDDDSLE SLLDNVIGLK QMLESSGEPL PLSDQDVEPV
LSAPESLQNL FNNRTAYVLA DVMDDQLKSM WFTPFQAEEI DTDLDLVKVD LIELSEKCCS
DFDLHSELER SFLSEPSSPG RSKTTKGFKL GKHKHETFIT SSGKSEYIEP AKRAHVVPPP
RGRGRGGFGQ GIRPHDIFRQ RKQNTSRPPS MHVDDFVAAE SKEVVPQDGI PPPKRPLKVS
QKISSRGGFS GNRGGRGAFH SQNRFFTPPA SKGNYSRREG TRGSSWSAQN TPRGNYNESR
GGQSNFNRGP LPPLRPLSST GYRPSPRDRA SRGRGGLGPS WASTNSGSGG SRGKFVSGGS
GRGRHVRSFT R
