RAI1_MOUSE
ID RAI1_MOUSE Reviewed; 1889 AA.
AC Q61818; B1AU87; Q6ZPH7; Q8CEV1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Retinoic acid-induced protein 1;
GN Name=Rai1; Synonyms=Kiaa1820;
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] (ISOFORM 2), PROTEIN SEQUENCE OF 676-690,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7476016; DOI=10.1016/0169-328x(95)00020-s;
RA Imai Y., Suzuki Y., Matsui T., Tohyama M., Wanaka A., Takagi T.;
RT "Cloning of a retinoic acid-induced gene, GT1, in the embryonal carcinoma
RT cell line P19: neuron-specific expression in the mouse brain.";
RL Brain Res. Mol. Brain Res. 31:1-9(1995).
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 372-1889 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1706-1840 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15746153; DOI=10.1093/hmg/ddi085;
RA Bi W., Ohyama T., Nakamura H., Yan J., Visvanathan J., Justice M.J.,
RA Lupski J.R.;
RT "Inactivation of Rai1 in mice recapitulates phenotypes observed in
RT chromosome engineered mouse models for Smith-Magenis syndrome.";
RL Hum. Mol. Genet. 14:983-995(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-1105 AND SER-1343,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
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 [7]
RP FUNCTION.
RX PubMed=22578325; DOI=10.1016/j.ajhg.2012.04.013;
RA Williams S.R., Zies D., Mullegama S.V., Grotewiel M.S., Elsea S.H.;
RT "Smith-Magenis syndrome results in disruption of CLOCK gene transcription
RT and reveals an integral role for RAI1 in the maintenance of circadian
RT rhythmicity.";
RL Am. J. Hum. Genet. 90:941-949(2012).
CC -!- FUNCTION: Transcriptional regulator of the circadian clock components:
CC CLOCK, ARNTL/BMAL1, ARNTL2/BMAL2, PER1/3, CRY1/2, NR1D1/2 and RORA/C.
CC Positively regulates the transcriptional activity of CLOCK a core
CC component of the circadian clock. Regulates transcription through
CC chromatin remodeling by interacting with other proteins in chromatin as
CC well as proteins in the basic transcriptional machinery. May be
CC important for embryonic and postnatal development. May be involved in
CC neuronal differentiation. {ECO:0000269|PubMed:15746153,
CC ECO:0000269|PubMed:22578325}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In neurons, localized to
CC neurites.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61818-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61818-2; Sequence=VSP_011004, VSP_011005;
CC -!- TISSUE SPECIFICITY: Detected in all tissues examined with strong
CC expression in the thymus and brain. Expressed in epithelial cells
CC involved in organogenesis. No expression was seen in the corpus
CC callosum of the brain. {ECO:0000269|PubMed:7476016}.
CC -!- DISRUPTION PHENOTYPE: Haploinsufficiency cause obesity and craniofacial
CC abnormalities. Homozygous mice die during gastrulation and
CC organogenesis. The few surviving mice experienced postnatal growth
CC retardation and most of them died before weaning.
CC {ECO:0000269|PubMed:15746153}.
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DR EMBL; D29801; BAA06184.1; -; mRNA.
DR EMBL; AL669954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK129449; BAC98259.1; -; mRNA.
DR EMBL; AK013909; BAC25417.1; -; mRNA.
DR CCDS; CCDS24784.1; -. [Q61818-1]
DR PIR; T30250; T30250.
DR RefSeq; NP_001032853.1; NM_001037764.1. [Q61818-1]
DR RefSeq; NP_033047.2; NM_009021.2. [Q61818-1]
DR AlphaFoldDB; Q61818; -.
DR SMR; Q61818; -.
DR BioGRID; 202577; 4.
DR IntAct; Q61818; 2.
DR STRING; 10090.ENSMUSP00000070896; -.
DR iPTMnet; Q61818; -.
DR PhosphoSitePlus; Q61818; -.
DR CPTAC; non-CPTAC-4055; -.
DR EPD; Q61818; -.
DR jPOST; Q61818; -.
DR MaxQB; Q61818; -.
DR PaxDb; Q61818; -.
DR PRIDE; Q61818; -.
DR ProteomicsDB; 254895; -. [Q61818-1]
DR ProteomicsDB; 254896; -. [Q61818-2]
DR Antibodypedia; 25487; 93 antibodies from 16 providers.
DR DNASU; 19377; -.
DR Ensembl; ENSMUST00000064190; ENSMUSP00000070896; ENSMUSG00000062115. [Q61818-1]
DR Ensembl; ENSMUST00000090806; ENSMUSP00000088315; ENSMUSG00000062115. [Q61818-2]
DR Ensembl; ENSMUST00000102688; ENSMUSP00000099749; ENSMUSG00000062115. [Q61818-1]
DR Ensembl; ENSMUST00000171108; ENSMUSP00000126183; ENSMUSG00000062115. [Q61818-1]
DR GeneID; 19377; -.
DR KEGG; mmu:19377; -.
DR UCSC; uc007jfk.1; mouse. [Q61818-1]
DR UCSC; uc007jfl.1; mouse. [Q61818-2]
DR CTD; 10743; -.
DR MGI; MGI:103291; Rai1.
DR VEuPathDB; HostDB:ENSMUSG00000062115; -.
DR eggNOG; KOG1084; Eukaryota.
DR GeneTree; ENSGT00940000156922; -.
DR HOGENOM; CLU_002579_1_0_1; -.
DR InParanoid; Q61818; -.
DR OMA; CCAAADF; -.
DR PhylomeDB; Q61818; -.
DR TreeFam; TF331317; -.
DR BioGRID-ORCS; 19377; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Rai1; mouse.
DR PRO; PR:Q61818; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61818; protein.
DR Bgee; ENSMUSG00000062115; Expressed in lateral septal nucleus and 251 other tissues.
DR ExpressionAtlas; Q61818; baseline and differential.
DR Genevisible; Q61818; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00249; PHD; 1.
DR PROSITE; PS51805; EPHD; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Biological rhythms; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1889
FT /note="Retinoic acid-induced protein 1"
FT /id="PRO_0000097160"
FT ZN_FING 1762..1817
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 1837..1885
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1583..1614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1143..1160
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1206..1223
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 13..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1273
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT MOD_RES 455
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 679
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT MOD_RES 1047
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT MOD_RES 1051
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT MOD_RES 1343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT CROSSLNK 794
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT CROSSLNK 802
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT CROSSLNK 884
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT CROSSLNK 884
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT CROSSLNK 1394
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5J4"
FT VAR_SEQ 1838..1840
FT /note="PCT -> VRG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7476016"
FT /id="VSP_011004"
FT VAR_SEQ 1841..1889
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7476016"
FT /id="VSP_011005"
FT CONFLICT 412..413
FT /note="DL -> EV (in Ref. 1; BAA06184)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="N -> D (in Ref. 1; BAA06184 and 3; BAC98259)"
FT /evidence="ECO:0000305"
FT CONFLICT 1170
FT /note="Y -> F (in Ref. 1; BAA06184 and 3; BAC98259)"
FT /evidence="ECO:0000305"
FT CONFLICT 1183
FT /note="N -> S (in Ref. 1; BAA06184 and 3; BAC98259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1889 AA; 201571 MW; 54F51C4CC901189E CRC64;
MQSFRERCGF HGKQQNYPQT SQETSRLENY RQPGQAGLSC DRQRLLAKDY YSPQPYTGYE
GGTGTPSGTV ATAAADKYHR GSKSLQGRPA FPSYVQDSSP YPGRYSGEEG LQTWGGPQPP
PPQPQPLPGA VSKYEENLMK KTVVPPPNRQ YPEQGPQLPF RTHSLHVPPP QPQQPLAYPK
LQRQKPQNDL ASPLPFPQGS HFPQHSQSFP TSSTYAPTVQ GGGQGAHSYK SCTAPSAQPH
DRPMSANANL APGQRVQNLH AYQPGRLGYE QQQQALQGRH HTQETLHYQN LAKYQHYGQQ
GQGYCPPDTA VRTPEQYYQT FSPSSSHSPA RSVGRSPSYS STPSPLMPNL ENFPYSQQPL
STGAFPTGIT DHSHFMPLLN PSPTDAASSV DPQAGNCKPL QKEKLPDNLL SDLSLQSLTA
LTSQVENISN TVQQLLLSKA TMPQKKGVKN LVSRTPEQHK SQHCSPEGSG YSAEPAGTPL
SEPPSSTPQS THAEPQDTDY LSGSEDPLER SFLYCSQARG SPARVNSNSK AKPESVSTCS
VTSPDDMSTK SDDSFQSLHS TLPLDSFSKF VAGERDCPRL LLSALAQEDL ASEILGLQEA
IVEKADKAWA EASSLPKDNG KPPFSLENHG ACLDTVAKTS WSQPGEPETL PEPLQLDKGG
STKDFSPGLF EDPSVAFATT DPKKTSSPLS FGTKPLLGTA TPDPTTAAFD CFPDTPTASS
VDGANPFAWP EENLGDACPR WGLHPGELTK GLEQGAKASD GVGKADAHEA SACMGFQEDH
AIGKPAAALS GDFKQQEAEG VKEEVGGLLQ CPEVAKANQW LEESRHCCSS TDFGDLPLLP
PPGRKEDLEA EEEYSSLCEL LGSPEQRPSL QDPLSPKAPL MCTKEEAEEA LDTKAGWVSP
CHLSGEPAVL LGPSVGAQSK VQSWFESSLS HMKPGEEGPE MERAPGSSGT SQGSLAPKPN
KPAVPEGPIA KKEPVPRGKS LRSRRVHRGL PEAEDSPCRV PALPKDLLLP ESCTGPPQGQ
AEGAGAPGRG LSEGLPRMCT RSLTALSEPQ TPGPPGLTTT PTPPDKLGGK QRAAFKSGKR
VGKPSPKAAS SPSNPAALPV ASDSSPMGSK TKEPDSPSMP GKDQRSMVLR SRTKPQQVFH
AKRRRPSESR IPDCRATKKL PANNHLPTAY KVSSGPQKEG RMNQRVKVPK PGTGNKLSDR
PLHTLKRKSA FMAPVPAKKR SLILRSNNGS GGDGREERAE SSPGLLRRMA SPQRARPRGS
GEPPPPPPLE PPAACMGLST QSSLPSAVRT KVLPPRKGRG LKLEAIVQKI TSPGLKKLAC
RVAGAPPGTP RSPALPERRP GGSPAGAEEG LGGMGQMLPA ASGADPLCRN PASRSLKGKL
LNSKKLSSAA DCPKAEAFMS PETLPSLGTA RAPKKRSRKG RTGTLGPSKG PLEKRPCPGQ
PLLLAPHDRA SSTQGGGEDN SSGGGKKPKT EELGPASQPP EGRPCQPQTR AQKQPGQASY
SSYSKRKRLS RGRGKTAHAS PCKGRATRRR QQQVLPLDPA EPEIRLKYIS SCKRLRADSR
TPAFSPFVRV EKRDAYTTIC TVVNSPGDEP KPHWKPSSSA ASSSTSSSSL EPAGASLTTF
PGGSVLQQRP SLPLSSTMHL GPVVSKALST SCLVCCLCQN PANFKDLGDL CGPYYPEHCL
PKKKPKLKEK ARLEGTLEEA SLPLERTLKG LECSASTTAA APTTATITTP TALGRLSRPD
GPADPAKQGP LRTSARGLSR RLQSCYCCDG QGDGGEEVAQ ADKSRKHECS KEAPTEPGGD
TQEHWVHEAC AVWTSGVYLV AGKLFGLQEA MKVAVDMPCT SCHEPGATIS CSYKGCIHTY
HYPCANDTGC TFIEENFTLK CPKHKRLPL
