HNRPL_RAT
ID HNRPL_RAT Reviewed; 623 AA.
AC F1LQ48; F1LPP9; Q5U1Y5;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein L;
DE Short=hnRNP L;
GN Name=Hnrnpl {ECO:0000312|RGD:71059}; Synonyms=Fblim1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:BAG72209.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH ELAVL1.
RC STRAIN=Wistar {ECO:0000312|EMBL:BAG72209.1};
RX PubMed=18161049; DOI=10.1002/hep.22036;
RA Matsui K., Nishizawa M., Ozaki T., Kimura T., Hashimoto I., Yamada M.,
RA Kaibori M., Kamiyama Y., Ito S., Okumura T.;
RT "Natural antisense transcript stabilizes inducible nitric oxide synthase
RT messenger RNA in rat hepatocytes.";
RL Hepatology 47:686-697(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary {ECO:0000312|EMBL:AAH86392.1};
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 [4] {ECO:0007744|PDB:2MQL, ECO:0007744|PDB:2MQM, ECO:0007744|PDB:2MQN, ECO:0007744|PDB:2MQO, ECO:0007744|PDB:2MQP, ECO:0007744|PDB:2MQQ}
RP STRUCTURE BY NMR OF 408-623, X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF
RP 31-245, DOMAIN, AND RNA-BINDING.
RX PubMed=26051023; DOI=10.1016/j.jmb.2015.05.020;
RA Blatter M., Dunin-Horkawicz S., Grishina I., Maris C., Thore S., Maier T.,
RA Bindereif A., Bujnicki J.M., Allain F.H.;
RT "The signature of the five-stranded vRRM fold defined by functional,
RT structural and computational analysis of the hnRNP L protein.";
RL J. Mol. Biol. 427:3001-3022(2015).
CC -!- FUNCTION: Splicing factor binding to exonic or intronic sites and
CC acting as either an activator or repressor of exon inclusion. Exhibits
CC a binding preference for CA-rich elements. Component of the
CC heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and
CC associated with most nascent transcripts. Associates, together with
CC APEX1, to the negative calcium responsive element (nCaRE) B2 of the
CC APEX2 promoter. As part of a ribonucleoprotein complex composed at
CC least of ZNF827, HNRNPK and the circular RNA circZNF827 that nucleates
CC the complex on chromatin, may negatively regulate the transcription of
CC genes involved in neuronal differentiation (By similarity).
CC {ECO:0000250|UniProtKB:P14866}.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with HNRNPLL. Interacts with
CC APEX1; the interaction is DNA-dependent. Component of a complex with
CC SETD2 (By similarity). Interacts with ELAVL1 (PubMed:18161049). Part of
CC a transcription inhibitory ribonucleoprotein complex composed at least
CC of the circular RNA circZNF827, ZNF827 and HNRNPK (By similarity).
CC {ECO:0000250|UniProtKB:P14866, ECO:0000269|PubMed:18161049}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P14866}. Cytoplasm
CC {ECO:0000269|PubMed:18161049}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. These granules are not
CC identical with P bodies or stress granules.
CC {ECO:0000250|UniProtKB:P14866}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F1LQ48-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F1LQ48-2; Sequence=VSP_058247;
CC -!- DOMAIN: RRM domain 2 has moderate RNA-binding affinity. RRM domains 3
CC and 4 may facilitate RNA looping when binding to two appropriately
CC separated binding sites within the same target pre-mRNA.
CC {ECO:0000250|UniProtKB:P14866}.
CC -!- PTM: Several isoelectric forms of the L protein are probably the
CC results of post-translational modifications.
CC {ECO:0000250|UniProtKB:P14866}.
CC -!- PTM: Phosphorylation at Ser-578 by CaMK4 enhances interaction with a
CC CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the
CC stress axis-regulated exon (STREX) of the KCNMA1 potassium channel
CC transcripts upon membrane depolarization.
CC {ECO:0000250|UniProtKB:P14866}.
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DR EMBL; AB260892; BAG72209.1; -; mRNA.
DR EMBL; AABR07002851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC086392; AAH86392.1; -; mRNA.
DR RefSeq; NP_001128232.1; NM_001134760.1. [F1LQ48-1]
DR PDB; 2MQL; NMR; -; A=86-190.
DR PDB; 2MQM; NMR; -; A=174-291.
DR PDB; 2MQN; NMR; -; A=408-623.
DR PDB; 2MQO; NMR; -; A=86-190.
DR PDB; 2MQP; NMR; -; A=174-291.
DR PDB; 2MQQ; NMR; -; A=409-623.
DR PDB; 4QPT; X-ray; 1.35 A; A=409-623.
DR PDBsum; 2MQL; -.
DR PDBsum; 2MQM; -.
DR PDBsum; 2MQN; -.
DR PDBsum; 2MQO; -.
DR PDBsum; 2MQP; -.
DR PDBsum; 2MQQ; -.
DR PDBsum; 4QPT; -.
DR AlphaFoldDB; F1LQ48; -.
DR SMR; F1LQ48; -.
DR IntAct; F1LQ48; 4.
DR MINT; F1LQ48; -.
DR STRING; 10116.ENSRNOP00000027425; -.
DR iPTMnet; F1LQ48; -.
DR PhosphoSitePlus; F1LQ48; -.
DR jPOST; F1LQ48; -.
DR PaxDb; F1LQ48; -.
DR PRIDE; F1LQ48; -.
DR GeneID; 80846; -.
DR KEGG; rno:80846; -.
DR UCSC; RGD:1359551; rat.
DR CTD; 3191; -.
DR RGD; 71059; Hnrnpl.
DR VEuPathDB; HostDB:ENSRNOG00000020235; -.
DR eggNOG; KOG1456; Eukaryota.
DR InParanoid; F1LQ48; -.
DR OMA; VYNAQYP; -.
DR OrthoDB; 1545178at2759; -.
DR TreeFam; TF354318; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:F1LQ48; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020235; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; F1LQ48; baseline and differential.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0045120; C:pronucleus; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0035770; C:ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1990715; F:mRNA CDS binding; IDA:RGD.
DR GO; GO:0097157; F:pre-mRNA intronic binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IDA:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IMP:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1902416; P:positive regulation of mRNA binding; IMP:RGD.
DR GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:1901652; P:response to peptide; IEP:RGD.
DR CDD; cd12780; RRM1_hnRNPL; 1.
DR CDD; cd12785; RRM2_hnRNPL; 1.
DR CDD; cd12699; RRM3_hnRNPL; 1.
DR CDD; cd12704; RRM4_hnRNPL; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR006536; HnRNP-L/PTB.
DR InterPro; IPR034816; hnRNP-L_RRM3.
DR InterPro; IPR035005; hnRNPL_RRM1.
DR InterPro; IPR035008; hnRNPL_RRM2.
DR InterPro; IPR034817; hnRNPL_RRM4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR021790; PTBP1-like_RRM2.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF11835; RRM_8; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR TIGRFAMs; TIGR01649; hnRNP-L_PTB; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribonucleoprotein; RNA-binding; Ubl conjugation.
FT CHAIN 1..623
FT /note="Heterogeneous nuclear ribonucleoprotein L"
FT /id="PRO_0000436064"
FT DOMAIN 99..173
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 190..267
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 416..490
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 498..586
FT /note="RRM 4"
FT /evidence="ECO:0000269|PubMed:26051023"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT MOD_RES 266
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT MOD_RES 388
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8R081"
FT MOD_RES 392
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8R081"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R081"
FT MOD_RES 578
FT /note="Phosphoserine; by CaMK4"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT CROSSLNK 59
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT CROSSLNK 62
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT CROSSLNK 602
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT VAR_SEQ 1..378
FT /note="Missing (in isoform 2)"
FT /id="VSP_058247"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:2MQL"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:2MQL"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2MQO"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:2MQL"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:2MQL"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:2MQL"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:2MQL"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:2MQL"
FT STRAND 159..170
FT /evidence="ECO:0007829|PDB:2MQL"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2MQO"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:2MQP"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:2MQM"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2MQO"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:2MQM"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:2MQM"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:2MQM"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:2MQM"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2MQM"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:2MQM"
FT HELIX 238..248
FT /evidence="ECO:0007829|PDB:2MQM"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:2MQM"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:2MQM"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:2MQM"
FT STRAND 276..284
FT /evidence="ECO:0007829|PDB:2MQM"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:2MQP"
FT STRAND 411..421
FT /evidence="ECO:0007829|PDB:4QPT"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:4QPT"
FT HELIX 430..437
FT /evidence="ECO:0007829|PDB:4QPT"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:4QPT"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:4QPT"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:4QPT"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:4QPT"
FT HELIX 463..473
FT /evidence="ECO:0007829|PDB:4QPT"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:2MQQ"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:4QPT"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:2MQQ"
FT STRAND 506..510
FT /evidence="ECO:0007829|PDB:4QPT"
FT HELIX 522..525
FT /evidence="ECO:0007829|PDB:4QPT"
FT STRAND 535..542
FT /evidence="ECO:0007829|PDB:4QPT"
FT HELIX 548..558
FT /evidence="ECO:0007829|PDB:4QPT"
FT STRAND 564..568
FT /evidence="ECO:0007829|PDB:4QPT"
FT STRAND 575..582
FT /evidence="ECO:0007829|PDB:4QPT"
FT HELIX 586..596
FT /evidence="ECO:0007829|PDB:4QPT"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:4QPT"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:4QPT"
SQ SEQUENCE 623 AA; 67903 MW; 0DEB312EC2B896AF CRC64;
MSRRLLPRAE KRRRRLEQRQ QPDEQLRRAG AMVKMAAAGG GGGGGRYYGG GNEGGRAPKR
LKTENAGDQH GGGGGGGSGA AGGGGGENYD DPHKTPASPV VHIRGLIDGV VEADLVEALQ
EFGPISYVVV MPKKRQALVE FEDVLGACNA VNYAADNQIY IAGHPAFVNY STSQKISRPG
DSDDSRSVNS VLLFTILNPI YSITTDVLYT ICNPCGPVQR IVIFRKNGVQ AMVEFDSVQS
AQRAKASLNG ADIYSGCCTL KIEYAKPTRL NVFKNDQDTW DYTNPNLSGQ GDPGSNPNKR
QRQPPLLGDH PAEYGEGRGF PSVDSRGSCA PARRPPRKFS PVLPLFPSHP PGGPHGGYHS
HYHDEGYGPP PPHYEGRRMG PPVGGHRRGP SRYGPQYGHP PPPPPPPDYG PHADSPVLMV
YGLDQSKMNC DRVFNVFCLY GNVEKVKFMK SKPGAAMVEM ADGYAVDRAI THLNNNFMFG
QKMNVCVSKQ PAIMPGQSYG LEDGSCSYKD FSESRNNRFS TPEQAAKNRI QHPSNVLHFF
NAPLEVTEEN FFEICDELGV KRPTSVKVFS GKSERSSSGL LEWDSKSDAL ETLGFLNHYQ
MKNPNGPYPY TLKLCFSTAQ HAS
