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 24-JAN-2024, entry version 86. 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). Regulates CC alternative splicing of a core group of genes involved in neuronal CC differentiation, likely by mediating H3K36me3-coupled transcription CC elongation and co-transcriptional RNA processing via interaction with CC CHD8. {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 Interacts with CHD8 in an RNA-dependent manner. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10116-ENSRNOP00000027425; -. DR GeneID; 80846; -. DR KEGG; rno:80846; -. DR UCSC; RGD:1359551; rat. DR AGR; RGD:1359551; -. DR AGR; RGD:71059; -. DR CTD; 3191; -. DR RGD; 71059; Hnrnpl. DR VEuPathDB; HostDB:ENSRNOG00000020235; -. DR eggNOG; KOG1456; Eukaryota. DR InParanoid; F1LQ48; -. DR OrthoDB; 4825346at2759; -. DR TreeFam; TF354318; -. DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway. DR Reactome; R-RNO-72203; Processing of Capped Intron-Containing Pre-mRNA. DR PRO; PR:F1LQ48; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000020235; Expressed in thymus and 19 other cell types or tissues. DR ExpressionAtlas; F1LQ48; baseline and differential. DR GO; GO:0000785; C:chromatin; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISO: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:0045202; C:synapse; ISO:RGD. 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:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; 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 NCBIfam; TIGR01649; hnRNP-L_PTB; 2. DR PANTHER; PTHR15592:SF20; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN L; 1. DR PANTHER; PTHR15592; MATRIN 3/NUCLEAR PROTEIN 220-RELATED; 1. DR Pfam; PF00076; RRM_1; 1. DR Pfam; PF13893; RRM_5; 1. DR Pfam; PF11835; RRM_8; 1. DR SMART; SM00360; RRM; 3. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 3. 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 //