ID U2AF2_HUMAN Reviewed; 475 AA. AC P26368; Q96HC5; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 19-FEB-2014, entry version 161. DE RecName: Full=Splicing factor U2AF 65 kDa subunit; DE AltName: Full=U2 auxiliary factor 65 kDa subunit; DE Short=hU2AF(65); DE Short=hU2AF65; DE AltName: Full=U2 snRNP auxiliary factor large subunit; GN Name=U2AF2; Synonyms=U2AF65; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1538748; DOI=10.1038/355609a0; RA Zamore P.D., Patton J.G., Green M.R.; RT "Cloning and domain structure of the mammalian splicing factor U2AF."; RL Nature 355:609-614(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Lymph, and Skin; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 2-9; 196-203; 277-286 AND 463-471, CLEAVAGE OF RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY. RC TISSUE=Colon carcinoma; RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.; RL Submitted (NOV-2006) to UniProtKB. RN [5] RP PROTEIN SEQUENCE OF 261-286, MASS SPECTROMETRY, AND INTERACTION WITH RP THE SPLICEOSOME. RX PubMed=12176931; DOI=10.1101/gr.473902; RA Rappsilber J., Ryder U., Lamond A.I., Mann M.; RT "Large-scale proteomic analysis of the human spliceosome."; RL Genome Res. 12:1231-1245(2002). RN [6] RP INTERACTION WITH ZRSR2. RX PubMed=9237760; DOI=10.1038/41137; RA Tronchere H., Wang J., Fu X.D.; RT "A protein related to splicing factor U2AF35 that interacts with RT U2AF65 and SR proteins in splicing of pre-mRNA."; RL Nature 388:397-400(1997). RN [7] RP INTERACTION WITH SCAF11. RX PubMed=9447963; RA Zhang W.-J., Wu J.Y.; RT "Sip1, a novel RS domain-containing protein essential for pre-mRNA RT splicing."; RL Mol. Cell. Biol. 18:676-684(1998). RN [8] RP INTERACTION WITH SF1. RX PubMed=10449420; DOI=10.1093/emboj/18.16.4549; RA Wang X., Bruderer S., Rafi Z., Xue J., Milburn P.J., Kraemer A., RA Robinson P.J.; RT "Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent RT protein kinase regulates spliceosome assembly."; RL EMBO J. 18:4549-4559(1999). RN [9] RP FUNCTION. RX PubMed=15009664; DOI=10.1046/j.1471-4159.2003.02232.x; RA Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.; RT "Tau exon 10, whose missplicing causes frontotemporal dementia, is RT regulated by an intricate interplay of cis elements and trans RT factors."; RL J. Neurochem. 88:1078-1090(2004). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP FUNCTION, AND RNA-BINDING. RX PubMed=19470458; DOI=10.1073/pnas.0900342106; RA Warf M.B., Diegel J.V., von Hippel P.H., Berglund J.A.; RT "The protein factors MBNL1 and U2AF65 bind alternative RNA structures RT to regulate splicing."; RL Proc. Natl. Acad. Sci. U.S.A. 106:9203-9208(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [16] RP FUNCTION, AND HYDROXYLATION AT LYS-15 AND LYS-276. RX PubMed=19574390; DOI=10.1126/science.1175865; RA Webby C.J., Wolf A., Gromak N., Dreger M., Kramer H., Kessler B., RA Nielsen M.L., Schmitz C., Butler D.S., Yates J.R. III, Delahunty C.M., RA Hahn P., Lengeling A., Mann M., Proudfoot N.J., Schofield C.J., RA Boettger A.; RT "Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated RT with RNA splicing."; RL Science 325:90-93(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-2 AND SER-79, AND MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP INTERACTION WITH SNW1. RX PubMed=21460037; DOI=10.1101/gad.2002611; RA Chen Y., Zhang L., Jones K.A.; RT "SKIP counteracts p53-mediated apoptosis via selective regulation of RT p21Cip1 mRNA splicing."; RL Genes Dev. 25:701-716(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS RP SPECTROMETRY. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [22] RP STRUCTURE BY NMR OF 148-237. RX PubMed=10449418; DOI=10.1093/emboj/18.16.4523; RA Ito T., Muto Y., Green M.R., Yokoyama S.; RT "Solution structures of the first and second RNA-binding domains of RT human U2 small nuclear ribonucleoprotein particle auxiliary factor RT (U2AF(65))."; RL EMBO J. 18:4523-4534(1999). RN [23] RP STRUCTURE BY NMR OF 372-475 IN COMPLEX WITH SF1, AND MUTAGENESIS OF RP 387-GLU-GLU-388; 391-ASP--GLU-393; 396-GLU-GLU-397 AND PHE-454. RX PubMed=12718882; DOI=10.1016/S1097-2765(03)00115-1; RA Selenko P., Gregorovic G., Sprangers R., Stier G., Rhani Z., RA Kraemer A., Sattler M.; RT "Structural basis for the molecular recognition between human splicing RT factors U2AF65 and SF1/mBBP."; RL Mol. Cell 11:965-976(2003). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 90-112 IN COMPLEX WITH U2AF1, RP AND MUTAGENESIS OF TRP-92; PRO-96 AND PRO-104. RX PubMed=11551507; DOI=10.1016/S0092-8674(01)00480-9; RA Kielkopf C.L., Rodionova N.A., Green M.R., Burley S.K.; RT "A novel peptide recognition mode revealed by the X-ray structure of a RT core U2AF35/U2AF65 heterodimer."; RL Cell 106:595-605(2001). CC -!- FUNCTION: Necessary for the splicing of pre-mRNA. Induces cardiac CC troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates CC the TNNT2 exon 5 inclusion through competition with MBNL1. Binds CC preferentially to a single-stranded structure within the CC polypyrimidine tract of TNNT2 intron 4 during spliceosome CC assembly. Required for the export of mRNA out of the nucleus, even CC if the mRNA is encoded by an intron-less gene. Represses the CC splicing of MAPT/Tau exon 10. CC -!- SUBUNIT: Interacts with U2AF1L4 (By similarity). Heterodimer with CC U2AF1. Binds unphosphorylated SF1. Interacts with SCAF11 and SNW1. CC Interacts with ZRSR2/U2AF1-RS2. CC -!- INTERACTION: CC P54253:ATXN1; NbExp=4; IntAct=EBI-742339, EBI-930964; CC Q8IWX8:CHERP; NbExp=2; IntAct=EBI-742339, EBI-2555370; CC Q8N684:CPSF7; NbExp=2; IntAct=EBI-742339, EBI-746909; CC P15941:MUC1; NbExp=2; IntAct=EBI-742339, EBI-2804728; CC O43395:PRPF3; NbExp=2; IntAct=EBI-742339, EBI-744322; CC P98175:RBM10; NbExp=2; IntAct=EBI-742339, EBI-721525; CC P52756:RBM5; NbExp=2; IntAct=EBI-742339, EBI-714003; CC P09012:SNRPA; NbExp=2; IntAct=EBI-742339, EBI-607085; CC Q13573:SNW1; NbExp=5; IntAct=EBI-742339, EBI-632715; CC P78362:SRPK2; NbExp=4; IntAct=EBI-742339, EBI-593303; CC Q8IWZ8:SUGP1; NbExp=3; IntAct=EBI-742339, EBI-2691671; CC Q01081:U2AF1; NbExp=8; IntAct=EBI-742339, EBI-632461; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P26368-1; Sequence=Displayed; CC Name=2; CC IsoId=P26368-2; Sequence=VSP_035414; CC -!- PTM: Lysyl-hydroxylation at Lys-15 and Lys-276 affects the mRNA CC splicing activity of the protein, leading to regulate some, but CC not all, alternative splicing events. CC -!- SIMILARITY: Belongs to the splicing factor SR family. CC -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains. 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; X64044; CAA45409.1; -; mRNA. DR EMBL; CH471135; EAW72404.1; -; Genomic_DNA. DR EMBL; BC008740; AAH08740.1; -; mRNA. DR EMBL; BC030574; AAH30574.1; -; mRNA. DR PIR; S20250; S20250. DR RefSeq; NP_001012496.1; NM_001012478.1. DR RefSeq; NP_009210.1; NM_007279.2. DR UniGene; Hs.528007; -. DR PDB; 1JMT; X-ray; 2.20 A; B=85-112. DR PDB; 1O0P; NMR; -; A=372-475. DR PDB; 1OPI; NMR; -; A=372-475. DR PDB; 1U2F; NMR; -; A=148-237. DR PDB; 2G4B; X-ray; 2.50 A; A=148-336. DR PDB; 2HZC; X-ray; 1.47 A; A=148-229. DR PDB; 2M0G; NMR; -; B=372-475. DR PDB; 2U2F; NMR; -; A=258-342. DR PDB; 2YH0; NMR; -; A=148-342. DR PDB; 2YH1; NMR; -; A=148-342. DR PDB; 3VAF; X-ray; 2.49 A; A/B=148-336. DR PDB; 3VAG; X-ray; 2.19 A; A/B=148-336. DR PDB; 3VAH; X-ray; 2.50 A; A/B=148-336. DR PDB; 3VAI; X-ray; 2.20 A; A/B=148-336. DR PDB; 3VAJ; X-ray; 1.90 A; A/B=148-336. DR PDB; 3VAK; X-ray; 2.17 A; A/B=148-336. DR PDB; 3VAL; X-ray; 2.50 A; A/B/D/I=148-336. DR PDB; 3VAM; X-ray; 2.40 A; A/B=148-336. DR PDB; 4FXW; X-ray; 2.29 A; A/C=375-475. DR PDBsum; 1JMT; -. DR PDBsum; 1O0P; -. DR PDBsum; 1OPI; -. DR PDBsum; 1U2F; -. DR PDBsum; 2G4B; -. DR PDBsum; 2HZC; -. DR PDBsum; 2M0G; -. DR PDBsum; 2U2F; -. DR PDBsum; 2YH0; -. DR PDBsum; 2YH1; -. DR PDBsum; 3VAF; -. DR PDBsum; 3VAG; -. DR PDBsum; 3VAH; -. DR PDBsum; 3VAI; -. DR PDBsum; 3VAJ; -. DR PDBsum; 3VAK; -. DR PDBsum; 3VAL; -. DR PDBsum; 3VAM; -. DR PDBsum; 4FXW; -. DR ProteinModelPortal; P26368; -. DR SMR; P26368; 148-475. DR BioGrid; 116466; 125. DR DIP; DIP-2154N; -. DR IntAct; P26368; 49. DR MINT; MINT-1192370; -. DR STRING; 9606.ENSP00000307863; -. DR PhosphoSite; P26368; -. DR DMDM; 267188; -. DR PaxDb; P26368; -. DR PRIDE; P26368; -. DR DNASU; 11338; -. DR Ensembl; ENST00000308924; ENSP00000307863; ENSG00000063244. DR Ensembl; ENST00000450554; ENSP00000388475; ENSG00000063244. DR GeneID; 11338; -. DR KEGG; hsa:11338; -. DR UCSC; uc002qlu.3; human. DR CTD; 11338; -. DR GeneCards; GC19P056165; -. DR HGNC; HGNC:23156; U2AF2. DR HPA; CAB010910; -. DR HPA; HPA041943; -. DR HPA; HPA043562; -. DR MIM; 191318; gene. DR neXtProt; NX_P26368; -. DR PharmGKB; PA134908683; -. DR eggNOG; NOG298004; -. DR HOGENOM; HOG000180745; -. DR HOVERGEN; HBG062169; -. DR InParanoid; P26368; -. DR KO; K12837; -. DR OMA; YARRETR; -. DR OrthoDB; EOG7CNZFZ; -. DR PhylomeDB; P26368; -. DR TreeFam; TF314111; -. DR Reactome; REACT_1675; mRNA Processing. DR Reactome; REACT_1788; Transcription. DR Reactome; REACT_71; Gene Expression. DR Reactome; REACT_78; Post-Elongation Processing of the Transcript. DR ChiTaRS; U2AF2; human. DR EvolutionaryTrace; P26368; -. DR GeneWiki; U2AF2; -. DR GenomeRNAi; 11338; -. DR NextBio; 43079; -. DR PMAP-CutDB; P26368; -. DR PRO; PR:P26368; -. DR ArrayExpress; P26368; -. DR Bgee; P26368; -. DR CleanEx; HS_U2AF2; -. DR Genevestigator; P26368; -. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005681; C:spliceosomal complex; IDA:HGNC. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome. DR GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:HGNC. DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome. DR Gene3D; 3.30.70.330; -; 3. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR006529; U2AF_lg. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 3. DR TIGRFAMs; TIGR01642; U2AF_lg; 1. DR PROSITE; PS50102; RRM; 3. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Direct protein sequencing; Hydroxylation; mRNA processing; KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Repressor; RNA-binding; Spliceosome. FT INIT_MET 1 1 Removed. FT CHAIN 2 475 Splicing factor U2AF 65 kDa subunit. FT /FTId=PRO_0000081988. FT DOMAIN 149 231 RRM 1. FT DOMAIN 259 337 RRM 2. FT DOMAIN 385 466 RRM 3. FT COMPBIAS 27 62 Arg/Ser-rich (RS domain). FT MOD_RES 2 2 N-acetylserine. FT MOD_RES 2 2 Phosphoserine. FT MOD_RES 15 15 5-hydroxylysine; by JMJD6. FT MOD_RES 70 70 N6-acetyllysine. FT MOD_RES 79 79 Phosphoserine. FT MOD_RES 276 276 5-hydroxylysine; by JMJD6. FT VAR_SEQ 345 348 Missing (in isoform 2). FT /FTId=VSP_035414. FT MUTAGEN 92 92 W->A: Decreases affinity for UAF1 by 3 FT orders of magnitude. FT MUTAGEN 96 96 P->G: Decreases affinity for UAF1 by 2 FT orders of magnitude. FT MUTAGEN 104 104 P->G: Decreases affinity for UAF1 by 2 FT orders of magnitude. FT MUTAGEN 387 388 EE->RR: Reduces interaction with SF1. FT MUTAGEN 391 394 DDEE->AAAA: Reduces interaction with SF1. FT MUTAGEN 391 394 DDEE->RRKK: Reduces interaction with SF1. FT MUTAGEN 396 397 EE->AA: No effect. FT MUTAGEN 396 397 EE->GA: Reduces interaction with SF1. FT MUTAGEN 396 397 EE->KK: Reduces interaction with SF1. FT MUTAGEN 454 454 F->A: Reduces interaction with SF1. FT HELIX 104 109 FT STRAND 150 155 FT HELIX 162 175 FT STRAND 180 183 FT STRAND 185 191 FT STRAND 193 204 FT HELIX 205 211 FT HELIX 212 214 FT STRAND 219 222 FT STRAND 225 227 FT STRAND 238 240 FT STRAND 244 246 FT STRAND 261 264 FT HELIX 272 280 FT STRAND 281 283 FT STRAND 285 292 FT TURN 294 296 FT STRAND 299 309 FT HELIX 312 320 FT STRAND 326 328 FT STRAND 331 334 FT STRAND 376 383 FT HELIX 386 389 FT HELIX 392 406 FT TURN 407 409 FT STRAND 414 416 FT TURN 422 424 FT TURN 427 430 FT STRAND 431 435 FT HELIX 439 449 FT STRAND 454 457 FT STRAND 460 463 FT HELIX 466 470 SQ SEQUENCE 475 AA; 53501 MW; 26AD271CD8FC6211 CRC64; MSDFDEFERQ LNENKQERDK ENRHRKRSHS RSRSRDRKRR SRSRDRRNRD QRSASRDRRR RSKPLTRGAK EEHGGLIRSP RHEKKKKVRK YWDVPPPGFE HITPMQYKAM QAAGQIPATA LLPTMTPDGL AVTPTPVPVV GSQMTRQARR LYVGNIPFGI TEEAMMDFFN AQMRLGGLTQ APGNPVLAVQ INQDKNFAFL EFRSVDETTQ AMAFDGIIFQ GQSLKIRRPH DYQPLPGMSE NPSVYVPGVV STVVPDSAHK LFIGGLPNYL NDDQVKELLT SFGPLKAFNL VKDSATGLSK GYAFCEYVDI NVTDQAIAGL NGMQLGDKKL LVQRASVGAK NATLVSPPST INQTPVTLQV PGLMSSQVQM GGHPTEVLCL MNMVLPEELL DDEEYEEIVE DVRDECSKYG LVKSIEIPRP VDGVEVPGCG KIFVEFTSVF DCQKAMQGLT GRKFANRVVV TKYCDPDSYH RRDFW //