ID SNTB2_HUMAN Reviewed; 540 AA. AC Q13425; Q9BY09; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 220. DE RecName: Full=Beta-2-syntrophin; DE AltName: Full=59 kDa dystrophin-associated protein A1 basic component 2; DE AltName: Full=Syntrophin-3; DE Short=SNT3; DE AltName: Full=Syntrophin-like; DE Short=SNTL; GN Name=SNTB2; Synonyms=D16S2531E, SNT2B2, SNTL; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH DMD; DTNA AND RP UTRN. RC TISSUE=Muscle; RX PubMed=8576247; DOI=10.1074/jbc.271.5.2724; RA Ahn A.H., Feener C.A., Gussoni E., Yoshida M., Ozawa E., Kunkel L.M.; RT "The three human syntrophin genes are expressed in diverse tissues, have RT distinct chromosomal locations, and each bind to dystrophin and its RT relatives."; RL J. Biol. Chem. 271:2724-2730(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH PTPRN. RC TISSUE=Brain; RX PubMed=11043403; DOI=10.1078/0171-9335-00095; RA Ort T., Maksimova E., Dirkx R., Kachinsky A.M., Berghs S., Froehner S.C., RA Solimena M.; RT "The receptor tyrosine phosphatase-like protein ICA512 binds the PDZ RT domains of beta2-syntrophin and nNOS in pancreatic beta-cells."; RL Eur. J. Cell Biol. 79:621-630(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Mammary gland; 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] RP INTERACTION WITH ERBB4. RX PubMed=10725395; DOI=10.1073/pnas.97.7.3596; RA Garcia R.A., Vasudevan K., Buonanno A.; RT "The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at RT neuronal synapses."; RL Proc. Natl. Acad. Sci. U.S.A. 97:3596-3601(2000). RN [5] RP INTERACTION WITH PTPRN. RX PubMed=11483505; DOI=10.1093/emboj/20.15.4013; RA Ort T., Voronov S., Guo J., Zawalich K., Froehner S.C., Zawalich W., RA Solimena M.; RT "Dephosphorylation of beta2-syntrophin and Ca2+/mu-calpain-mediated RT cleavage of ICA512 upon stimulation of insulin secretion."; RL EMBO J. 20:4013-4023(2001). RN [6] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-233 AND SER-393, AND 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-110; SER-222 AND RP SER-393, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] 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., Buerckstuemmer T., RA 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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-110; SER-129; RP SER-222; SER-393 AND SER-395, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-110 AND SER-211, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP VARIANT ARG-376. RX PubMed=24234652; DOI=10.1093/hmg/ddt578; RA Ohkawara B., Cabrera-Serrano M., Nakata T., Milone M., Asai N., Ito K., RA Ito M., Masuda A., Ito Y., Engel A.G., Ohno K.; RT "LRP4 third beta-propeller domain mutations cause novel congenital RT myasthenia by compromising agrin-mediated MuSK signaling in a position- RT specific manner."; RL Hum. Mol. Genet. 23:1856-1868(2014). CC -!- FUNCTION: Adapter protein that binds to and probably organizes the CC subcellular localization of a variety of membrane proteins. May link CC various receptors to the actin cytoskeleton and the dystrophin CC glycoprotein complex. May play a role in the regulation of secretory CC granules via its interaction with PTPRN. CC -!- SUBUNIT: Monomer and homodimer (Probable). Interacts with the other CC members of the syntrophin family: SNTA1 and SNTB1; and with the sodium CC channel proteins SCN4A and SCN5A. Interacts with SAST, MAST205, CC microtubules and microtubule-associated proteins (By similarity). CC Interacts with the dystrophin protein DMD and related proteins DTNA and CC UTRN, and with the neuroregulin receptor ERBB4. Interacts with PTPRN CC when phosphorylated, protecting PTPRN from protein cleavage by CAPN1. CC Dephosphorylation upon insulin stimulation disrupts the interaction CC with PTPRN and results in the cleavage of PTPRN. Interacts with DTNB CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q61235, CC ECO:0000269|PubMed:10725395, ECO:0000269|PubMed:11043403, CC ECO:0000269|PubMed:11483505, ECO:0000269|PubMed:8576247, ECO:0000305}. CC -!- INTERACTION: CC Q13425; P25100: ADRA1D; NbExp=16; IntAct=EBI-80411, EBI-489993; CC Q13425; O14936: CASK; NbExp=3; IntAct=EBI-80411, EBI-1215506; CC Q13425; P11532: DMD; NbExp=2; IntAct=EBI-80411, EBI-295827; CC -!- SUBCELLULAR LOCATION: Membrane. Cytoplasmic vesicle, secretory vesicle CC membrane; Peripheral membrane protein. Cell junction {ECO:0000250}. CC Cytoplasm, cytoskeleton. Note=Membrane-associated. In muscle, it is CC exclusively localized at the neuromuscular junction (By similarity). In CC insulinoma cell line, it is enriched in secretory granules. CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Beta2-syntrophin58; CC IsoId=Q13425-1; Sequence=Displayed; CC Name=2; Synonyms=Beta2-syntrophin28; CC IsoId=Q13425-2; Sequence=VSP_006358, VSP_006359; CC -!- TISSUE SPECIFICITY: Ubiquitous. Isoform 1 is the predominant isoform. CC Weak level of isoform 2 is present in all tested tissues, except in CC liver and heart where it is highly expressed. CC -!- DOMAIN: The PH 1 domain mediates the oligomerization in a calcium CC dependent manner. {ECO:0000250}. CC -!- DOMAIN: The PDZ domain binds to the last three or four amino acids of CC ion channels and receptor proteins. The association with dystrophin or CC related proteins probably leaves the PDZ domain available to recruit CC proteins to the membrane (By similarity). {ECO:0000250}. CC -!- DOMAIN: The SU domain binds calmodulin in a calcium-dependent manner. CC {ECO:0000250}. CC -!- PTM: Phosphorylated. Partially dephosphorylated upon insulin CC stimulation. CC -!- MISCELLANEOUS: [Isoform 2]: Lacks domains required for interaction with CC dystrophin related proteins. May be produced at very low levels due to CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the syntrophin family. {ECO:0000305}. 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; U40572; AAC50449.1; -; mRNA. DR EMBL; AF243385; AAK15149.1; -; mRNA. DR EMBL; BC048215; AAH48215.1; -; mRNA. DR CCDS; CCDS10873.1; -. [Q13425-1] DR RefSeq; NP_006741.1; NM_006750.3. [Q13425-1] DR PDB; 2VRF; X-ray; 2.00 A; A/B/C/D=112-200. DR PDBsum; 2VRF; -. DR AlphaFoldDB; Q13425; -. DR SMR; Q13425; -. DR BioGRID; 112528; 148. DR IntAct; Q13425; 66. DR MINT; Q13425; -. DR STRING; 9606.ENSP00000338191; -. DR GlyGen; Q13425; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q13425; -. DR PhosphoSitePlus; Q13425; -. DR SwissPalm; Q13425; -. DR BioMuta; SNTB2; -. DR DMDM; 23822158; -. DR EPD; Q13425; -. DR jPOST; Q13425; -. DR MassIVE; Q13425; -. DR MaxQB; Q13425; -. DR PaxDb; 9606-ENSP00000338191; -. DR PeptideAtlas; Q13425; -. DR ProteomicsDB; 59410; -. [Q13425-1] DR ProteomicsDB; 59411; -. [Q13425-2] DR Pumba; Q13425; -. DR Antibodypedia; 656; 179 antibodies from 21 providers. DR DNASU; 6645; -. DR Ensembl; ENST00000336278.9; ENSP00000338191.4; ENSG00000168807.17. [Q13425-1] DR Ensembl; ENST00000467311.5; ENSP00000436443.1; ENSG00000168807.17. [Q13425-2] DR GeneID; 6645; -. DR KEGG; hsa:6645; -. DR MANE-Select; ENST00000336278.9; ENSP00000338191.4; NM_006750.4; NP_006741.1. DR UCSC; uc002ewu.4; human. [Q13425-1] DR AGR; HGNC:11169; -. DR CTD; 6645; -. DR DisGeNET; 6645; -. DR GeneCards; SNTB2; -. DR HGNC; HGNC:11169; SNTB2. DR HPA; ENSG00000168807; Low tissue specificity. DR MIM; 600027; gene. DR neXtProt; NX_Q13425; -. DR OpenTargets; ENSG00000168807; -. DR PharmGKB; PA36009; -. DR VEuPathDB; HostDB:ENSG00000168807; -. DR eggNOG; KOG3551; Eukaryota. DR GeneTree; ENSGT00950000182863; -. DR HOGENOM; CLU_026406_3_1_1; -. DR InParanoid; Q13425; -. DR OMA; GGNHWDY; -. DR OrthoDB; 2906429at2759; -. DR PhylomeDB; Q13425; -. DR TreeFam; TF317932; -. DR PathwayCommons; Q13425; -. DR SignaLink; Q13425; -. DR SIGNOR; Q13425; -. DR BioGRID-ORCS; 6645; 9 hits in 1149 CRISPR screens. DR ChiTaRS; SNTB2; human. DR EvolutionaryTrace; Q13425; -. DR GeneWiki; SNTB2; -. DR GenomeRNAi; 6645; -. DR Pharos; Q13425; Tbio. DR PRO; PR:Q13425; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q13425; Protein. DR Bgee; ENSG00000168807; Expressed in tibia and 197 other cell types or tissues. DR ExpressionAtlas; Q13425; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IBA:GO_Central. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0045202; C:synapse; IBA:GO_Central. DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR CDD; cd00992; PDZ_signaling; 1. DR CDD; cd01258; PHsplit_syntrophin; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR041428; PHsplit_syntrophin. DR InterPro; IPR015482; Syntrophin. DR PANTHER; PTHR10554:SF8; BETA-2-SYNTROPHIN; 1. DR PANTHER; PTHR10554; SYNTROPHIN; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF18012; PH_17; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00233; PH; 2. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR Genevisible; Q13425; HS. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative splicing; Calcium; KW Calmodulin-binding; Cell junction; Cytoplasm; Cytoplasmic vesicle; KW Cytoskeleton; Membrane; Microtubule; Phosphoprotein; Reference proteome; KW Repeat. FT CHAIN 1..540 FT /note="Beta-2-syntrophin" FT /id="PRO_0000184011" FT DOMAIN 115..198 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 163..300 FT /note="PH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 325..437 FT /note="PH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 484..540 FT /note="SU" FT REGION 73..114 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 220..240 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 518..540 FT /note="Calmodulin-binding" FT /evidence="ECO:0000250" FT COMPBIAS 89..106 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 95 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 110 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 129 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 211 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 222 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 233 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 393 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 395 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 266..267 FT /note="LI -> QN (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11043403" FT /id="VSP_006358" FT VAR_SEQ 268..540 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11043403" FT /id="VSP_006359" FT VARIANT 376 FT /note="S -> R" FT /evidence="ECO:0000269|PubMed:24234652" FT /id="VAR_073697" FT VARIANT 424 FT /note="D -> E (in dbSNP:rs1058482)" FT /id="VAR_014076" FT STRAND 113..119 FT /evidence="ECO:0007829|PDB:2VRF" FT STRAND 127..133 FT /evidence="ECO:0007829|PDB:2VRF" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:2VRF" FT STRAND 138..145 FT /evidence="ECO:0007829|PDB:2VRF" FT HELIX 150..154 FT /evidence="ECO:0007829|PDB:2VRF" FT STRAND 161..166 FT /evidence="ECO:0007829|PDB:2VRF" FT HELIX 176..184 FT /evidence="ECO:0007829|PDB:2VRF" FT STRAND 188..196 FT /evidence="ECO:0007829|PDB:2VRF" SQ SEQUENCE 540 AA; 57950 MW; 53A9F3340DC024ED CRC64; MRVAAATAAA GAGPAMAVWT RATKAGLVEL LLRERWVRVV AELSGESLSL TGDAAAAELE PALGPAAAAF NGLPNGGGAG DSLPGSPSRG LGPPSPPAPP RGPAGEAGAS PPVRRVRVVK QEAGGLGISI KGGRENRMPI LISKIFPGLA ADQSRALRLG DAILSVNGTD LRQATHDQAV QALKRAGKEV LLEVKFIREV TPYIKKPSLV SDLPWEGAAP QSPSFSGSED SGSPKHQNST KDRKIIPLKM CFAARNLSMP DLENRLIELH SPDSRNTLIL RCKDTATAHS WFVAIHTNIM ALLPQVLAEL NAMLGATSTA GGSKEVKHIA WLAEQAKLDG GRQQWRPVLM AVTEKDLLLY DCMPWTRDAW ASPCHSYPLV ATRLVHSGSG CRSPSLGSDL TFATRTGSRQ GIEMHLFRVE THRDLSSWTR ILVQGCHAAA ELIKEVSLGC MLNGQEVRLT IHYENGFTIS RENGGSSSIL YRYPFERLKM SADDGIRNLY LDFGGPEGEL TMDLHSCPKP IVFVLHTFLS AKVTRMGLLV //