SNTB1_HUMAN
ID SNTB1_HUMAN Reviewed; 538 AA.
AC Q13884; A8K9E0; O14912; Q4KMG8;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Beta-1-syntrophin;
DE AltName: Full=59 kDa dystrophin-associated protein A1 basic component 1;
DE Short=DAPA1B;
DE AltName: Full=BSYN2;
DE AltName: Full=Syntrophin-2;
DE AltName: Full=Tax interaction protein 43;
DE Short=TIP-43;
GN Name=SNTB1; Synonyms=SNT2B1;
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 [GENOMIC DNA] (ISOFORM 1), PROTEIN SEQUENCE OF 105-114;
RP 197-208; 339-348 AND 351-355, AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=8183929; DOI=10.1073/pnas.91.10.4446;
RA Ahn A.H., Yoshida M., Anderson M.S., Feener C.A., Selig S., Hagiwara Y.,
RA Ozawa E., Kunkel L.M.;
RT "Cloning of human basic A1, a distinct 59-kDa dystrophin-associated protein
RT encoded on chromosome 8q23-24.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4446-4450(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 2-19, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [5]
RP PROTEIN SEQUENCE OF 2-19; 23-31; 145-169; 325-332 AND 364-379, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Histiocytic lymphoma;
RA Bienvenut W.V., Okada H.;
RL Submitted (OCT-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 95-538 (ISOFORM 2), AND INTERACTION WITH
RP HTLV-1 TAX.
RC TISSUE=Lymphocyte;
RX PubMed=9482110; DOI=10.1038/sj.onc.1201567;
RA Rousset R., Fabre S., Desbois C., Bantignies F., Jalinot P.;
RT "The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the
RT PDZ domain of cellular proteins.";
RL Oncogene 16:643-654(1998).
RN [7]
RP INTERACTION WITH DMD; DTNA AND UTRN.
RX PubMed=7844150; DOI=10.1083/jcb.128.3.363;
RA Ahn A.H., Kunkel L.M.;
RT "Syntrophin binds to an alternatively spliced exon of dystrophin.";
RL J. Cell Biol. 128:363-371(1995).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-219 AND SER-389, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-389, AND
RP 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND IDENTIFICATION BY
RP 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-126; THR-214;
RP SER-219; SER-232 AND SER-389, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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.
CC -!- SUBUNIT: Monomer and homodimer (Probable). Interacts with the other
CC members of the syntrophin family SNTA1 and SNTB2; with the sodium
CC channel proteins SCN4A and SCN5A (By similarity). Interacts with the
CC viral HTLV-1 TAX protein and with dystrophin protein DMD and related
CC proteins DTNA and UTRN. Interacts with DTNB (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q99L88, ECO:0000269|PubMed:7844150,
CC ECO:0000269|PubMed:9482110, ECO:0000305}.
CC -!- INTERACTION:
CC Q13884; O95477: ABCA1; NbExp=3; IntAct=EBI-295843, EBI-784112;
CC Q13884; P11532: DMD; NbExp=4; IntAct=EBI-295843, EBI-295827;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cell junction {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=In skeletal muscle, it localizes at the cytoplasmic
CC side of the sarcolemmal membrane and at neuromuscular junctions.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13884-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13884-2; Sequence=VSP_006354, VSP_006355;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8183929}.
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 by CaM-kinase II. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the syntrophin family. {ECO:0000305}.
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DR EMBL; L31529; AAA81523.1; -; Genomic_DNA.
DR EMBL; AK292655; BAF85344.1; -; mRNA.
DR EMBL; BC098573; AAH98573.1; -; mRNA.
DR EMBL; AF028828; AAB84253.1; -; mRNA.
DR CCDS; CCDS6334.1; -. [Q13884-1]
DR PIR; I59291; I59291.
DR RefSeq; NP_066301.1; NM_021021.3. [Q13884-1]
DR RefSeq; XP_011515541.1; XM_011517239.1. [Q13884-2]
DR AlphaFoldDB; Q13884; -.
DR SMR; Q13884; -.
DR BioGRID; 112524; 54.
DR DIP; DIP-466N; -.
DR IntAct; Q13884; 28.
DR MINT; Q13884; -.
DR STRING; 9606.ENSP00000378965; -.
DR GlyGen; Q13884; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13884; -.
DR PhosphoSitePlus; Q13884; -.
DR BioMuta; SNTB1; -.
DR DMDM; 23822159; -.
DR EPD; Q13884; -.
DR jPOST; Q13884; -.
DR MassIVE; Q13884; -.
DR MaxQB; Q13884; -.
DR PaxDb; Q13884; -.
DR PeptideAtlas; Q13884; -.
DR PRIDE; Q13884; -.
DR ProteomicsDB; 59711; -. [Q13884-1]
DR ProteomicsDB; 59712; -. [Q13884-2]
DR TopDownProteomics; Q13884-2; -. [Q13884-2]
DR Antibodypedia; 13755; 162 antibodies from 25 providers.
DR DNASU; 6641; -.
DR Ensembl; ENST00000395601.7; ENSP00000378965.3; ENSG00000172164.15. [Q13884-1]
DR Ensembl; ENST00000517992.2; ENSP00000431124.1; ENSG00000172164.15. [Q13884-1]
DR GeneID; 6641; -.
DR KEGG; hsa:6641; -.
DR MANE-Select; ENST00000517992.2; ENSP00000431124.1; NM_021021.4; NP_066301.1.
DR UCSC; uc010mdg.4; human. [Q13884-1]
DR CTD; 6641; -.
DR DisGeNET; 6641; -.
DR GeneCards; SNTB1; -.
DR HGNC; HGNC:11168; SNTB1.
DR HPA; ENSG00000172164; Tissue enhanced (liver).
DR MIM; 600026; gene.
DR neXtProt; NX_Q13884; -.
DR OpenTargets; ENSG00000172164; -.
DR PharmGKB; PA36008; -.
DR VEuPathDB; HostDB:ENSG00000172164; -.
DR eggNOG; KOG3551; Eukaryota.
DR GeneTree; ENSGT00950000182863; -.
DR HOGENOM; CLU_026406_3_1_1; -.
DR InParanoid; Q13884; -.
DR OMA; GENEKQW; -.
DR OrthoDB; 1261897at2759; -.
DR PhylomeDB; Q13884; -.
DR TreeFam; TF317932; -.
DR PathwayCommons; Q13884; -.
DR SignaLink; Q13884; -.
DR SIGNOR; Q13884; -.
DR BioGRID-ORCS; 6641; 15 hits in 1070 CRISPR screens.
DR ChiTaRS; SNTB1; human.
DR GeneWiki; SNTB1; -.
DR GenomeRNAi; 6641; -.
DR Pharos; Q13884; Tbio.
DR PRO; PR:Q13884; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q13884; protein.
DR Bgee; ENSG00000172164; Expressed in right adrenal gland and 161 other tissues.
DR ExpressionAtlas; Q13884; baseline and differential.
DR Genevisible; Q13884; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR CDD; cd01258; PHsplit_syntrophin; 1.
DR Gene3D; 2.30.29.30; -; 3.
DR Gene3D; 2.30.42.10; -; 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; PTHR10554; 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; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Calcium;
KW Calmodulin-binding; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.5,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..538
FT /note="Beta-1-syntrophin"
FT /id="PRO_0000184009"
FT DOMAIN 19..298
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 112..195
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 322..433
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 482..538
FT /note="SU"
FT REGION 205..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..538
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 220..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.5,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99L88"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99L88"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 379..382
FT /note="RLVH -> SPHP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9482110"
FT /id="VSP_006354"
FT VAR_SEQ 383..538
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9482110"
FT /id="VSP_006355"
SQ SEQUENCE 538 AA; 58061 MW; BF8E7B416D5CF289 CRC64;
MAVAAAAAAA GPAGAGGGRA QRSGLLEVLV RDRWHKVLVN LSEDALVLSS EEGAAAYNGI
GTATNGSFCR GAGAGHPGAG GAQPPDSPAG VRTAFTDLPE QVPESISNQK RGVKVLKQEL
GGLGISIKGG KENKMPILIS KIFKGLAADQ TQALYVGDAI LSVNGADLRD ATHDEAVQAL
KRAGKEVLLE VKYMREATPY VKKGSPVSEI GWETPPPESP RLGGSTSDPP SSQSFSFHRD
RKSIPLKMCY VTRSMALADP ENRQLEIHSP DAKHTVILRS KDSATAQAWF SAIHSNVNDL
LTRVIAEVRE QLGKTGIAGS REIRHLGWLA EKVPGESKKQ WKPALVVLTE KDLLIYDSMP
RRKEAWFSPV HTYPLLATRL VHSGPGKGSP QAGVDLSFAT RTGTRQGIET HLFRAETSRD
LSHWTRSIVQ GCHNSAELIA EISTACTYKN QECRLTIHYE NGFSITTEPQ EGAFPKTIIQ
SPYEKLKMSS DDGIRMLYLD FGGKDGEIQL DLHSCPKPIV FIIHSFLSAK ITRLGLVA
