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 24-JAN-2024, entry version 196. 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}. 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; 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 PDB; 7P70; X-ray; 2.00 A; A=107-196. DR PDB; 7PC4; X-ray; 2.30 A; A=107-196. DR PDBsum; 7P70; -. DR PDBsum; 7PC4; -. DR AlphaFoldDB; Q13884; -. DR SMR; Q13884; -. DR BioGRID; 112524; 65. DR ComplexPortal; CPX-2424; Dystrophin glycoprotein complex, skeletal muscle variant. DR ComplexPortal; CPX-2443; Dystrophin glycoprotein complex, neuromuscular junction variant. DR ComplexPortal; CPX-2454; Dystrophin glycoprotein complex, retinal outer plexiform layer variant. DR ComplexPortal; CPX-2455; Dystrophin glycoprotein complex, retinal inner limiting membrane variant. DR DIP; DIP-466N; -. DR IntAct; Q13884; 37. 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 SwissPalm; Q13884; -. DR BioMuta; SNTB1; -. DR DMDM; 23822159; -. DR EPD; Q13884; -. DR jPOST; Q13884; -. DR MassIVE; Q13884; -. DR MaxQB; Q13884; -. DR PaxDb; 9606-ENSP00000378965; -. DR PeptideAtlas; Q13884; -. DR ProteomicsDB; 59711; -. [Q13884-1] DR ProteomicsDB; 59712; -. [Q13884-2] DR Pumba; Q13884; -. DR TopDownProteomics; Q13884-2; -. [Q13884-2] DR Antibodypedia; 13755; 176 antibodies from 26 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 AGR; HGNC:11168; -. 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; 2906429at2759; -. DR PhylomeDB; Q13884; -. DR TreeFam; TF317932; -. DR PathwayCommons; Q13884; -. DR SignaLink; Q13884; -. DR SIGNOR; Q13884; -. DR BioGRID-ORCS; 6641; 15 hits in 1148 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 162 other cell types or tissues. DR ExpressionAtlas; Q13884; baseline and differential. 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; cd00992; PDZ_signaling; 1. DR CDD; cd00821; PH; 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); 3. 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:SF11; BETA-1-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; 2. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50003; PH_DOMAIN; 2. DR Genevisible; Q13884; HS. PE 1: Evidence at protein level; KW 3D-structure; 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" FT STRAND 111..116 FT /evidence="ECO:0007829|PDB:7P70" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:7P70" FT STRAND 125..130 FT /evidence="ECO:0007829|PDB:7P70" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:7P70" FT STRAND 135..142 FT /evidence="ECO:0007829|PDB:7P70" FT HELIX 147..151 FT /evidence="ECO:0007829|PDB:7P70" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:7P70" FT HELIX 173..182 FT /evidence="ECO:0007829|PDB:7P70" FT STRAND 185..193 FT /evidence="ECO:0007829|PDB:7P70" 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 //