SNTB2_HUMAN
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 03-AUG-2022, entry version 211.
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}.
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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; 124.
DR IntAct; Q13425; 56.
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; Q13425; -.
DR PeptideAtlas; Q13425; -.
DR PRIDE; Q13425; -.
DR ProteomicsDB; 59410; -. [Q13425-1]
DR ProteomicsDB; 59411; -. [Q13425-2]
DR Antibodypedia; 656; 155 antibodies from 20 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 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; AHSWFMA; -.
DR PhylomeDB; Q13425; -.
DR TreeFam; TF317932; -.
DR PathwayCommons; Q13425; -.
DR SignaLink; Q13425; -.
DR SIGNOR; Q13425; -.
DR BioGRID-ORCS; 6645; 9 hits in 1071 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 195 other tissues.
DR ExpressionAtlas; Q13425; baseline and differential.
DR Genevisible; Q13425; HS.
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; cd01258; PHsplit_syntrophin; 1.
DR Gene3D; 2.30.29.30; -; 1.
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; IPR028550; SNTB2.
DR InterPro; IPR015482; Syntrophin.
DR PANTHER; PTHR10554; PTHR10554; 1.
DR PANTHER; PTHR10554:SF8; PTHR10554:SF8; 1.
DR Pfam; PF00595; PDZ; 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; 1.
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
