ERG_HUMAN
ID ERG_HUMAN Reviewed; 479 AA.
AC P11308; B4DTW5; B4E0T4; Q16113; Q6XXX4; Q6XXX5; Q8IXK9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 3.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Transcriptional regulator ERG;
DE AltName: Full=Transforming protein ERG;
GN Name=ERG;
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 3).
RX PubMed=3299708; DOI=10.1126/science.3299708;
RA Rao V.N., Papas T.S., Shyam E., Reddy P.;
RT "erg, a human ets-related gene on chromosome 21: alternative splicing,
RT polyadenylation, and translation.";
RL Science 237:635-639(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=3476934; DOI=10.1073/pnas.84.17.6131;
RA Reddy E.S.P., Rao V.N., Papas T.S.;
RT "The erg gene: a human gene related to the ets oncogene.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6131-6135(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
RX PubMed=14693372; DOI=10.1016/j.gene.2003.09.047;
RA Owczarek C.M., Portbury K.J., Hardy M.P., O'Leary D.A., Kudoh J.,
RA Shibuya K., Shimizu N., Kola I., Hertzog P.J.;
RT "Detailed mapping of the ERG-ETS2 interval of human chromosome 21 and
RT comparison with the region of conserved synteny on mouse chromosome 16.";
RL Gene 324:65-77(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 230-259 (ISOFORM 2).
RX PubMed=8290279;
RA Prasad D.D., Rao V.N., Lee L., Reddy E.S.;
RT "Differentially spliced erg-3 product functions as a transcriptional
RT activator.";
RL Oncogene 9:669-673(1994).
RN [7]
RP CHROMOSOMAL TRANSLOCATION WITH EWSR1.
RX PubMed=8076344; DOI=10.1016/0165-4608(94)90063-9;
RA Dunn T., Praissman L., Hagag N., Viola M.V.;
RT "ERG gene is translocated in an Ewing's sarcoma cell line.";
RL Cancer Genet. Cytogenet. 76:19-22(1994).
RN [8]
RP CHROMOSOMAL TRANSLOCATION WITH FUS.
RX PubMed=8187069;
RA Ichikawa H., Shimizu K., Hayashi Y., Ohki M.;
RT "An RNA-binding protein gene, TLS/FUS, is fused to ERG in human myeloid
RT leukemia with t(16;21) chromosomal translocation.";
RL Cancer Res. 54:2865-2868(1994).
RN [9]
RP CHROMOSOMAL TRANSLOCATION WITH ELF4.
RX PubMed=16303180; DOI=10.1016/j.leukres.2005.10.014;
RA Moore S.D., Offor O., Ferry J.A., Amrein P.C., Morton C.C., Dal Cin P.;
RT "ELF4 is fused to ERG in a case of acute myeloid leukemia with a
RT t(X;21)(q25-26;q22).";
RL Leuk. Res. 30:1037-1042(2006).
RN [10]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-282, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [12]
RP STRUCTURE BY NMR OF 105-201.
RX PubMed=15351649; DOI=10.1016/j.jmb.2004.07.094;
RA Mackereth C.D., Scharpf M., Gentile L.N., MacIntosh S.E., Slupsky C.M.,
RA McIntosh L.P.;
RT "Diversity in structure and function of the Ets family PNT domains.";
RL J. Mol. Biol. 342:1249-1264(2004).
CC -!- FUNCTION: Transcriptional regulator. May participate in transcriptional
CC regulation through the recruitment of SETDB1 histone methyltransferase
CC and subsequent modification of local chromatin structure.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with SETDB1.
CC {ECO:0000269|PubMed:17289661}.
CC -!- INTERACTION:
CC P11308; P10275: AR; NbExp=4; IntAct=EBI-79704, EBI-608057;
CC P11308; O75164: KDM4A; NbExp=2; IntAct=EBI-79704, EBI-936709;
CC P11308; P09874: PARP1; NbExp=7; IntAct=EBI-79704, EBI-355676;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237,
CC ECO:0000269|PubMed:17289661}. Cytoplasm {ECO:0000269|PubMed:17289661}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=P11308-4; Sequence=Displayed;
CC Name=2; Synonyms=ERG-3;
CC IsoId=P11308-3; Sequence=VSP_060678;
CC Name=3; Synonyms=ERG-2;
CC IsoId=P11308-1; Sequence=VSP_060678, VSP_060679;
CC Name=4; Synonyms=ERG-1;
CC IsoId=P11308-2; Sequence=VSP_060677, VSP_060679;
CC Name=5;
CC IsoId=P11308-5; Sequence=VSP_060678, VSP_060681, VSP_060682;
CC Name=6;
CC IsoId=P11308-6; Sequence=VSP_060678, VSP_060680, VSP_060683;
CC -!- DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant,
CC metastatic, primitive small round cell tumor of bone and soft tissue
CC that affects children and adolescents. It belongs to the Ewing sarcoma
CC family of tumors, a group of morphologically heterogeneous neoplasms
CC that share the same cytogenetic features. They are considered neural
CC tumors derived from cells of the neural crest. Ewing sarcoma represents
CC the less differentiated form of the tumors.
CC {ECO:0000269|PubMed:8076344}. Note=The gene represented in this entry
CC is involved in disease pathogenesis. A chromosomal aberration involving
CC ERG has been found in patients with Erwing sarcoma. Translocation
CC t(21;22)(q22;q12) with EWSR1. {ECO:0000269|PubMed:8076344}.
CC -!- DISEASE: Note=Chromosomal aberrations involving ERG have been found in
CC acute myeloid leukemia (AML). Translocation t(16;21)(p11;q22) with FUS
CC (PubMed:8187069). Translocation t(X;21)(q25-26;q22) with ELF4
CC (PubMed:16303180). {ECO:0000269|PubMed:16303180,
CC ECO:0000269|PubMed:8187069}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ERGID53ch21q22.html";
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DR EMBL; M17254; AAA52398.1; -; mRNA.
DR EMBL; M21535; AAA35811.1; -; mRNA.
DR EMBL; AY204741; AAP41719.1; -; mRNA.
DR EMBL; AY204742; AAP41720.1; -; mRNA.
DR EMBL; AK300395; BAG62127.1; -; mRNA.
DR EMBL; AK303518; BAG64546.1; -; mRNA.
DR EMBL; BC040168; AAH40168.1; -; mRNA.
DR EMBL; S68130; AAB29724.1; -; mRNA.
DR CCDS; CCDS13657.1; -. [P11308-1]
DR CCDS; CCDS13658.1; -. [P11308-4]
DR CCDS; CCDS46648.1; -. [P11308-3]
DR CCDS; CCDS58789.1; -. [P11308-2]
DR PIR; A94294; TVHUEG.
DR RefSeq; NP_001129626.1; NM_001136154.1. [P11308-3]
DR RefSeq; NP_001129627.1; NM_001136155.1.
DR RefSeq; NP_001230357.1; NM_001243428.1. [P11308-3]
DR RefSeq; NP_001230358.1; NM_001243429.1. [P11308-2]
DR RefSeq; NP_001230361.1; NM_001243432.2. [P11308-5]
DR RefSeq; NP_001278320.1; NM_001291391.1. [P11308-6]
DR RefSeq; NP_004440.1; NM_004449.4. [P11308-1]
DR RefSeq; NP_891548.1; NM_182918.3. [P11308-4]
DR PDB; 1SXE; NMR; -; A=108-201.
DR PDB; 4IRG; X-ray; 1.70 A; A=306-405.
DR PDB; 4IRH; X-ray; 2.10 A; A=280-405.
DR PDB; 4IRI; X-ray; 2.77 A; A=280-405.
DR PDB; 5YBC; X-ray; 2.50 A; A/C=310-401.
DR PDB; 5YBD; X-ray; 2.77 A; A/X=310-399.
DR PDB; 6VGE; X-ray; 4.25 A; A=306-419.
DR PDB; 6VGG; X-ray; 4.31 A; A=306-419.
DR PDBsum; 1SXE; -.
DR PDBsum; 4IRG; -.
DR PDBsum; 4IRH; -.
DR PDBsum; 4IRI; -.
DR PDBsum; 5YBC; -.
DR PDBsum; 5YBD; -.
DR PDBsum; 6VGE; -.
DR PDBsum; 6VGG; -.
DR AlphaFoldDB; P11308; -.
DR BMRB; P11308; -.
DR SMR; P11308; -.
DR BioGRID; 108389; 196.
DR CORUM; P11308; -.
DR DIP; DIP-31028N; -.
DR ELM; P11308; -.
DR IntAct; P11308; 118.
DR MINT; P11308; -.
DR STRING; 9606.ENSP00000414150; -.
DR BindingDB; P11308; -.
DR ChEMBL; CHEMBL1293191; -.
DR GlyGen; P11308; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P11308; -.
DR PhosphoSitePlus; P11308; -.
DR BioMuta; ERG; -.
DR DMDM; 152031600; -.
DR jPOST; P11308; -.
DR MassIVE; P11308; -.
DR MaxQB; P11308; -.
DR PaxDb; P11308; -.
DR PeptideAtlas; P11308; -.
DR PRIDE; P11308; -.
DR ProteomicsDB; 52735; -. [P11308-3]
DR ProteomicsDB; 52736; -. [P11308-1]
DR ProteomicsDB; 52737; -. [P11308-2]
DR ProteomicsDB; 52738; -. [P11308-4]
DR ProteomicsDB; 52739; -. [P11308-5]
DR ProteomicsDB; 52740; -. [P11308-6]
DR TopDownProteomics; P11308-6; -. [P11308-6]
DR ABCD; P11308; 1 sequenced antibody.
DR Antibodypedia; 4338; 638 antibodies from 41 providers.
DR DNASU; 2078; -.
DR Ensembl; ENST00000288319.12; ENSP00000288319.7; ENSG00000157554.20. [P11308-4]
DR Ensembl; ENST00000398897.5; ENSP00000381871.1; ENSG00000157554.20. [P11308-2]
DR Ensembl; ENST00000398911.5; ENSP00000381882.1; ENSG00000157554.20. [P11308-1]
DR Ensembl; ENST00000398919.6; ENSP00000381891.2; ENSG00000157554.20. [P11308-3]
DR Ensembl; ENST00000417133.6; ENSP00000414150.2; ENSG00000157554.20. [P11308-3]
DR Ensembl; ENST00000442448.5; ENSP00000394694.1; ENSG00000157554.20. [P11308-1]
DR GeneID; 2078; -.
DR KEGG; hsa:2078; -.
DR MANE-Select; ENST00000288319.12; ENSP00000288319.7; NM_182918.4; NP_891548.1.
DR UCSC; uc002yxa.4; human. [P11308-4]
DR CTD; 2078; -.
DR DisGeNET; 2078; -.
DR GeneCards; ERG; -.
DR HGNC; HGNC:3446; ERG.
DR HPA; ENSG00000157554; Low tissue specificity.
DR MalaCards; ERG; -.
DR MIM; 165080; gene.
DR MIM; 612219; phenotype.
DR neXtProt; NX_P11308; -.
DR OpenTargets; ENSG00000157554; -.
DR Orphanet; 370334; Extraskeletal Ewing sarcoma.
DR Orphanet; 319; Skeletal Ewing sarcoma.
DR PharmGKB; PA27858; -.
DR VEuPathDB; HostDB:ENSG00000157554; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000160662; -.
DR HOGENOM; CLU_045216_0_0_1; -.
DR InParanoid; P11308; -.
DR OMA; RVPQQEW; -.
DR PhylomeDB; P11308; -.
DR TreeFam; TF350537; -.
DR PathwayCommons; P11308; -.
DR SignaLink; P11308; -.
DR SIGNOR; P11308; -.
DR BioGRID-ORCS; 2078; 12 hits in 1093 CRISPR screens.
DR ChiTaRS; ERG; human.
DR EvolutionaryTrace; P11308; -.
DR GeneWiki; ERG_(gene); -.
DR GenomeRNAi; 2078; -.
DR Pharos; P11308; Tbio.
DR PRO; PR:P11308; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P11308; protein.
DR Bgee; ENSG00000157554; Expressed in tendon of biceps brachii and 163 other tissues.
DR ExpressionAtlas; P11308; baseline and differential.
DR Genevisible; P11308; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR003118; Pointed_dom.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF00178; Ets; 1.
DR Pfam; PF02198; SAM_PNT; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SMART; SM00251; SAM_PNT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR PROSITE; PS51433; PNT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosomal rearrangement; Cytoplasm;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..479
FT /note="Transcriptional regulator ERG"
FT /id="PRO_0000204103"
FT DOMAIN 113..199
FT /note="PNT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT DNA_BIND 311..391
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 34..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 462..463
FT /note="Breakpoint for translocation to form ELF4-ERG
FT oncogene"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P81270"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P81270"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P81270"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..92
FT /note="Missing (in isoform 4)"
FT /id="VSP_060677"
FT VAR_SEQ 1..4
FT /note="MAST -> MIQTVPDPAAH (in isoform 2, isoform 3,
FT isoform 5 and isoform 6)"
FT /id="VSP_060678"
FT VAR_SEQ 225..248
FT /note="Missing (in isoform 3 and isoform 4)"
FT /id="VSP_060679"
FT VAR_SEQ 249..318
FT /note="DLPYEPPRRSAWTGHGHPTPQSKAAQPSPSTVPKTEDQRPQLDPYQILGPTS
FT SRLANPGSGQIQLWQFLL -> GTKTPLCDLFIERHPRCPAEIRALSHVIQRELIPELK
FT PVPDSLILPLLIWRLNPLKPFHSKTTLKELRAD (in isoform 6)"
FT /id="VSP_060680"
FT VAR_SEQ 308..310
FT /note="SGQ -> WTQ (in isoform 5)"
FT /id="VSP_060681"
FT VAR_SEQ 311..479
FT /note="Missing (in isoform 5)"
FT /id="VSP_060682"
FT VAR_SEQ 319..479
FT /note="Missing (in isoform 6)"
FT /id="VSP_060683"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1SXE"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:1SXE"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:1SXE"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:1SXE"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1SXE"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:1SXE"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:1SXE"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1SXE"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:1SXE"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:4IRG"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:4IRG"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:4IRG"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:5YBC"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:5YBC"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:4IRG"
FT HELIX 344..355
FT /evidence="ECO:0007829|PDB:4IRG"
FT HELIX 362..374
FT /evidence="ECO:0007829|PDB:4IRG"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:4IRG"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:4IRG"
FT HELIX 392..398
FT /evidence="ECO:0007829|PDB:4IRG"
SQ SEQUENCE 479 AA; 53838 MW; A5069C393E409483 CRC64;
MASTIKEALS VVSEDQSLFE CAYGTPHLAK TEMTASSSSD YGQTSKMSPR VPQQDWLSQP
PARVTIKMEC NPSQVNGSRN SPDECSVAKG GKMVGSPDTV GMNYGSYMEE KHMPPPNMTT
NERRVIVPAD PTLWSTDHVR QWLEWAVKEY GLPDVNILLF QNIDGKELCK MTKDDFQRLT
PSYNADILLS HLHYLRETPL PHLTSDDVDK ALQNSPRLMH ARNTGGAAFI FPNTSVYPEA
TQRITTRPDL PYEPPRRSAW TGHGHPTPQS KAAQPSPSTV PKTEDQRPQL DPYQILGPTS
SRLANPGSGQ IQLWQFLLEL LSDSSNSSCI TWEGTNGEFK MTDPDEVARR WGERKSKPNM
NYDKLSRALR YYYDKNIMTK VHGKRYAYKF DFHGIAQALQ PHPPESSLYK YPSDLPYMGS
YHAHPQKMNF VAPHPPALPV TSSSFFAAPN PYWNSPTGGI YPNTRLPTSH MPSHLGTYY
