ZBED6_MOUSE
ID ZBED6_MOUSE Reviewed; 980 AA.
AC D2EAC2; D2EAC3; Q3UMD3; Q8C1U4; Q8CBM9;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Zinc finger BED domain-containing protein 6 {ECO:0000303|PubMed:20016685};
DE AltName: Full=Muscle growth regulator {ECO:0000303|PubMed:20134481};
DE Short=MGR {ECO:0000303|PubMed:20134481};
GN Name=Zbed6 {ECO:0000303|PubMed:20016685};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAT02778.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE INITIATION,
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Myoblast {ECO:0000269|PubMed:20016685};
RX PubMed=20016685; DOI=10.1371/journal.pbio.1000256;
RA Markljung E., Jiang L., Jaffe J.D., Mikkelsen T.S., Wallerman O.,
RA Larhammar M., Zhang X., Wang L., Saenz-Vash V., Gnirke A., Lindroth A.M.,
RA Barres R., Yan J., Stromberg S., De S., Ponten F., Lander E.S., Carr S.A.,
RA Zierath J.R., Kullander K., Wadelius C., Lindblad-Toh K., Andersson G.,
RA Hjalm G., Andersson L.;
RT "ZBED6, a novel transcription factor derived from a domesticated DNA
RT transposon regulates IGF2 expression and muscle growth.";
RL PLoS Biol. 7:E1000256-E1000256(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC41160.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC41160.1};
RC TISSUE=Diencephalon {ECO:0000312|EMBL:BAC41160.1},
RC Mammary gland {ECO:0000312|EMBL:BAE26165.1}, and
RC Urinary bladder {ECO:0000312|EMBL:BAC29161.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=20134481; DOI=10.1038/embor.2010.6;
RA Butter F., Kappei D., Buchholz F., Vermeulen M., Mann M.;
RT "A domesticated transposon mediates the effects of a single-nucleotide
RT polymorphism responsible for enhanced muscle growth.";
RL EMBO Rep. 11:305-311(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24043816; DOI=10.1073/pnas.1303625110;
RA Wang X., Jiang L., Wallerman O., Engstroem U., Ameur A., Gupta R.K., Qi Y.,
RA Andersson L., Welsh N.;
RT "Transcription factor ZBED6 affects gene expression, proliferation, and
RT cell death in pancreatic beta cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:15997-16002(2013).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26750727; DOI=10.1038/srep19006;
RA Wang X., Xie B., Qi Y., Wallerman O., Vasylovska S., Andersson L.,
RA Kozlova E.N., Welsh N.;
RT "Knock-down of ZBED6 in insulin-producing cells promotes N-cadherin
RT junctions between beta-cells and neural crest stem cells in vitro.";
RL Sci. Rep. 6:19006-19006(2016).
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=29440408; DOI=10.1073/pnas.1719278115;
RA Younis S., Schoenke M., Massart J., Hjortebjerg R., Sundstroem E.,
RA Gustafson U., Bjoernholm M., Krook A., Frystyk J., Zierath J.R.,
RA Andersson L.;
RT "The ZBED6-IGF2 axis has a major effect on growth of skeletal muscle and
RT internal organs in placental mammals.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E2048-E2057(2018).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32557799; DOI=10.1096/fj.201901321r;
RA Younis S., Naboulsi R., Wang X., Cao X., Larsson M., Sargsyan E.,
RA Bergsten P., Welsh N., Andersson L.;
RT "The importance of the ZBED6-IGF2 axis for metabolic regulation in mouse
RT myoblast cells.";
RL FASEB J. 34:10250-10266(2020).
CC -!- FUNCTION: Transcriptional repressor which binds to the consensus
CC sequence 5'-GCTCGC-3', transcription regulation may be tissue-specific
CC (PubMed:20016685, PubMed:20134481, PubMed:24043816, PubMed:29440408,
CC PubMed:32557799). Regulates the expression of target genes such as:
CC IGF2, PGAP6/TMEM8, ENHO, and PIANP (PubMed:20016685, PubMed:20134481,
CC PubMed:24043816, PubMed:29440408, PubMed:32557799). Acts as a
CC transcriptional repressor of growth factor IGF2, thereby negatively
CC regulating postnatal growth of muscles and internal organs, especially
CC in females (PubMed:20016685, PubMed:29440408, PubMed:32557799).
CC Negatively regulates myoblast differentiation and myoblast
CC mitochondrial activity via its regulation of IGF2 transcription
CC (PubMed:32557799). Negatively regulates the cell cycle of myoblasts,
CC potentially via transcriptional regulation of the E2F family of
CC transcription factors such as: E2F1 and E2F2 (PubMed:20016685,
CC PubMed:32557799). Positively regulates the cell cycle and survival of
CC pancreatic beta cells (PubMed:24043816). Binds to the CDH2 gene and may
CC directly repress CDH2 transcription (PubMed:26750727). Probably by
CC controlling CDH2 expression, regulates pancreatic beta cell adhesion,
CC and formation of cell-to-cell junctions between pancreatic beta cells
CC and neural crest stem cells (PubMed:26750727). May also play a role in
CC embryonic beta cell differentiation (PubMed:24043816). May play a role
CC in insulin sensitivity and glucose clearance (PubMed:29440408).
CC {ECO:0000269|PubMed:20016685, ECO:0000269|PubMed:20134481,
CC ECO:0000269|PubMed:24043816, ECO:0000269|PubMed:26750727,
CC ECO:0000269|PubMed:29440408, ECO:0000269|PubMed:32557799}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20016685,
CC ECO:0000269|PubMed:24043816, ECO:0000269|PubMed:26750727,
CC ECO:0000269|PubMed:32557799}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:20016685}. Cytoplasm {ECO:0000269|PubMed:24043816,
CC ECO:0000269|PubMed:26750727, ECO:0000269|PubMed:32557799}. Note=Located
CC predominantly in the nucleolus but is also dispersed throughout the
CC nucleus (PubMed:20016685). Mainly cytoplasmic in insulin- and glucagon-
CC positive islet pancreatic cells, however nuclear localization is
CC evidence in some pancreatic endocrine cells (PubMed:24043816).
CC {ECO:0000269|PubMed:20016685, ECO:0000269|PubMed:24043816}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:20016685}; Synonyms=Zbed6a
CC {ECO:0000269|PubMed:20016685};
CC IsoId=D2EAC2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:20016685}; Synonyms=Zbed6b
CC {ECO:0000269|PubMed:20016685};
CC IsoId=D2EAC2-2; Sequence=VSP_053206;
CC -!- TISSUE SPECIFICITY: Expressed in pancreatic islet cells and weakly
CC expressed in surrounding exocrine tissues (at protein level)
CC (PubMed:24043816). Expressed in muscle and brain (at protein level)
CC (PubMed:20016685). Shows broad tissue distribution with expression
CC detected in brain, stomach, intestine, heart, kidney, liver, lung,
CC skeletal muscle, ovary, spleen, tail and testis (PubMed:20016685).
CC {ECO:0000269|PubMed:20016685, ECO:0000269|PubMed:24043816}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal muscle tissues at 12.5 dpc.
CC {ECO:0000269|PubMed:29440408}.
CC -!- DISRUPTION PHENOTYPE: Increase in body weight of mice at 20 weeks of
CC age, at 23 weeks of age only female mice show an increase in body
CC weight and lean mass as a result of an increase in muscle mass
CC (PubMed:29440408). Increase in the weight of kidneys in both male and
CC female adult mice with an increase in the weight of the liver in female
CC mice (PubMed:29440408). Decrease in plasma insulin levels with an
CC increase in blood glucose clearance and increased reliance on
CC carbohydrates as a fuel source in male mice (PubMed:29440408). Increase
CC in serum IGF2 protein levels in adult mice (PubMed:29440408). Increase
CC in expression of IGF2, PGAP6/TMEM8, and ENHO in skeletal muscle
CC (PubMed:29440408). Expression of ENHO and PIANP also increases in the
CC heart and kidney, in addition to an increase of PGAP6/TMEM8 expression
CC in the heart (PubMed:29440408). Significant increase in expression of
CC PGAP6/TMEM8 and ENHO in fetal muscle tissue with a small marginal
CC increase in IGF2 expression (PubMed:29440408).
CC {ECO:0000269|PubMed:29440408}.
CC -!- MISCELLANEOUS: Encoded by an exapted DNA transposon located in an
CC intron of the Zc3h11a gene. {ECO:0000269|PubMed:20016685}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41160.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FM882123; CAT02778.1; -; mRNA.
DR EMBL; FM882123; CAT02779.1; -; mRNA.
DR EMBL; AK035705; BAC29161.1; -; mRNA.
DR EMBL; AK090300; BAC41160.1; ALT_INIT; mRNA.
DR EMBL; AK144981; BAE26165.1; -; mRNA.
DR EMBL; AC124338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS56643.1; -. [D2EAC2-1]
DR RefSeq; NP_001160024.1; NM_001166552.1. [D2EAC2-1]
DR AlphaFoldDB; D2EAC2; -.
DR STRING; 10090.ENSMUSP00000136026; -.
DR iPTMnet; D2EAC2; -.
DR PhosphoSitePlus; D2EAC2; -.
DR jPOST; D2EAC2; -.
DR MaxQB; D2EAC2; -.
DR PaxDb; D2EAC2; -.
DR PeptideAtlas; D2EAC2; -.
DR PRIDE; D2EAC2; -.
DR ProteomicsDB; 298491; -. [D2EAC2-1]
DR ProteomicsDB; 298492; -. [D2EAC2-2]
DR Antibodypedia; 77040; 9 antibodies from 6 providers.
DR Ensembl; ENSMUST00000179598; ENSMUSP00000136026; ENSMUSG00000094410. [D2EAC2-1]
DR GeneID; 667118; -.
DR KEGG; mmu:667118; -.
DR UCSC; uc007cqr.2; mouse. [D2EAC2-1]
DR CTD; 100381270; -.
DR MGI; MGI:3828086; Zbed6.
DR VEuPathDB; HostDB:ENSMUSG00000094410; -.
DR eggNOG; KOG1121; Eukaryota.
DR GeneTree; ENSGT00940000163411; -.
DR HOGENOM; CLU_303823_0_0_1; -.
DR InParanoid; D2EAC2; -.
DR OMA; KTSAVWN; -.
DR PhylomeDB; D2EAC2; -.
DR TreeFam; TF322818; -.
DR BioGRID-ORCS; 667118; 2 hits in 39 CRISPR screens.
DR PRO; PR:D2EAC2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; D2EAC2; protein.
DR Bgee; ENSMUSG00000094410; Expressed in ascending aorta and 198 other tissues.
DR ExpressionAtlas; D2EAC2; baseline and differential.
DR Genevisible; D2EAC2; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:0051148; P:negative regulation of muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0003309; P:type B pancreatic cell differentiation; IMP:UniProtKB.
DR InterPro; IPR008906; HATC_C_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR003656; Znf_BED.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR Pfam; PF02892; zf-BED; 2.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50808; ZF_BED; 2.
PE 1: Evidence at protein level;
KW Alternative initiation; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..980
FT /note="Zinc finger BED domain-containing protein 6"
FT /id="PRO_0000392574"
FT ZN_FING 130..187
FT /note="BED-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT ZN_FING 265..322
FT /note="BED-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT REGION 1..89
FT /note="Required for nucleolar localization"
FT /evidence="ECO:0000269|PubMed:20016685"
FT REGION 89..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..950
FT /note="HATC (Hobo-Ac-Tam3) domain"
FT COMPBIAS 205..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20016685"
FT /id="VSP_053206"
FT CONFLICT 574
FT /note="H -> Q (in Ref. 2; BAE26165)"
FT /evidence="ECO:0000305"
FT CONFLICT 901
FT /note="T -> I (in Ref. 2; BAC41160)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 980 AA; 109152 MW; B57559C15367A9DF CRC64;
MSVCTLSVPV SSISPGRRCS TFGDAGILGC VSINSNTDED DVVEGKMVAE GANKETKLPA
KKKRKKGLRI KGKRRRKKLI LAKKFSKDLG SGRPVADAPA SLASGAPEQD EESLFEGNIE
KQIYLPSTRA KTSIVWHFFH VDPQYTWRAI CNLCEKSVSR GKPGSHLGTS TLQRHLQARH
SPHWTRANKF GVTNGEEDFT LDLSLSPPSP GSNGSFEYIP TDSVDENRMG KKRDKSASDA
LRAKRGRFLI KSNIVKHALI PGTRAKTSAV WNFFYTDPQH ISRAVCNICK RSVSRGRPGS
HLGTSTLQRH LQATHPIHWA VANKDSGAIG NGLDETETES SDLLNDTMPG EKSSGSQDLT
AEDLSDSDTD EPPCLEVENR SESPIPVADQ DNPVHAQERE TTTHCENAAA NQISQAVIQM
IVEDLHPYNY FSTPAFQRFL QIVAPDYRLP SETYFFTKAV PQLYDSVREK IFLTLENVQS
QKIHLTADIW THDPSTDYFI VTVHWVSLET ASSPSNGGTP NFRKWAVLCV TGLAKDCLIT
NILQELNDQI GLWLSPNFLT PSFIVSDNSS NVVHAIKGGG FTHVPCFLHC LNIVIQDFFC
EHKSIENMLV AARKTCHHFS HSVKARQILQ EFQNDHQLPW KNLKQDETGH WISTFYMLKW
LLEHCYSVHH SLGRASGVVL TSLQWTLMTY VCDILKPFEE ATQRVSVKTT GLNQVLPLIH
HLLFSLQRLR EDFQVRGITQ ALNLVDSLSL KLESDALLSA MLKSKHCILA TLLDPCFKNS
LEDFFPQGAD LETYKQILAE EVCNYMESSP GACQISSSET SGPLVRLGTD SFTSIKEGTS
SAGSLDSSAA GSVAVGSKSS LLPAAVAVVD EYFKEKYSEL SGGDDPLVYW QRKVSIWPAL
TQVAIQYLSC PMCSWQSECM FTTNSHFHPK QIMNMDFDNI EQLIFLKMNL ENVNYDYSTL
ILSWDPENKA VQSNEKEILP
