ID TFE3_HUMAN Reviewed; 575 AA. AC P19532; A8MZL6; Q5JU74; Q92757; Q92758; Q99964; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 4. DT 16-MAR-2016, entry version 173. DE RecName: Full=Transcription factor E3; DE AltName: Full=Class E basic helix-loop-helix protein 33; DE Short=bHLHe33; GN Name=TFE3; Synonyms=BHLHE33; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION RP WITH PSF AND NONO. RX PubMed=9393982; DOI=10.1038/sj.onc.1201394; RA Clark J., Lu Y.-J., Sidhar S.K., Parker C., Gill S., Smedley D., RA Hamoudi R., Linehan W.M., Shipley J., Cooper C.S.; RT "Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3 RT gene in papillary renal cell carcinoma."; RL Oncogene 15:2233-2239(1997). RN [2] RP SEQUENCE REVISION. RA Clark J.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-219, AND CHROMOSOMAL RP TRANSLOCATION WITH PRCC. RX PubMed=8986805; DOI=10.1073/pnas.93.26.15294; RA Weterman M.A.J., Wilbrink M., Geurts van Kessel A.; RT "Fusion of the transcription factor TFE3 gene to a novel gene, PRCC, RT in t(X;1)(p11;q21)-positive papillary renal cell carcinomas."; RL Proc. Natl. Acad. Sci. U.S.A. 93:15294-15298(1996). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-575, AND CHROMOSOMAL RP TRANSLOCATION WITH PRCC. RC TISSUE=Monocyte; RX PubMed=8872474; DOI=10.1093/hmg/5.9.1333; RA Sidhar S.K., Clark J., Gill S., Hamoudi R., Crew A.J., Gwilliam R., RA Ross M., Linehan W.M., Birdsall S., Shipley J., Cooper C.S.; RT "The t(X;1)(p11.2;q21.2) translocation in papillary renal cell RT carcinoma fuses a novel gene PRCC to the TFE3 transcription factor RT gene."; RL Hum. Mol. Genet. 5:1333-1338(1996). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 212-575 (ISOFORM 1). RC TISSUE=Leukemia; RX PubMed=2338243; DOI=10.1101/gad.4.2.167; RA Beckmann H., Su L.-K., Kadesch T.; RT "TFE3: a helix-loop-helix protein that activates transcription through RT the immunoglobulin enhancer muE3 motif."; RL Genes Dev. 4:167-179(1990). RN [8] RP CHROMOSOMAL TRANSLOCATION WITH ASPSCR1. RX PubMed=11358836; RA Heimann P., El Housni H., Ogur G., Weterman M.A.J., Petty E.M., RA Vassart G.; RT "Fusion of a novel gene, RCC17, to the TFE3 gene in RT t(X;17)(p11.2;q25.3)-bearing papillary renal cell carcinomas."; RL Cancer Res. 61:4130-4135(2001). RN [9] RP CHROMOSOMAL TRANSLOCATION WITH ASPSCR1, AND INVOLVEMENT IN ASPS. RX PubMed=11244503; DOI=10.1038/sj.onc.1204074; RA Ladanyi M., Lui M.Y., Antonescu C.R., Krause-Boehm A., Meindl A., RA Argani P., Healey J.H., Ueda T., Yoshikawa H., Meloni-Ehrig A., RA Sorensen P.H.B., Mertens F., Mandahl N., van den Berghe H., Sciot R., RA Dal Cin P., Bridge J.; RT "The der(17)t(X;17)(p11;q25) of human alveolar soft part sarcoma fuses RT the TFE3 transcription factor gene to ASPL, a novel gene at 17q25."; RL Oncogene 20:48-57(2001). RN [10] RP SUMOYLATION, AND INTERACTION WITH MITF. RX PubMed=15507434; DOI=10.1074/jbc.M411757200; RA Miller A.J., Levy C., Davis I.J., Razin E., Fisher D.E.; RT "Sumoylation of MITF and its related family members TFE3 and TFEB."; RL J. Biol. Chem. 280:146-155(2005). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, AND IDENTIFICATION RP BY 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [12] 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., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548; SER-556 AND RP SER-560, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556 AND SER-568, AND 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542 AND SER-548, 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Transcription factor that specifically recognizes and CC binds E-box sequences (5'-CANNTG-3'). Efficient DNA-binding CC requires dimerization with itself or with another MiT/TFE family CC member such as TFEB or MITF. In association with TFEB, activates CC the expression of CD40L in T-cells, thereby playing a role in T- CC cell-dependent antibody responses in activated CD4(+) T-cells and CC thymus-dependent humoral immunity. Specifically recognizes the CC MUE3 box, a subset of E-boxes, present in the immunoglobulin CC enhancer. It also binds very well to a USF/MLTF site. CC -!- SUBUNIT: Homodimer and heterodimer; with TFEB or MITF. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P19532-1; Sequence=Displayed; CC Name=2; CC IsoId=P19532-2; Sequence=VSP_056882, VSP_056883; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Ubiquitous in fetal and adult tissues. CC -!- PTM: Sumoylated; does not affect dimerization with MITF. CC {ECO:0000269|PubMed:15507434}. CC -!- DISEASE: Note=A chromosomal aberration involving TFE3 is found in CC patients with alveolar soft part sarcoma. Translocation CC t(X;17)(p11;q25) with ASPSCR1 forms a ASPSCR1-TFE3 fusion protein. CC {ECO:0000269|PubMed:11358836}. CC -!- DISEASE: Note=Chromosomal aberrations involving TFE3 are found in CC patients with papillary renal cell carcinoma. Translocation CC t(X;1)(p11.2;q21.2) with PRCC; translocation t(X;1)(p11.2;p34) CC with PSF; inversion inv(X)(p11.2;q12) that fuses NONO to TFE3. CC {ECO:0000269|PubMed:8872474, ECO:0000269|PubMed:8986805}. CC -!- SIMILARITY: Belongs to the MiT/TFE family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 bHLH (basic helix-loop-helix) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00981}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA35714.1; Type=Frameshift; Positions=557; Evidence={ECO:0000305}; CC Sequence=CAA65800.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/TFE3ID86.html"; 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; X96717; CAA65478.1; -; mRNA. DR EMBL; AL161985; CAI46207.1; -; mRNA. DR EMBL; AC146820; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF196779; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX572102; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X99721; CAA68061.1; -; Genomic_DNA. DR EMBL; X97160; CAA65800.1; ALT_SEQ; Genomic_DNA. DR EMBL; X97161; CAA65800.1; JOINED; Genomic_DNA. DR EMBL; X97162; CAA65800.1; JOINED; Genomic_DNA. DR EMBL; X51330; CAA35714.1; ALT_SEQ; mRNA. DR CCDS; CCDS14315.3; -. [P19532-1] DR PIR; A34596; A34596. DR RefSeq; NP_001269071.1; NM_001282142.1. DR RefSeq; NP_006512.2; NM_006521.5. [P19532-1] DR UniGene; Hs.730740; -. DR ProteinModelPortal; P19532; -. DR SMR; P19532; 347-437. DR BioGrid; 112888; 21. DR DIP; DIP-50187N; -. DR IntAct; P19532; 4. DR STRING; 9606.ENSP00000314129; -. DR iPTMnet; P19532; -. DR PhosphoSite; P19532; -. DR DMDM; 160113240; -. DR EPD; P19532; -. DR MaxQB; P19532; -. DR PaxDb; P19532; -. DR PRIDE; P19532; -. DR DNASU; 7030; -. DR Ensembl; ENST00000315869; ENSP00000314129; ENSG00000068323. [P19532-1] DR Ensembl; ENST00000493583; ENSP00000476976; ENSG00000068323. [P19532-2] DR GeneID; 7030; -. DR KEGG; hsa:7030; -. DR UCSC; uc004dmb.5; human. [P19532-1] DR CTD; 7030; -. DR GeneCards; TFE3; -. DR HGNC; HGNC:11752; TFE3. DR HPA; HPA023881; -. DR MalaCards; TFE3; -. DR MIM; 314310; gene. DR neXtProt; NX_P19532; -. DR Orphanet; 163699; Alveolar soft-tissue sarcoma. DR Orphanet; 319308; Translocation renal cell carcinoma. DR PharmGKB; PA36467; -. DR eggNOG; KOG1318; Eukaryota. DR eggNOG; ENOG410ZYYV; LUCA. DR GeneTree; ENSGT00390000004402; -. DR HOGENOM; HOG000231368; -. DR HOVERGEN; HBG006768; -. DR InParanoid; P19532; -. DR KO; K09105; -. DR OMA; PGTATFH; -. DR OrthoDB; EOG72G182; -. DR PhylomeDB; P19532; -. DR TreeFam; TF317174; -. DR ChiTaRS; TFE3; human. DR GeneWiki; TFE3; -. DR GenomeRNAi; 7030; -. DR NextBio; 27465; -. DR PRO; PR:P19532; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; P19532; -. DR CleanEx; HS_TFE3; -. DR ExpressionAtlas; P19532; baseline and differential. DR Genevisible; P19532; HS. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IMP:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB. DR GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB. DR GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0006959; P:humoral immune response; ISS:UniProtKB. DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB. DR GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:Ensembl. DR Gene3D; 4.10.280.10; -; 1. DR InterPro; IPR011598; bHLH_dom. DR InterPro; IPR021802; MiT/TFE_C. DR InterPro; IPR031867; MiT/TFE_N. DR InterPro; IPR024100; TFE3. DR PANTHER; PTHR12565:SF163; PTHR12565:SF163; 2. DR Pfam; PF11851; DUF3371; 1. DR Pfam; PF00010; HLH; 1. DR Pfam; PF15951; MITF_TFEB_C_3_N; 1. DR SMART; SM00353; HLH; 1. DR SUPFAM; SSF47459; SSF47459; 1. DR PROSITE; PS50888; BHLH; 1. PE 1: Evidence at protein level; KW Activator; Adaptive immunity; Alternative splicing; KW Chromosomal rearrangement; Complete proteome; DNA-binding; Immunity; KW Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1 575 Transcription factor E3. FT /FTId=PRO_0000127471. FT DOMAIN 346 399 bHLH. {ECO:0000255|PROSITE- FT ProRule:PRU00981}. FT REGION 260 271 Strong transcription activation domain. FT {ECO:0000255}. FT REGION 409 430 Leucine-zipper. FT SITE 178 179 Breakpoint for translocation to form FT PRCC-TFE3 oncogene. FT SITE 260 261 Breakpoint for translocation to form FT ASPSCR1-TFE3 oncogene. FT SITE 295 296 Breakpoint for translocation to form FT NONO-TFE3, PSF-TFE3 and ASPSCR1-TFE3 FT oncogenes. FT MOD_RES 542 542 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 548 548 Phosphoserine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 554 554 Phosphoserine. FT {ECO:0000250|UniProtKB:Q64092}. FT MOD_RES 556 556 Phosphoserine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 560 560 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 568 568 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT VAR_SEQ 77 109 SLPISLQATPATPATLSASSSAGGSRTPAMSSS -> RGLQ FT DPCHVVIFFIEGLAAAAANAGPGAGAGEA (in isoform FT 2). {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_056882. FT VAR_SEQ 110 575 Missing (in isoform 2). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_056883. FT VARIANT 96 96 S -> C (in dbSNP:rs5953258). FT /FTId=VAR_027501. FT VARIANT 313 313 T -> A (in dbSNP:rs3027470). FT /FTId=VAR_027502. FT CONFLICT 172 172 V -> M (in Ref. 6; CAA65800). FT {ECO:0000305}. FT CONFLICT 219 219 P -> S (in Ref. 6; CAA65800). FT {ECO:0000305}. FT CONFLICT 222 222 P -> K (in Ref. 7; CAA35714). FT {ECO:0000305}. FT CONFLICT 229 229 P -> L (in Ref. 6; CAA65800). FT {ECO:0000305}. FT CONFLICT 443 443 P -> G (in Ref. 7; CAA35714). FT {ECO:0000305}. FT CONFLICT 455 455 A -> T (in Ref. 6; CAA65800 and 7; FT CAA35714). {ECO:0000305}. FT CONFLICT 475 475 A -> R (in Ref. 7; CAA35714). FT {ECO:0000305}. FT CONFLICT 575 575 S -> M (in Ref. 6; CAA65800). FT {ECO:0000305}. SQ SEQUENCE 575 AA; 61521 MW; EF1F11AB624C6BE1 CRC64; MSHAAEPARD GVEASAEGPR AVFVLLEERR PADSAQLLSL NSLLPESGIV ADIELENVLD PDSFYELKSQ PLPLRSSLPI SLQATPATPA TLSASSSAGG SRTPAMSSSS SSRVLLRQQL MRAQAQEQER RERREQAAAA PFPSPAPASP AISVVGVSAG GHTLSRPPPA QVPREVLKVQ THLENPTRYH LQQARRQQVK QYLSTTLGPK LASQALTPPP GPASAQPLPA PEAAHTTGPT GSAPNSPMAL LTIGSSSEKE IDDVIDEIIS LESSYNDEML SYLPGGTTGL QLPSTLPVSG NLLDVYSSQG VATPAITVSN SCPAELPNIK REISETEAKA LLKERQKKDN HNLIERRRRF NINDRIKELG TLIPKSSDPE MRWNKGTILK ASVDYIRKLQ KEQQRSKDLE SRQRSLEQAN RSLQLRIQEL ELQAQIHGLP VPPTPGLLSL ATTSASDSLK PEQLDIEEEG RPGAATFHVG GGPAQNAPHQ QPPAPPSDAL LDLHFPSDHL GDLGDPFHLG LEDILMEEEE GVVGGLSGGA LSPLRAASDP LLSSVSPAVS KASSRRSSFS MEEES //