ID   TLE2_HUMAN              Reviewed;         743 AA.
AC   Q04725; B4DE03; E9PEV7; F8WCH2; Q8WVY0; Q9Y6S0;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2002, sequence version 2.
DT   27-MAR-2024, entry version 203.
DE   RecName: Full=Transducin-like enhancer protein 2;
DE   AltName: Full=Enhancer of split groucho-like protein 2;
DE            Short=ESG2;
GN   Name=TLE2;
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).
RC   TISSUE=Fetal brain;
RX   PubMed=1303260; DOI=10.1038/ng1092-119;
RA   Stifani S., Blaumueller C.M., Redhead N.J., Hill R.E.,
RA   Artavanis-Tsakonas S.;
RT   "Human homologs of a Drosophila enhancer of split gene product define a
RT   novel family of nuclear proteins.";
RL   Nat. Genet. 2:119-127(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP   GLY-381.
RC   TISSUE=Brain, and Urinary bladder;
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 GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
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   [5]
RP   OLIGOMERIZATION, AND INTERACTION WITH HES1 AND HES5.
RX   PubMed=9874198; DOI=10.1046/j.1432-1327.1998.2580339.x;
RA   Grbavec D., Lo R., Liu Y., Stifani S.;
RT   "Transducin-like Enhancer of split 2, a mammalian homologue of Drosophila
RT   Groucho, acts as a transcriptional repressor, interacts with Hairy/Enhancer
RT   of split proteins, and is expressed during neuronal development.";
RL   Eur. J. Biochem. 258:339-349(1998).
RN   [6]
RP   INTERACTION WITH UTY.
RX   PubMed=9854018; DOI=10.1042/bj3370013;
RA   Grbavec D., Lo R., Liu Y., Greenfield A., Stifani S.;
RT   "Groucho/transducin-like enhancer of split (TLE) family members interact
RT   with the yeast transcriptional co-repressor SSN6 and mammalian SSN6-related
RT   proteins: implications for evolutionary conservation of transcription
RT   repression mechanisms.";
RL   Biochem. J. 337:13-17(1999).
RN   [7]
RP   INTERACTION WITH LEF1; TCF7; TCF7L1 AND TCF7L2.
RX   PubMed=11266540; DOI=10.1093/nar/29.7.1410;
RA   Brantjes H., Roose J., van De Wetering M., Clevers H.;
RT   "All Tcf HMG box transcription factors interact with Groucho-related co-
RT   repressors.";
RL   Nucleic Acids Res. 29:1410-1419(2001).
RN   [8]
RP   REVIEW.
RX   PubMed=18254933; DOI=10.1186/gb-2008-9-1-205;
RA   Jennings B.H., Ish-Horowicz D.;
RT   "The Groucho/TLE/Grg family of transcriptional co-repressors.";
RL   Genome Biol. 9:R205.1-R205.7(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, AND IDENTIFICATION BY
RP   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   [10]
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   [11]
RP   UBIQUITINATION BY XIAP/BIRC4.
RX   PubMed=22304967; DOI=10.1016/j.molcel.2011.12.032;
RA   Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A., Lee E.;
RT   "XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling.";
RL   Mol. Cell 45:619-628(2012).
CC   -!- FUNCTION: Transcriptional corepressor that binds to a number of
CC       transcription factors. Inhibits the transcriptional activation mediated
CC       by CTNNB1 and TCF family members in Wnt signaling. The effects of full-
CC       length TLE family members may be modulated by association with
CC       dominant-negative AES (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer and heterooligomer with other family members.
CC       Binds LEF1, TCF7, TCF7L1, TCF7L2, UTY, HES1 and HES5.
CC   -!- INTERACTION:
CC       Q04725; Q16531: DDB1; NbExp=2; IntAct=EBI-1176061, EBI-350322;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q04725-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q04725-2; Sequence=VSP_045693, VSP_045694;
CC       Name=3;
CC         IsoId=Q04725-3; Sequence=VSP_046162, VSP_046163, VSP_046164;
CC   -!- TISSUE SPECIFICITY: In all tissues examined, mostly in heart, brain,
CC       and muscle.
CC   -!- DOMAIN: WD repeat Groucho/TLE family members are characterized by 5
CC       regions, a glutamine-rich Q domain, a glycine/proline-rich GP domain, a
CC       central CcN domain, containing a nuclear localization signal, and a
CC       serine/proline-rich SP domain. The most highly conserved are the N-
CC       terminal Q domain and the C-terminal WD-repeat domain.
CC       {ECO:0000305|PubMed:18254933}.
CC   -!- PTM: Ubiquitinated by XIAP/BIRC4. {ECO:0000269|PubMed:22304967}.
CC   -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK308137; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M99436; AAA61193.1; -; mRNA.
DR   EMBL; AK293407; BAG56914.1; -; mRNA.
DR   EMBL; AK308137; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC007766; AAD38075.1; -; Genomic_DNA.
DR   EMBL; AC011549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC093053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC017364; AAH17364.1; -; mRNA.
DR   CCDS; CCDS45911.1; -. [Q04725-1]
DR   CCDS; CCDS45912.1; -. [Q04725-2]
DR   CCDS; CCDS45913.1; -. [Q04725-3]
DR   PIR; C56695; C56695.
DR   RefSeq; NP_001138233.1; NM_001144761.1. [Q04725-3]
DR   RefSeq; NP_001138234.1; NM_001144762.1. [Q04725-2]
DR   RefSeq; NP_001287775.1; NM_001300846.1.
DR   RefSeq; NP_003251.2; NM_003260.4. [Q04725-1]
DR   AlphaFoldDB; Q04725; -.
DR   SMR; Q04725; -.
DR   BioGRID; 112944; 137.
DR   CORUM; Q04725; -.
DR   IntAct; Q04725; 26.
DR   MINT; Q04725; -.
DR   STRING; 9606.ENSP00000466542; -.
DR   GlyCosmos; Q04725; 2 sites, 1 glycan.
DR   GlyGen; Q04725; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q04725; -.
DR   PhosphoSitePlus; Q04725; -.
DR   BioMuta; TLE2; -.
DR   DMDM; 20532416; -.
DR   EPD; Q04725; -.
DR   jPOST; Q04725; -.
DR   MassIVE; Q04725; -.
DR   MaxQB; Q04725; -.
DR   PaxDb; 9606-ENSP00000466542; -.
DR   PeptideAtlas; Q04725; -.
DR   ProteomicsDB; 19967; -.
DR   ProteomicsDB; 31151; -.
DR   ProteomicsDB; 58267; -. [Q04725-1]
DR   Antibodypedia; 23107; 227 antibodies from 31 providers.
DR   DNASU; 7089; -.
DR   Ensembl; ENST00000262953.11; ENSP00000262953.5; ENSG00000065717.16. [Q04725-1]
DR   Ensembl; ENST00000426948.6; ENSP00000392869.2; ENSG00000065717.16. [Q04725-3]
DR   Ensembl; ENST00000443826.7; ENSP00000392427.2; ENSG00000065717.16. [Q04725-2]
DR   Ensembl; ENST00000591529.5; ENSP00000468279.1; ENSG00000065717.16. [Q04725-3]
DR   GeneID; 7089; -.
DR   KEGG; hsa:7089; -.
DR   MANE-Select; ENST00000262953.11; ENSP00000262953.5; NM_003260.5; NP_003251.2.
DR   UCSC; uc002lww.3; human. [Q04725-1]
DR   AGR; HGNC:11838; -.
DR   CTD; 7089; -.
DR   DisGeNET; 7089; -.
DR   GeneCards; TLE2; -.
DR   HGNC; HGNC:11838; TLE2.
DR   HPA; ENSG00000065717; Tissue enhanced (brain).
DR   MIM; 601041; gene.
DR   neXtProt; NX_Q04725; -.
DR   OpenTargets; ENSG00000065717; -.
DR   PharmGKB; PA36540; -.
DR   VEuPathDB; HostDB:ENSG00000065717; -.
DR   eggNOG; KOG0639; Eukaryota.
DR   GeneTree; ENSGT01030000234519; -.
DR   HOGENOM; CLU_007612_3_0_1; -.
DR   InParanoid; Q04725; -.
DR   OrthoDB; 1333122at2759; -.
DR   PhylomeDB; Q04725; -.
DR   TreeFam; TF314167; -.
DR   PathwayCommons; Q04725; -.
DR   Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR   Reactome; R-HSA-4641265; Repression of WNT target genes.
DR   SignaLink; Q04725; -.
DR   SIGNOR; Q04725; -.
DR   BioGRID-ORCS; 7089; 28 hits in 1160 CRISPR screens.
DR   ChiTaRS; TLE2; human.
DR   GeneWiki; TLE2; -.
DR   GenomeRNAi; 7089; -.
DR   Pharos; Q04725; Tbio.
DR   PRO; PR:Q04725; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q04725; Protein.
DR   Bgee; ENSG00000065717; Expressed in cerebellar hemisphere and 204 other cell types or tissues.
DR   ExpressionAtlas; Q04725; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR005617; Groucho/TLE_N.
DR   InterPro; IPR009146; Groucho_enhance.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR10814; TRANSDUCIN-LIKE ENHANCER PROTEIN; 1.
DR   PANTHER; PTHR10814:SF4; TRANSDUCIN-LIKE ENHANCER PROTEIN 2; 1.
DR   Pfam; PF03920; TLE_N; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR01850; GROUCHOFAMLY.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
DR   Genevisible; Q04725; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation;
KW   WD repeat; Wnt signaling pathway.
FT   CHAIN           1..743
FT                   /note="Transducin-like enhancer protein 2"
FT                   /id="PRO_0000051278"
FT   REPEAT          455..493
FT                   /note="WD 1"
FT   REPEAT          501..540
FT                   /note="WD 2"
FT   REPEAT          545..584
FT                   /note="WD 3"
FT   REPEAT          587..626
FT                   /note="WD 4"
FT   REPEAT          669..708
FT                   /note="WD 5"
FT   REPEAT          710..742
FT                   /note="WD 6"
FT   REGION          1..127
FT                   /note="Q domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q04724"
FT   REGION          128..191
FT                   /note="GP domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q04724"
FT   REGION          179..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..254
FT                   /note="CcN domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q04724"
FT   REGION          239..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..423
FT                   /note="SP domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q04724"
FT   REGION          296..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           214..217
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        214..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         228
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         249
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         253
FT                   /note="Phosphothreonine; by CDK1"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         281
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VAR_SEQ         1..55
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045693"
FT   VAR_SEQ         1..8
FT                   /note="MYPQGRHP -> MVQSRLTATSASQDSPASGLQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046162"
FT   VAR_SEQ         124..190
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045694"
FT   VAR_SEQ         124
FT                   /note="Q -> QQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046163"
FT   VAR_SEQ         683..743
FT                   /note="GRWFVSTGKDNLLNAWRTPYGASIFQSKESSSVLSCDISRNNKYIVTGSGDK
FT                   KATVYEVVY -> VQGVVLSPEL (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046164"
FT   VARIANT         381
FT                   /note="S -> G (in dbSNP:rs199788562)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_069063"
FT   CONFLICT        280
FT                   /note="G -> R (in Ref. 1; AAA61193)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        328
FT                   /note="A -> L (in Ref. 1; AAA61193)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        441
FT                   /note="G -> D (in Ref. 1; AAA61193)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        495
FT                   /note="A -> R (in Ref. 1; AAA61193)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        636..637
FT                   /note="LG -> PC (in Ref. 1; AAA61193)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        660
FT                   /note="R -> G (in Ref. 1; AAA61193)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        681
FT                   /note="S -> P (in Ref. 1; AAA61193)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   743 AA;  79841 MW;  5E3DBFAB67278219 CRC64;
     MYPQGRHPTP LQSGQPFKFS ILEICDRIKE EFQFLQAQYH SLKLECEKLA SEKTEMQRHY
     VMYYEMSYGL NIEMHKQAEI VKRLSGICAQ IIPFLTQEHQ QQVLQAVERA KQVTVGELNS
     LIGQQLQPLS HHAPPVPLTP RPAGLVGGSA TGLLALSGAL AAQAQLAAAV KEDRAGVEAE
     GSRVERAPSR SASPSPPESL VEEERPSGPG GGGKQRADEK EPSGPYESDE DKSDYNLVVD
     EDQPSEPPSP ATTPCGKVPI CIPARRDLVD SPASLASSLG SPLPRAKELI LNDLPASTPA
     SKSCDSSPPQ DASTPGPSSA SHLCQLAAKP APSTDSVALR SPLTLSSPFT TSFSLGSHST
     LNGDLSVPSS YVSLHLSPQV SSSVVYGRSP VMAFESHPHL RGSSVSSSLP SIPGGKPAYS
     FHVSADGQMQ PVPFPSDALV GAGIPRHARQ LHTLAHGEVV CAVTISGSTQ HVYTGGKGCV
     KVWDVGQPGA KTPVAQLDCL NRDNYIRSCK LLPDGRSLIV GGEASTLSIW DLAAPTPRIK
     AELTSSAPAC YALAVSPDAK VCFSCCSDGN IVVWDLQNQT MVRQFQGHTD GASCIDISDY
     GTRLWTGGLD NTVRCWDLRE GRQLQQHDFS SQIFSLGHCP NQDWLAVGME SSNVEILHVR
     KPEKYQLHLH ESCVLSLKFA SCGRWFVSTG KDNLLNAWRT PYGASIFQSK ESSSVLSCDI
     SRNNKYIVTG SGDKKATVYE VVY
//