POP1_CAEEL
ID POP1_CAEEL Reviewed; 438 AA.
AC Q10666; O45007;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein pop-1;
DE AltName: Full=Posterior pharynx defect protein 1;
GN Name=pop-1 {ECO:0000312|WormBase:W10C8.2};
GN ORFNames=W10C8.2 {ECO:0000312|WormBase:W10C8.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=7585963; DOI=10.1016/0092-8674(95)90100-0;
RA Lin R., Thompson S., Priess J.R.;
RT "pop-1 encodes an HMG box protein required for the specification of a
RT mesoderm precursor in early C. elegans embryos.";
RL Cell 83:599-609(1995).
RN [2]
RP SEQUENCE REVISION.
RA Lin R., Thompson S., Priess J.R.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP SUBCELLULAR LOCATION, INTERACTION WITH LIT-1 AND WRM-1, DEVELOPMENTAL
RP STAGE, AND PHOSPHORYLATION.
RX PubMed=10380924; DOI=10.1016/s0092-8674(00)80784-9;
RA Rocheleau C.E., Yasuda J., Shin T.H., Lin R., Sawa H., Okano H.,
RA Priess J.R., Davis R.J., Mello C.C.;
RT "WRM-1 activates the LIT-1 protein kinase to transduce anterior/posterior
RT polarity signals in C. elegans.";
RL Cell 97:717-726(1999).
RN [5]
RP INTERACTION WITH BAR-1.
RX PubMed=10952315; DOI=10.1038/35020099;
RA Korswagen H.C., Herman M.A., Clevers H.C.;
RT "Distinct beta-catenins mediate adhesion and signalling functions in C.
RT elegans.";
RL Nature 406:527-532(2000).
RN [6]
RP FUNCTION, AND INTERACTION WITH HDA-1.
RX PubMed=11742996; DOI=10.1093/emboj/20.24.7197;
RA Calvo D., Victor M., Gay F., Sui G., Luke M.P.-S., Dufourcq P., Wen G.,
RA Maduro M., Rothman J., Shi Y.;
RT "A POP-1 repressor complex restricts inappropriate cell type-specific gene
RT transcription during Caenorhabditis elegans embryogenesis.";
RL EMBO J. 20:7197-7208(2001).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ASP-9 AND ASN-225.
RX PubMed=11807036; DOI=10.1242/dev.129.2.443;
RA Siegfried K.R., Kimble J.;
RT "POP-1 controls axis formation during early gonadogenesis in C. elegans.";
RL Development 129:443-453(2002).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=12810601; DOI=10.1242/dev.00563;
RA Park F.D., Priess J.R.;
RT "Establishment of POP-1 asymmetry in early C. elegans embryos.";
RL Development 130:3547-3556(2003).
RN [9]
RP INTERACTION WITH PAR-5 AND LIT-1, PHOSPHORYLATION AT SER-118 AND SER-127,
RP AND MUTAGENESIS OF SER-107; SER-109; SER-118; THR-120 AND SER-127.
RX PubMed=15066285; DOI=10.1016/s0092-8674(04)00203-x;
RA Lo M.-C., Gay F., Odom R., Shi Y., Lin R.;
RT "Phosphorylation by the beta-catenin/MAPK complex promotes 14-3-3-mediated
RT nuclear export of TCF/POP-1 in signal-responsive cells in C. elegans.";
RL Cell 117:95-106(2004).
RN [10]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15649465; DOI=10.1016/j.ydbio.2004.10.020;
RA Deshpande R., Inoue T., Priess J.R., Hill R.J.;
RT "lin-17/Frizzled and lin-18 regulate POP-1/TCF-1 localization and cell type
RT specification during C. elegans vulval development.";
RL Dev. Biol. 278:118-129(2005).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ASP-9 AND ASN-225.
RX PubMed=19427847; DOI=10.1016/j.ydbio.2009.05.538;
RA Amin N.M., Lim S.E., Shi H., Chan T.L., Liu J.;
RT "A conserved Six-Eya cassette acts downstream of Wnt signaling to direct
RT non-myogenic versus myogenic fates in the C. elegans postembryonic
RT mesoderm.";
RL Dev. Biol. 331:350-360(2009).
RN [12]
RP INTERACTION WITH EGL-5.
RX PubMed=20553900; DOI=10.1016/j.ydbio.2010.05.516;
RA Kalis A.K., Murphy M.W., Zarkower D.;
RT "EGL-5/ABD-B plays an instructive role in male cell fate determination in
RT the C. elegans somatic gonad.";
RL Dev. Biol. 344:827-835(2010).
RN [13]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=25569233; DOI=10.1371/journal.pgen.1004921;
RA Uehara T., Kage-Nakadai E., Yoshina S., Imae R., Mitani S.;
RT "The tumor suppressor BCL7B functions in the Wnt signaling pathway.";
RL PLoS Genet. 11:E1004921-E1004921(2015).
RN [14] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=31740621; DOI=10.1242/dev.180034;
RA van der Horst S.E.M., Cravo J., Woollard A., Teapal J., van den Heuvel S.;
RT "C. elegans Runx/CBFbeta suppresses POP-1 TCF to convert asymmetric to
RT proliferative division of stem cell-like seam cells.";
RL Development 146:0-0(2019).
CC -!- FUNCTION: Part of the Wnt signaling pathway essential for the
CC specification of the mesodermal cell fate in early embryos
CC (PubMed:11742996, PubMed:11807036, PubMed:19427847). Required for
CC asymmetrical division of somatic gonadal precursor descendants which
CC initiate axis formation required to control organ shape
CC (PubMed:11807036). Similarly, involved in asymmetrical division of seam
CC cells, a stem cell-like lineage (PubMed:31740621). Represses expression
CC of target genes via its interaction with hda-1 histone deacetylase
CC (PubMed:11742996). Required for specification of the M lineage-derived
CC coelomocyte and sex myoblast fate (PubMed:19427847). Regulates
CC coelomocyte fate by positively regulating proliferation and ceh-34 and
CC possibly eya-1 expression in M.dlpa and M.drpa precursors
CC (PubMed:19427847). {ECO:0000269|PubMed:11742996,
CC ECO:0000269|PubMed:11807036, ECO:0000269|PubMed:19427847,
CC ECO:0000269|PubMed:31740621}.
CC -!- SUBUNIT: Interacts with hda-1 (PubMed:11742996). Interacts with bar-1
CC (PubMed:10952315). Interacts with par-5; the interaction is direct and
CC is enhanced by lit-1-mediated pop-1 phosphorylation (PubMed:15066285).
CC The interaction also leads to the subsequent nuclear export of pop-1
CC (PubMed:15066285). Interacts (when phosphorylated on Ser-118 and Ser-
CC 127) with lit-1; the interaction is dependent on the beta-catenin-lit-1
CC complex (PubMed:10380924, PubMed:15066285). Interacts with wrm-1
CC (PubMed:10380924). Interacts with homeobox protein egl-5.
CC {ECO:0000269|PubMed:10380924, ECO:0000269|PubMed:10952315,
CC ECO:0000269|PubMed:11742996, ECO:0000269|PubMed:15066285,
CC ECO:0000269|PubMed:20553900}.
CC -!- INTERACTION:
CC Q10666; Q18825: bar-1; NbExp=6; IntAct=EBI-317870, EBI-2528850;
CC Q10666; O17670: eya-1; NbExp=4; IntAct=EBI-317870, EBI-311862;
CC Q10666; O17695: hda-1; NbExp=3; IntAct=EBI-317870, EBI-318045;
CC Q10666; O18214: mab-3; NbExp=3; IntAct=EBI-317870, EBI-2420993;
CC Q10666; P41932: par-5; NbExp=2; IntAct=EBI-317870, EBI-318108;
CC Q10666; Q9XVI2: sys-1; NbExp=6; IntAct=EBI-317870, EBI-3871339;
CC Q10666; Q9XVD5: tbx-38; NbExp=3; IntAct=EBI-317870, EBI-2413404;
CC Q10666; Q18694: unc-130; NbExp=3; IntAct=EBI-317870, EBI-2414897;
CC Q10666; O02482: unc-37; NbExp=3; IntAct=EBI-317870, EBI-314716;
CC Q10666; Q9NAE4: zip-7; NbExp=3; IntAct=EBI-317870, EBI-332523;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:10380924, ECO:0000269|PubMed:15649465,
CC ECO:0000269|PubMed:19427847, ECO:0000269|PubMed:25569233,
CC ECO:0000269|PubMed:31740621}. Cytoplasm {ECO:0000269|PubMed:10380924}.
CC Note=Predominantly nuclear, but is exported out of the nucleus and into
CC the cytoplasm upon lit-1-mediated phosphorylation (PubMed:10380924,
CC PubMed:15066285). Soon after the nuclei reform in telophase, pop-1
CC levels decrease in the posterior nucleus, in contrast to the anterior
CC nucleus. There is a ~2-fold nuclear enrichment of pop-1 in the anterior
CC compared with posterior daughter cells at the time of cytokinesis.
CC {ECO:0000269|PubMed:10380924, ECO:0000269|PubMed:15066285,
CC ECO:0000269|PubMed:31740621}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically
CC (PubMed:10380924). Expressed in the first 32 daughter cells of the MS
CC blastomere cell, and in the 8-cell stage ABar blastomere and
CC subsequently, asymmetrically in its descendants (PubMed:12810601).
CC Expression is higher in the anterior daughters of dividing cells, but
CC lower in the posterior daughters (PubMed:12810601, PubMed:10380924).
CC Expressed asymmetrically in vulva precursor cells P5.p, P6.p and P7.p
CC at L2 larval stage and in their descendants (PubMed:15649465).
CC Expressed asymmetrically in somatic gonadal precursor cells Z1.p, Z4.a,
CC Z1.a and Z4.p (PubMed:25569233). During M-lineage cell fate
CC specification, expressed evenly from 1-M to 4-M stages followed by
CC asymmetric expression in anterior cells at the 8-M, 16-M and 18-M
CC stages (PubMed:19427847). Expressed asymmetrically in seam cells at
CC larval stages L2 and L3. {ECO:0000269|PubMed:10380924,
CC ECO:0000269|PubMed:12810601, ECO:0000269|PubMed:15649465,
CC ECO:0000269|PubMed:19427847, ECO:0000269|PubMed:25569233,
CC ECO:0000269|PubMed:31740621}.
CC -!- PTM: Phosphorylated on Ser-118 and Ser-127 by lit-1 in the beta-
CC catenin-lit-1 complex (PubMed:10380924, PubMed:15066285).
CC Phosphorylation promotes the interaction of pop-1 and par-5 and the
CC subsequent translocation of pop-1 from the nucleus to the cytoplasm
CC (PubMed:10380924, PubMed:15066285). {ECO:0000269|PubMed:10380924,
CC ECO:0000269|PubMed:15066285}.
CC -!- DISRUPTION PHENOTYPE: Knockout specifically targeted at seam cells
CC causes an increase in seam cell number, but this is caused by a
CC combination of anterior daughter cells adopting the seam fate, and
CC abnormal differentiation of posterior seam cells (PubMed:31740621).
CC RNAi-mediated knockdown also increases the number of seam cells as a
CC result of anterior daughter cells failing to differentiate and adopting
CC the seam fate (PubMed:31740621). RNAi-mediated knockdown in L1 larvae
CC causes a severe loss of M lineage-derived coelomocytes and sex
CC myoblasts (PubMed:19427847). The loss of sex myoblasts is due to a fate
CC transformation of M.v(l/r)pa cell to the fate of its posterior sister
CC M.v(l/r)pp cell (PubMed:19427847). The loss of coelomocytes is due to a
CC combination of reduced proliferation of the dorsal M lineage and fate
CC transformation of M.d(l/r)pa cell to the fate of its posterior sister
CC M.d(l/r)pp cell (PubMed:19427847). Loss of ceh-34 expression in the M
CC lineage (PubMed:19427847). {ECO:0000269|PubMed:19427847,
CC ECO:0000269|PubMed:31740621}.
CC -!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
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DR EMBL; U37532; AAC05308.1; -; mRNA.
DR EMBL; BX284601; CCD73394.2; -; Genomic_DNA.
DR PIR; A57667; A57667.
DR PIR; C87732; C87732.
DR PIR; T32931; T32931.
DR RefSeq; NP_491053.4; NM_058652.3.
DR PDB; 3C2G; X-ray; 2.50 A; C/D=8-15.
DR PDBsum; 3C2G; -.
DR AlphaFoldDB; Q10666; -.
DR SMR; Q10666; -.
DR BioGRID; 37329; 66.
DR DIP; DIP-25683N; -.
DR IntAct; Q10666; 50.
DR STRING; 6239.W10C8.2; -.
DR iPTMnet; Q10666; -.
DR EPD; Q10666; -.
DR PaxDb; Q10666; -.
DR PeptideAtlas; Q10666; -.
DR EnsemblMetazoa; W10C8.2.1; W10C8.2.1; WBGene00004077.
DR GeneID; 171849; -.
DR KEGG; cel:CELE_W10C8.2; -.
DR UCSC; W10C8.2; c. elegans.
DR CTD; 171849; -.
DR WormBase; W10C8.2; CE46967; WBGene00004077; pop-1.
DR eggNOG; KOG3248; Eukaryota.
DR GeneTree; ENSGT00940000168653; -.
DR HOGENOM; CLU_625901_0_0_1; -.
DR InParanoid; Q10666; -.
DR OMA; RCLWYRE; -.
DR OrthoDB; 807716at2759; -.
DR Reactome; R-CEL-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-CEL-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-CEL-4086398; Ca2+ pathway.
DR Reactome; R-CEL-4641265; Repression of WNT target genes.
DR Reactome; R-CEL-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-CEL-8951430; RUNX3 regulates WNT signaling.
DR SignaLink; Q10666; -.
DR EvolutionaryTrace; Q10666; -.
DR PRO; PR:Q10666; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004077; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:WormBase.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:WormBase.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB.
DR GO; GO:0008356; P:asymmetric cell division; IMP:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:WormBase.
DR GO; GO:0001709; P:cell fate determination; IMP:UniProtKB.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:UniProtKB.
DR GO; GO:0035262; P:gonad morphogenesis; IMP:UniProtKB.
DR GO; GO:0007500; P:mesodermal cell fate determination; IMP:WormBase.
DR GO; GO:0007501; P:mesodermal cell fate specification; IMP:UniProtKB.
DR GO; GO:0051782; P:negative regulation of cell division; IMP:UniProtKB.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0043282; P:pharyngeal muscle development; IMP:WormBase.
DR GO; GO:0010085; P:polarity specification of proximal/distal axis; IGI:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0040026; P:positive regulation of vulval development; IMP:WormBase.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IGI:WormBase.
DR GO; GO:0042659; P:regulation of cell fate specification; IGI:WormBase.
DR GO; GO:2000746; P:regulation of defecation rhythm; IMP:WormBase.
DR GO; GO:0061853; P:regulation of neuroblast migration; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:WormBase.
DR GO; GO:0016055; P:Wnt signaling pathway; TAS:UniProtKB.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR028782; Pangolin-like.
DR InterPro; IPR024940; TCF/LEF.
DR PANTHER; PTHR10373; PTHR10373; 1.
DR PANTHER; PTHR10373:SF38; PTHR10373:SF38; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; Developmental protein; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..438
FT /note="Protein pop-1"
FT /id="PRO_0000048603"
FT DNA_BIND 192..262
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..130
FT /note="Involved in nuclear asymmetry"
FT REGION 250..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..419
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 118
FT /note="Phosphoserine; by LIT1"
FT /evidence="ECO:0000269|PubMed:15066285"
FT MOD_RES 127
FT /note="Phosphoserine; by LIT1"
FT /evidence="ECO:0000269|PubMed:15066285"
FT MUTAGEN 9
FT /note="D->E: In q645; abnormal gonad development and
FT hermaphrodites are sterile. Formation of ectopic M lineage-
FT derived coelomocytes on the dorsal side and ectopic sex
FT myoblast on the ventral side. Simultaneous RNAi-mediated
FT knockdown of ceh-34 causes a loss of all M lineage-derived
FT coelomocytes."
FT /evidence="ECO:0000269|PubMed:11807036,
FT ECO:0000269|PubMed:19427847"
FT MUTAGEN 107
FT /note="S->A: Abolishes nuclear asymmetry, defective in
FT nuclear export and loss of par-5 interaction; when
FT associated with A-109; A-118; T-120 and A-127."
FT /evidence="ECO:0000269|PubMed:15066285"
FT MUTAGEN 109
FT /note="S->A: Abolishes nuclear asymmetry, defective in
FT nuclear export and loss of par-5 interaction; when
FT associated with A-107; A-118; T-120 and A-127."
FT /evidence="ECO:0000269|PubMed:15066285"
FT MUTAGEN 118
FT /note="S->A: Abolishes nuclear asymmetry, defective in
FT nuclear export and loss of par-5 interaction; when
FT associated with A-107; A-109; T-120 and A-127."
FT /evidence="ECO:0000269|PubMed:15066285"
FT MUTAGEN 120
FT /note="T->A: Abolishes nuclear asymmetry, defective in
FT nuclear export and loss of par-5 interaction; when
FT associated with A-107; A-109; A-118 and A-127."
FT /evidence="ECO:0000269|PubMed:15066285"
FT MUTAGEN 127
FT /note="S->A: Abolishes nuclear asymmetry, defective in
FT nuclear export and loss of par-5 interaction; when
FT associated with A-107; A-109; A-118 and A-120."
FT /evidence="ECO:0000269|PubMed:15066285"
FT MUTAGEN 225
FT /note="N->I: In q624; low penetrance defects including
FT abnormal gonad development, L1 viability and T-cell
FT defects. Severe loss of M lineage-derived coelomocytes and
FT sex myoblasts."
FT /evidence="ECO:0000269|PubMed:11807036,
FT ECO:0000269|PubMed:19427847"
FT CONFLICT 200
FT /note="M -> V (in Ref. 1; AAC05308)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 48627 MW; 494078BE40B40E2E CRC64;
MMADEELGDE VKVFRRDEDA DDDPMISGET SEQQLADDKK EAVMEAELDG AGRNPSIDVL
KSAFPKVEPM SPSFPGLMSH FSPGYSAAAL PMFMPLFMNP YAAALRSPSL MFPMGAMSPT
FPMFPPSPVY GAAIAAAAAK QHFENMAPLN MRAGHPMNQM GMPPYMHPSS MAPQNVDRRA
QGGGKAKKDD HVKKPLNAFM WFMKENRKAL LEEIGNNEKQ SAELNKELGK RWHDLSKEEQ
AKYFEMAKKD KETHKERYPE WSARENYAVN KKKTKKRRDK SIPSENNDQK KCRARFGVNN
TEMWCKFCKR KKKCEYATDR SGGSDITDSQ DGRGTSGAYS SSSESPSPKA NAGIALTTQQ
QQAAMMHTML MQMRLGSTTG ASTHVPSPLA SSSAGRSPLD ANASDSESDV EEEEDEQIDP
TVMQQTHDML MQESMCTI
