MEI3A_XENLA
ID MEI3A_XENLA Reviewed; 453 AA.
AC Q5U4X3; Q9YGY1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Homeobox protein meis3-A {ECO:0000250|UniProtKB:Q99687, ECO:0000312|EMBL:AAH84920.1};
DE Short=XMeis3 {ECO:0000250|UniProtKB:Q99687, ECO:0000303|PubMed:10096059, ECO:0000303|PubMed:11566848};
GN Name=meis3-a; Synonyms=meis3 {ECO:0000312|EMBL:AAH84920.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD02948.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=10096059; DOI=10.1016/s0925-4773(98)00187-7;
RA Salzberg A., Elias S., Nachaliel N., Bonstein L., Henig C., Frank D.;
RT "A Meis family protein caudalizes neural cell fates in Xenopus.";
RL Mech. Dev. 80:3-13(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH84920.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAH84920.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=11566847; DOI=10.1242/dev.128.18.3405;
RA Inbal A., Halachmi N., Dibner C., Frank D., Salzberg A.;
RT "Genetic evidence for the transcriptional-activating function of Homothorax
RT during adult fly development.";
RL Development 128:3405-3413(2001).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=11566848; DOI=10.1242/dev.128.18.3415;
RA Dibner C., Elias S., Frank D.;
RT "XMeis3 protein activity is required for proper hindbrain patterning in
RT Xenopus laevis embryos.";
RL Development 128:3415-3426(2001).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=14660437; DOI=10.1242/dev.00905;
RA Aamar E., Frank D.;
RT "Xenopus Meis3 protein forms a hindbrain-inducing center by activating
RT FGF/MAP kinase and PCP pathways.";
RL Development 131:153-163(2004).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=15196951; DOI=10.1016/j.ydbio.2004.02.029;
RA Dibner C., Elias S., Ofir R., Souopgui J., Kolm P.J., Sive H.L., Pieler T.,
RA Frank D.;
RT "The Meis3 protein and retinoid signaling interact to pattern the Xenopus
RT hindbrain.";
RL Dev. Biol. 271:75-86(2004).
CC -!- FUNCTION: Caudalizing protein which is required to pattern the
CC anterior/posterior (A/P) axis during central nervous system (CNS)
CC formation. Inhibits anterior neural expression and acts as a
CC transcriptional activator to induce posterior neural gene expression.
CC Maintains a proper A/P balance required for hindbrain formation by
CC activating the FGF/MAPK pathway, which modulates the planar cell
CC polarity (PCP) pathway. Interacts with retinoid signaling during
CC hindbrain patterning. {ECO:0000269|PubMed:10096059,
CC ECO:0000269|PubMed:11566847, ECO:0000269|PubMed:11566848,
CC ECO:0000269|PubMed:14660437, ECO:0000269|PubMed:15196951}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5U4X3-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10096059};
CC IsoId=Q5U4X3-2; Sequence=VSP_052972, VSP_052973;
CC -!- TISSUE SPECIFICITY: In early-mid neurula stages, expressed in a single
CC stripe in the neural plate. By neurula/early-tailbud stages, expression
CC is localized to rhombomeres r2, r3 and r4 and the anterior spinal cord.
CC Some ventral expression was also detected in posterior rhombomeres. Not
CC expressed in rhombomere r1. {ECO:0000269|PubMed:10096059}.
CC -!- DEVELOPMENTAL STAGE: Initially expressed at gastrula stages. Expression
CC peaks at neurula stage, and is maintained at stable levels through
CC tailbud stages. {ECO:0000269|PubMed:10096059}.
CC -!- SIMILARITY: Belongs to the TALE/MEIS homeobox family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD02948.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF072895; AAD02948.1; ALT_FRAME; mRNA.
DR EMBL; BC084920; AAH84920.1; -; mRNA.
DR RefSeq; NP_001081866.1; NM_001088397.1. [Q5U4X3-1]
DR RefSeq; XP_018084193.1; XM_018228704.1. [Q5U4X3-1]
DR RefSeq; XP_018084194.1; XM_018228705.1. [Q5U4X3-2]
DR AlphaFoldDB; Q5U4X3; -.
DR SMR; Q5U4X3; -.
DR DNASU; 398093; -.
DR GeneID; 398093; -.
DR KEGG; xla:398093; -.
DR CTD; 398093; -.
DR Xenbase; XB-GENE-6252025; meis3.L.
DR OMA; HSERPLF; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; IMP:UniProtKB.
DR GO; GO:0030902; P:hindbrain development; IMP:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR008422; Homeobox_KN_domain.
DR InterPro; IPR032453; PKNOX/Meis_N.
DR Pfam; PF05920; Homeobox_KN; 1.
DR Pfam; PF16493; Meis_PKNOX_N; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; Developmental protein; Differentiation;
KW DNA-binding; Homeobox; Neurogenesis; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..453
FT /note="Homeobox protein meis3-A"
FT /id="PRO_0000355571"
FT DOMAIN 102..185
FT /note="MEIS N-terminal"
FT /evidence="ECO:0000255"
FT DNA_BIND 267..329
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 37..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 368..385
FT /note="FQGIPGDYTAAPSTMPMG -> AMGGLGMAVGMEGQWHYM (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:10096059"
FT /id="VSP_052972"
FT VAR_SEQ 386..453
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10096059"
FT /id="VSP_052973"
FT CONFLICT 211
FT /note="R -> Q (in Ref. 1; AAD02948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 49116 MW; C3197177D530A8FE CRC64;
MAQRYDEMLH YPTLDGMPLA GFGDAHTGRA LQHHSLSQSA PYGSTGAGHR VPMPPGMGSN
DGLKREKDEI YGHPLFPLLA LVFEKCELAT CSPRDNSGSF PGGDVCSSDS FNEDIAVFAK
QVRTEKPLFS SNPELDSLMI QAIQVLRFHL LELEKVHDLC DNFCHRYITC LKGKMPIDLV
IDDRDGSSKS DLEDFTGSCT SLSDQNNSWL RDHDETGSAH SGTPGPSSGG LASQSGDNSS
EQGDCMDNSV ASPSTGDDDD LDRDKKRNKK RGIFPKVATN IMRAWLFQHL SHPYPSEEQK
KQLAQDTGLT ILQVNNWFIN ARRRIVQPMI DQSNRTGQGG APYSPDGQNM GGYVMDGQQH
MGIRPPGFQG IPGDYTAAPS TMPMGFPPAG YTPAIPPHSA GLRHGPSLHS YLPGHPHHAS
MILPAGASPH HLVSAQSPAD ALLNGQNIDI HAH
