ID PITX2_MOUSE Reviewed; 317 AA. AC P97474; O08646; O70336; P97933; Q9JLA0; Q9QXB8; Q9R1V9; Q9Z141; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 29-MAY-2024, entry version 197. DE RecName: Full=Pituitary homeobox 2 {ECO:0000305}; DE AltName: Full=ALL1-responsive protein ARP1 {ECO:0000303|PubMed:9539779}; DE AltName: Full=BRX1 homeoprotein; DE AltName: Full=Bicoid-related homeobox protein 1 {ECO:0000303|PubMed:9347917}; DE AltName: Full=Homeobox protein PITX2; DE AltName: Full=Orthodenticle-like homeobox 2; DE AltName: Full=Paired-like homeodomain transcription factor 2; DE AltName: Full=Solurshin {ECO:0000303|PubMed:8944018}; GN Name=Pitx2 {ECO:0000312|MGI:MGI:109340}; GN Synonyms=Arp1 {ECO:0000303|PubMed:9539779}, GN Brx1 {ECO:0000303|PubMed:9347917}, Otlx2, GN Ptx2 {ECO:0000303|PubMed:9147650}, Rgs, Rieg {ECO:0000303|PubMed:8944018}; 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] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PTX2A). RA Mucchielli M.L., Martinez S., Pattyn A., Goridis C., Brunet J.-F.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PTX2A AND PTX2B), TISSUE SPECIFICITY, RP AND DEVELOPMENTAL STAGE. RC TISSUE=Pituitary; RX PubMed=9147650; DOI=10.1093/hmg/6.3.457; RA Gage P.J., Camper S.A.; RT "Pituitary homeobox 2, a novel member of the bicoid-related family of RT homeobox genes, is a potential regulator of anterior structure formation."; RL Hum. Mol. Genet. 6:457-464(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PTX2B AND PTX2C), AND DEVELOPMENTAL RP STAGE. RX PubMed=9347917; DOI=10.1016/s0925-4773(97)00110-x; RA Kitamura K., Miura H., Yanazawa M., Miyashita T., Kato K.; RT "Expression patterns of Brx1 (Rieg gene), Sonic hedgehog, Nkx2.2, Dlx1 and RT Arx during zona limitans intrathalamica and embryonic ventral lateral RT geniculate nuclear formation."; RL Mech. Dev. 67:83-96(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PTX2A AND PTX2C), AND DEVELOPMENTAL RP STAGE. RX PubMed=9539779; DOI=10.1073/pnas.95.8.4573; RA Arakawa H., Nakamura T., Zhadanov A.B., Fidanza Y., Yano T., Bullrich F., RA Shimizu M., Blechman J., Mazo A., Canaani E., Croce C.M.; RT "Identification and characterization of the ARP1 gene, a target for the RT human acute leukemia ALL1 gene."; RL Proc. Natl. Acad. Sci. U.S.A. 95:4573-4578(1998). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-61 (ISOFORM PTX2C), FUNCTION, AND RP DEVELOPMENTAL STAGE. RX PubMed=10585561; DOI=10.1016/s0925-4773(99)00227-0; RA Schweickert A., Campione M., Steinbeisser H., Blum M.; RT "Pitx2 isoforms: involvement of Pitx2c but not Pitx2a or Pitx2b in RT vertebrate left-right asymmetry."; RL Mech. Dev. 90:41-51(2000). RN [6] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PTX2C), AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX PubMed=11319841; DOI=10.1006/cbir.2000.0638; RA Nicholson L.F.B., Ma L., Goulding M.; RT "Cloning and expression of Munc 30: a member of the paired-like homeodomain RT gene family."; RL Cell Biol. Int. 25:351-365(2001). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 63-317, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryonic carcinoma; RX PubMed=8944018; DOI=10.1038/ng1296-392; RA Semina E.V., Reiter R., Leysens N.J., Alward W.L.M., Small K.W., RA Datson N.A., Siegle-Bartelt J., Bierke-Nelson D., Bitoun P., Zabel B.U., RA Carey J.C., Murray J.C.; RT "Cloning and characterization of a novel bicoid-related homeobox RT transcription factor gene, RIEG, involved in Rieger syndrome."; RL Nat. Genet. 14:392-399(1996). RN [8] RP ALTERNATIVE SPLICING (ISOFORM PITX2CALPHA) AND ALTERNATIVE INITIATION RP (ISOFORM PITX2CBETA). RA Lamba P., Hjalt T.A., Bernard D.J.; RT "Novel forms of paired-like homeodomain transcription factor 2 (PITX2): RT generation by alternative translation initiation and mRNA splicing."; RL Unpublished observations (JAN-2008). RN [9] RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND INDUCTION BY RP CITED2; TFAP2A AND TFAP2C. RX PubMed=15475956; DOI=10.1038/ng1446; RA Bamforth S.D., Braganca J., Farthing C.R., Schneider J.E., Broadbent C., RA Michell A.C., Clarke K., Neubauer S., Norris D., Brown N.A., Anderson R.H., RA Bhattacharya S.; RT "Cited2 controls left-right patterning and heart development through a RT Nodal-Pitx2c pathway."; RL Nat. Genet. 36:1189-1196(2004). RN [10] RP PHOSPHORYLATION AT THR-90, FUNCTION, MUTAGENESIS OF THR-90, SUBCELLULAR RP LOCATION, AND INTERACTION WITH ELAVL1. RX PubMed=20019746; DOI=10.1038/cdd.2009.194; RA Gherzi R., Trabucchi M., Ponassi M., Gallouzi I.E., Rosenfeld M.G., RA Briata P.; RT "Akt2-mediated phosphorylation of Pitx2 controls Ccnd1 mRNA decay during RT muscle cell differentiation."; RL Cell Death Differ. 17:975-983(2010). CC -!- FUNCTION: May play a role in myoblast differentiation. When CC unphosphorylated, associates with an ELAVL1-containing complex, which CC stabilizes cyclin mRNA and ensuring cell proliferation. Phosphorylation CC by AKT2 impairs this association, leading to CCND1 mRNA destabilization CC and progression towards differentiation. {ECO:0000269|PubMed:20019746}. CC -!- FUNCTION: [Isoform Ptx2c]: Involved in the establishment of left-right CC asymmetry in the developing embryo. {ECO:0000269|PubMed:10585561}. CC -!- SUBUNIT: Interacts with EFEMP2 (By similarity). Interacts (when CC unphosphorylated on Thr-90) with ELAVL1/HUR (PubMed:20019746). CC {ECO:0000250|UniProtKB:Q99697, ECO:0000269|PubMed:20019746}. CC -!- INTERACTION: CC P97474; Q60795: Nfe2l2; NbExp=2; IntAct=EBI-1175125, EBI-642563; CC P97474; P46938: Yap1; NbExp=2; IntAct=EBI-1175125, EBI-1211949; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm CC {ECO:0000269|PubMed:20019746}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=5; CC Name=Ptx2b {ECO:0000303|PubMed:9147650}; Synonyms=ARP1B, Brx1b CC {ECO:0000303|PubMed:9347917}, Pitx2c {ECO:0000303|PubMed:15475956}; CC IsoId=P97474-1; Sequence=Displayed; CC Name=Ptx2c {ECO:0000303|PubMed:10585561}; Synonyms=ARP1c CC {ECO:0000303|PubMed:9539779}, Brx1a {ECO:0000303|PubMed:9347917}, CC Munc30 {ECO:0000303|PubMed:11319841}; CC IsoId=P97474-2; Sequence=VSP_002262; CC Name=Ptx2a {ECO:0000303|PubMed:9147650}; Synonyms=ARP1a CC {ECO:0000303|PubMed:9539779}; CC IsoId=P97474-3; Sequence=VSP_002263; CC Name=Pitx2Calpha; CC IsoId=P97474-4; Sequence=VSP_031522; CC Name=Pitx2Cbeta; CC IsoId=P97474-5; Sequence=VSP_031521; CC -!- TISSUE SPECIFICITY: Expressed in pituitary gland, brain, heart, kidney, CC eye, lung, testis, tongue, spinal cord and skeletal muscle. CC {ECO:0000269|PubMed:11319841, ECO:0000269|PubMed:9147650}. CC -!- DEVELOPMENTAL STAGE: Detected as early as 8.5 dpc (PubMed:9147650). At CC 9.5 dpc, detected in ectodermal cells in first branchial arch, CC ventrolateral dermomyotome of early somites and neural tissues CC (PubMed:9539779). In the developing brain, at 9.5-11.5 dpc, expressed CC in the ventral diencephalon and zona limitans intrathalamica (ZLI), as CC well as in the lateral plate mesenchyme, mandibular and maxillary CC epithelium and the vitelline and umbilical vessels (PubMed:8944018, CC PubMed:9347917). At 11.5 dpc, also detected in the mesenchyme around CC the eye, Rathke's pouch, the dental lamina, the limb mesenchyme and the CC dorsal mesentery (PubMed:8944018). At 12.5 dpc, detected in the ZLI and CC in the mammillary area, as well as in Rathke's pouch. At 14.5 dpc, CC expressed in early ventral lateral geniculate nucleus. At 18.5 dpc, CC expressed along the anterioposterior axis in the ventral lateral CC geniculate nucleus (PubMed:9347917). {ECO:0000269|PubMed:8944018, CC ECO:0000269|PubMed:9147650, ECO:0000269|PubMed:9347917, CC ECO:0000269|PubMed:9539779}. CC -!- DEVELOPMENTAL STAGE: [Isoform Ptx2c]: At 8.5 dpc, expressed CC asymmetrically in the left lateral plate mesoderm and symmetrically in CC the head mesoderm (PubMed:10585561, PubMed:15475956). At 13.5 dpc, CC expressed in the heart, in the left atrium and right ventricle. At this CC stage, also expressed in the gastro-intestinal tract, in the left side CC of the stomach, the cecum, the small intestine and the superior CC mesenteric artery (PubMed:10585561). In the developing heart, at 15.5 CC dpc, expressed in the ventral aspects of the outflow tract region and CC of the right ventricle and also in the left atrium (PubMed:15475956). CC {ECO:0000269|PubMed:10585561, ECO:0000269|PubMed:15475956}. CC -!- INDUCTION: Expression is activated by CITED2 and TFAP2A and TFAP2C. CC {ECO:0000269|PubMed:15475956}. CC -!- PTM: Phosphorylated at Thr-90 by AKT2, but not AKT1. Phosphorylation CC impairs its association with a CCND1 mRNA-stabilizing complex, thus CC shortening the half-life of CCND1. {ECO:0000269|PubMed:20019746}. CC -!- DISRUPTION PHENOTYPE: [Isoform Ptx2c]: Knockout embryos exhibit cardiac CC and laterality defects. Embryos have defects in the aortic arch CC vessels, such as double-outlet right ventricle and right-sided or CC double aortic arches. Most have bilateral, left-sided or midline CC inferior caval veins, right atrial and pulmonary isomerism. None have CC abnormal ventricular topology, but some have malposition of the heart CC to the right and the hearts of the remaining embryos are in the midline CC rather than to the left. In addition, most embryos have ventricular CC septal defects with associated double-outlet right ventricle. Some CC embryos show right-sided aortic arches and some have right-sided CC stomachs or, in one case, a midline stomach. The spleen is absent or CC small. Unlike mice lacking all Pitx2 isoforms, Pitx2c-specific knockout CC embryos have no defects in ventral body wall closure. CC {ECO:0000269|PubMed:15475956}. CC -!- MISCELLANEOUS: [Isoform Pitx2Cbeta]: Produced by alternative initiation CC at Met-35 of isoform Ptx2C. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the paired homeobox family. Bicoid subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF44618.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; U80036; AAB38505.1; -; mRNA. DR EMBL; U80010; AAC53119.1; -; mRNA. DR EMBL; U80011; AAC53120.1; -; mRNA. DR EMBL; AB006320; BAA75247.1; -; mRNA. DR EMBL; AB006321; BAA75248.1; -; mRNA. DR EMBL; AF048723; AAC40086.1; -; mRNA. DR EMBL; AF048724; AAC40087.1; -; mRNA. DR EMBL; AJ243597; CAB65259.1; -; mRNA. DR EMBL; AF201091; AAF44618.1; ALT_INIT; mRNA. DR EMBL; U70132; AAB38864.1; -; mRNA. DR CCDS; CCDS17830.1; -. [P97474-1] DR CCDS; CCDS38630.1; -. [P97474-3] DR CCDS; CCDS38631.1; -. [P97474-2] DR CCDS; CCDS71316.1; -. [P97474-4] DR RefSeq; NP_001035967.1; NM_001042502.2. [P97474-2] DR RefSeq; NP_001035969.1; NM_001042504.2. [P97474-3] DR RefSeq; NP_035228.2; NM_011098.4. [P97474-1] DR RefSeq; XP_006501194.1; XM_006501131.3. [P97474-1] DR RefSeq; XP_006501195.1; XM_006501132.2. [P97474-3] DR RefSeq; XP_006501196.1; XM_006501133.1. [P97474-3] DR AlphaFoldDB; P97474; -. DR BMRB; P97474; -. DR BioGRID; 202187; 3. DR DIP; DIP-37454N; -. DR IntAct; P97474; 3. DR STRING; 10090.ENSMUSP00000047359; -. DR iPTMnet; P97474; -. DR PhosphoSitePlus; P97474; -. DR PaxDb; 10090-ENSMUSP00000047359; -. DR ProteomicsDB; 289582; -. [P97474-1] DR ProteomicsDB; 289583; -. [P97474-2] DR ProteomicsDB; 289584; -. [P97474-3] DR ProteomicsDB; 289585; -. [P97474-4] DR ProteomicsDB; 289586; -. [P97474-5] DR DNASU; 18741; -. DR Ensembl; ENSMUST00000042587.12; ENSMUSP00000047359.10; ENSMUSG00000028023.17. [P97474-2] DR Ensembl; ENSMUST00000106382.11; ENSMUSP00000101990.5; ENSMUSG00000028023.17. [P97474-3] DR Ensembl; ENSMUST00000172645.8; ENSMUSP00000134692.2; ENSMUSG00000028023.17. [P97474-4] DR Ensembl; ENSMUST00000174661.9; ENSMUSP00000133756.2; ENSMUSG00000028023.17. [P97474-1] DR GeneID; 18741; -. DR KEGG; mmu:18741; -. DR UCSC; uc008rhu.2; mouse. [P97474-1] DR UCSC; uc008rhv.2; mouse. [P97474-3] DR AGR; MGI:109340; -. DR CTD; 5308; -. DR MGI; MGI:109340; Pitx2. DR VEuPathDB; HostDB:ENSMUSG00000028023; -. DR eggNOG; KOG0486; Eukaryota. DR GeneTree; ENSGT00940000154518; -. DR HOGENOM; CLU_030301_0_0_1; -. DR InParanoid; P97474; -. DR OMA; MNCLKEP; -. DR OrthoDB; 5395268at2759; -. DR PhylomeDB; P97474; -. DR TreeFam; TF351940; -. DR BioGRID-ORCS; 18741; 4 hits in 81 CRISPR screens. DR ChiTaRS; Pitx2; mouse. DR PRO; PR:P97474; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; P97474; Protein. DR Bgee; ENSMUSG00000028023; Expressed in calcareous tooth and 281 other cell types or tissues. DR ExpressionAtlas; P97474; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:0009653; P:anatomical structure morphogenesis; IMP:MGI. DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI. DR GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; IMP:MGI. DR GO; GO:0003171; P:atrioventricular valve development; IMP:MGI. DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI. DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI. DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:MGI. DR GO; GO:0003253; P:cardiac neural crest cell migration involved in outflow tract morphogenesis; IMP:BHF-UCL. DR GO; GO:0061325; P:cell proliferation involved in outflow tract morphogenesis; IMP:MGI. DR GO; GO:0035993; P:deltoid tuberosity development; IMP:BHF-UCL. DR GO; GO:0007368; P:determination of left/right symmetry; IMP:BHF-UCL. DR GO; GO:0055123; P:digestive system development; IMP:MGI. DR GO; GO:0031076; P:embryonic camera-type eye development; IMP:MGI. DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:MGI. DR GO; GO:0060971; P:embryonic heart tube left/right pattern formation; IMP:BHF-UCL. DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IGI:MGI. DR GO; GO:0061031; P:endodermal digestive tract morphogenesis; IMP:MGI. DR GO; GO:0002074; P:extraocular skeletal muscle development; IMP:MGI. DR GO; GO:0008585; P:female gonad development; IEA:Ensembl. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0021855; P:hypothalamus cell migration; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0060460; P:left lung morphogenesis; IMP:MGI. DR GO; GO:0070986; P:left/right axis specification; IMP:BHF-UCL. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0008584; P:male gonad development; IEA:Ensembl. DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl. DR GO; GO:0001764; P:neuron migration; IMP:MGI. DR GO; GO:0042476; P:odontogenesis; IMP:MGI. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl. DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL. DR GO; GO:0021983; P:pituitary gland development; IMP:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0003350; P:pulmonary myocardium development; IMP:MGI. DR GO; GO:0060577; P:pulmonary vein morphogenesis; IMP:MGI. DR GO; GO:0030334; P:regulation of cell migration; IMP:MGI. DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0009725; P:response to hormone; IEA:Ensembl. DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl. DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI. DR GO; GO:0048536; P:spleen development; IMP:BHF-UCL. DR GO; GO:0021763; P:subthalamic nucleus development; IMP:MGI. DR GO; GO:0060578; P:superior vena cava morphogenesis; IMP:MGI. DR GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; IMP:MGI. DR GO; GO:0001570; P:vasculogenesis; IMP:MGI. DR GO; GO:0055015; P:ventricular cardiac muscle cell development; IMP:MGI. DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:MGI. DR GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI. DR CDD; cd00086; homeodomain; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR017970; Homeobox_CS. DR InterPro; IPR001356; Homeobox_dom. DR InterPro; IPR016233; Homeobox_Pitx/unc30. DR InterPro; IPR003654; OAR_dom. DR PANTHER; PTHR45882:SF4; PITUITARY HOMEOBOX 2; 1. DR PANTHER; PTHR45882; PITUITARY HOMEOBOX HOMOLOG PTX1; 1. DR Pfam; PF00046; Homeodomain; 1. DR Pfam; PF03826; OAR; 1. DR PIRSF; PIRSF000563; Homeobox_protein_Pitx/Unc30; 1. DR SMART; SM00389; HOX; 1. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS50803; OAR; 1. PE 1: Evidence at protein level; KW Alternative initiation; Alternative splicing; Cytoplasm; KW Developmental protein; DNA-binding; Homeobox; Nucleus; Phosphoprotein; KW Reference proteome. FT CHAIN 1..317 FT /note="Pituitary homeobox 2" FT /id="PRO_0000049224" FT DNA_BIND 85..144 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 35..99 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 279..292 FT /note="OAR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00138" FT MOTIF 285..289 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 35..83 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 90 FT /note="Phosphothreonine; by PKB/AKT2" FT /evidence="ECO:0000269|PubMed:20019746" FT VAR_SEQ 1..61 FT /note="METNCRKLVSACVQLGVQPAAVECLFSKDSEIKKVEFTDSPKSRKESASSKL FT FPRQHPGAN -> MASVLAPGQPRSLDSSKHRLEVHTISDTSSPEVA (in isoform FT Pitx2Cbeta)" FT /evidence="ECO:0000305" FT /id="VSP_031521" FT VAR_SEQ 1..61 FT /note="METNCRKLVSACVQLGVQPAAVECLFSKDSEIKKVEFTDSPKSRKESASSKL FT FPRQHPGAN -> MNCMKGPLPLEHRAAGTKLSAASSPFCHHPQALAMASVLAPGQPRS FT LDSSKHRLEVHTISDTSSPEVA (in isoform Ptx2c)" FT /evidence="ECO:0000303|PubMed:9347917, FT ECO:0000303|PubMed:9539779" FT /id="VSP_002262" FT VAR_SEQ 16..61 FT /note="Missing (in isoform Ptx2a)" FT /evidence="ECO:0000303|PubMed:9147650, FT ECO:0000303|PubMed:9539779, ECO:0000303|Ref.1" FT /id="VSP_002263" FT VAR_SEQ 16..28 FT /note="Missing (in isoform Pitx2Calpha)" FT /evidence="ECO:0000305" FT /id="VSP_031522" FT MUTAGEN 90 FT /note="T->A: Loss of phosphorylation by AKT2." FT /evidence="ECO:0000269|PubMed:20019746" FT CONFLICT 187 FT /note="A -> T (in Ref. 3; BAA75247/BAA75248)" FT /evidence="ECO:0000305" SQ SEQUENCE 317 AA; 35321 MW; 188315708E6BD95D CRC64; METNCRKLVS ACVQLGVQPA AVECLFSKDS EIKKVEFTDS PKSRKESASS KLFPRQHPGA NEKDKGQQGK NEDVGAEDPS KKKRQRRQRT HFTSQQLQEL EATFQRNRYP DMSTREEIAV WTNLTEARVR VWFKNRRAKW RKRERNQQAE LCKNGFGPQF NGLMQPYDDM YPGYSYNNWA AKGLTSASLS TKSFPFFNSM NVNPLSSQSM FSPPNSISSM SMSSSMVPSA VTGVPGSSLN SLNNLNNLSS PSLNSAVPTP ACPYAPPTPP YVYRDTCNSS LASLRLKAKQ HSSFGYASVQ NPASNLSACQ YAVDRPV //