PAX2B_XENLA
ID PAX2B_XENLA Reviewed; 494 AA.
AC O57682; O57678; Q6AZQ6; Q9PUK6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Paired box protein Pax-2-B;
DE Short=xPax-2b;
GN Name=pax2-b; Synonyms=pax-2B;
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:CAA71206.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Embryonic head {ECO:0000312|EMBL:CAA71206.1}, and
RC Embryonic kidney {ECO:0000269|PubMed:9486533};
RX PubMed=9486533; DOI=10.1016/s0925-4773(97)00158-5;
RA Heller N., Braendli A.W.;
RT "Xenopus Pax-2 displays multiple splice forms during embryogenesis and
RT pronephric kidney development.";
RL Mech. Dev. 69:83-104(1997).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD52680.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo {ECO:0000269|PubMed:10491256};
RX PubMed=10491256; DOI=10.1006/dbio.1999.9414;
RA Carroll T.J., Vize P.D.;
RT "Synergism between Pax-8 and lim-1 in embryonic kidney development.";
RL Dev. Biol. 214:46-59(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH77463.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH77463.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=10322629;
RX DOI=10.1002/(sici)1520-6408(1999)24:3/4<208::aid-dvg4>3.0.co;2-j;
RA Heller N., Braendli A.W.;
RT "Xenopus Pax-2/5/8 orthologues: novel insights into Pax gene evolution and
RT identification of Pax-8 as the earliest marker for otic and pronephric cell
RT lineages.";
RL Dev. Genet. 24:208-219(1999).
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=15223346; DOI=10.1016/j.ydbio.2004.04.013;
RA Schlosser G., Ahrens K.;
RT "Molecular anatomy of placode development in Xenopus laevis.";
RL Dev. Biol. 271:439-466(2004).
RN [6] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=10322628;
RX DOI=10.1002/(sici)1520-6408(1999)24:3/4<199::aid-dvg3>3.0.co;2-d;
RA Carroll T.J., Wallingford J.B., Vize P.D.;
RT "Dynamic patterns of gene expression in the developing pronephros of
RT Xenopus laevis.";
RL Dev. Genet. 24:199-207(1999).
CC -!- FUNCTION: Probable transcription factor. Involved in kidney
CC development, acting synergistically with lhx1/lim-1 in pronephric
CC morphogenesis during the tailbud stages. {ECO:0000269|PubMed:10491256}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02962,
CC ECO:0000255|PROSITE-ProRule:PRU00381}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=12 {ECO:0000269|PubMed:10491256};
CC IsoId=O57682-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:9486533};
CC IsoId=O57682-2; Sequence=VSP_052441, VSP_052443;
CC Name=3; Synonyms=8 {ECO:0000269|PubMed:9486533};
CC IsoId=O57682-3; Sequence=VSP_052442, VSP_052443;
CC Name=4; Synonyms=11;
CC IsoId=O57682-4; Sequence=VSP_052441, VSP_052442, VSP_052443;
CC -!- TISSUE SPECIFICITY: Expression becomes spatially localized at mid-
CC gastrula stages and is localized to the nervous system (midbrain,
CC hindbrain, spinal cord), sensory organs (optic vesicle and stalk, otic
CC vesicle), visceral arches, developing excretory system (pronephros,
CC pronephric duct, rectal diverticulum, proctodaeum) and thryoid gland.
CC Splicing does not appear to be tissue-specific.
CC {ECO:0000269|PubMed:10322628, ECO:0000269|PubMed:10322629,
CC ECO:0000269|PubMed:10491256, ECO:0000269|PubMed:15223346,
CC ECO:0000269|PubMed:9486533}.
CC -!- DEVELOPMENTAL STAGE: Splicing is temporally regulated. Isoform 3 is
CC expressed both maternally and zygotically, whereas isoform 2 is
CC exclusively zygotic. Expression is highest in embryos from stage 12 on,
CC with expression levels remaining constant throughout embryogenesis.
CC {ECO:0000269|PubMed:9486533}.
CC -!- INDUCTION: By activin. Weakly by bFGF. {ECO:0000269|PubMed:9486533}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD52680.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y10120; CAA71206.1; -; mRNA.
DR EMBL; AJ000668; CAA04224.1; -; mRNA.
DR EMBL; AF179300; AAD52680.1; ALT_FRAME; mRNA.
DR EMBL; BC077463; AAH77463.1; -; mRNA.
DR RefSeq; XP_018083072.1; XM_018227583.1. [O57682-2]
DR AlphaFoldDB; O57682; -.
DR SMR; O57682; -.
DR GeneID; 108697493; -.
DR KEGG; xla:108697493; -.
DR OrthoDB; 592933at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 108697493; Expressed in kidney and 3 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0048793; P:pronephros development; IGI:UniProtKB.
DR GO; GO:0007367; P:segment polarity determination; IEA:UniProtKB-KW.
DR CDD; cd00131; PAX; 1.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR043182; PAIRED_DNA-bd_dom.
DR InterPro; IPR001523; Paired_dom.
DR InterPro; IPR022130; Pax2_C.
DR InterPro; IPR043565; PAX_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR45636; PTHR45636; 2.
DR Pfam; PF00292; PAX; 1.
DR Pfam; PF12403; Pax2_C; 2.
DR PRINTS; PR00027; PAIREDBOX.
DR SMART; SM00351; PAX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00034; PAIRED_1; 1.
DR PROSITE; PS51057; PAIRED_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; DNA-binding; Nucleus;
KW Paired box; Reference proteome; Segmentation polarity protein;
KW Transcription; Transcription regulation.
FT CHAIN 1..494
FT /note="Paired box protein Pax-2-B"
FT /id="PRO_0000289133"
FT DNA_BIND 15..141
FT /note="Paired"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT REGION 18..74
FT /note="PAI subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT REGION 93..141
FT /note="RED subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT REGION 142..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 15
FT /note="R -> PG (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9486533, ECO:0000303|Ref.3"
FT /id="VSP_052441"
FT VAR_SEQ 203..373
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9486533, ECO:0000303|Ref.3"
FT /id="VSP_052442"
FT VAR_SEQ 408..440
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9486533, ECO:0000303|Ref.3"
FT /id="VSP_052443"
SQ SEQUENCE 494 AA; 53038 MW; 7D319E30BF0C7B55 CRC64;
MDMHCKADPF SAMHRHGGVN QLGGVFVNGR PLPDVVRQRI VELAHQGVRP CDISRQLRVS
HGCVSKILGR YYETGSIKPG VIGGSKPKVA TPKVVDKIAD YKRQNPTMFA WEIRDRLLAE
GICDNDTVPS VSSINRIIRT KVQQPFHPTP DGTPVSTPGH TLVPSTASPP VSSASNDPVG
SYSINGILGI PRSNGEKRKR DEDGSDGSGP NGDSQSSVES LRKHLRADNF TQQQLEALDR
VFERPSYPDV FQSAEHIKSE QASEYSLPAL TPGLDEVKSS LSASGNADLG SNVSGPQSYP
VVTESFASHL YLKQEPHEAS LTPFTPSSLA SSGLADIQPF QMALTVDAST PTYSSFTHHG
PPYGQFGSQP LIAGRDMSST TLPGYPPHVP PTGQGSYPTS TLAGMVPGTN VSVHHSVQPV
ECCSCLSSSK PCLFHCRTGS GSEFSGNPYS HPQYTTYNEA WRFSNPALLS SPYYYSATSR
GSAPPTAATA YDRH
