PAX2A_XENLA
ID PAX2A_XENLA Reviewed; 497 AA.
AC O57685; O57677; O57680; O57681; O57684; Q7SZU4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Paired box protein Pax-2-A;
DE Short=xPax-2a;
GN Name=pax2-a; Synonyms=pax-2a {ECO:0000312|EMBL:CAA71208.1};
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:CAA71208.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Embryonic head {ECO:0000312|EMBL:CAA71207.1}, 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:AAH55960.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH55960.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {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 [4] {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).
CC -!- FUNCTION: Probable transcription factor. Involved in kidney
CC development, acting synergistically with lhx1/lim-1 in pronephric
CC morphogenesis during the tailbud stages (By similarity).
CC {ECO:0000250|UniProtKB:O57682}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02962,
CC ECO:0000255|PROSITE-ProRule:PRU00381}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=4 {ECO:0000269|PubMed:9486533};
CC IsoId=O57685-1; Sequence=Displayed;
CC Name=2; Synonyms=1 {ECO:0000269|PubMed:9486533};
CC IsoId=O57685-2; Sequence=VSP_052438, VSP_052439;
CC Name=3 {ECO:0000269|PubMed:9486533};
CC IsoId=O57685-3; Sequence=VSP_052438;
CC Name=4; Synonyms=5 {ECO:0000269|PubMed:9486533};
CC IsoId=O57685-4; Sequence=VSP_052435, VSP_052438, VSP_052439;
CC Name=5; Synonyms=7 {ECO:0000269|PubMed:9486533};
CC IsoId=O57685-5; Sequence=VSP_052437, VSP_052440;
CC Name=6; Synonyms=10;
CC IsoId=O57685-6; Sequence=VSP_052436, VSP_052439, VSP_052440;
CC -!- TISSUE SPECIFICITY: Expression becomes spatially localized at mid-
CC gastrula stages and is confined 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 thyroid gland.
CC Splicing does not appear to be tissue-specific and tissues displayed
CC the same spectrum of splice variants. {ECO:0000269|PubMed:10322629,
CC ECO:0000269|PubMed:15223346, ECO:0000269|PubMed:9486533}.
CC -!- DEVELOPMENTAL STAGE: Splicing is temporally regulated. Isoform 5 is
CC expressed both maternally and zygotically, whereas isoform 1, isoform
CC 2, isoform 3 and isoform 4 are exclusively zygotic. Expression is
CC highest in embryos from stage 12 on, with expression levels remaining
CC constant throughout embryogenesis. {ECO:0000269|PubMed:9486533}.
CC -!- INDUCTION: By activin. Weakly by bFGF. {ECO:0000269|PubMed:9486533}.
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DR EMBL; Y10119; CAA71205.1; -; mRNA.
DR EMBL; Y10121; CAA71207.1; -; mRNA.
DR EMBL; Y10122; CAA71208.1; -; mRNA.
DR EMBL; Y10123; CAA71209.1; -; mRNA.
DR EMBL; AJ000667; CAA04223.1; -; mRNA.
DR EMBL; BC055960; AAH55960.1; -; mRNA.
DR RefSeq; NP_001079830.1; NM_001086361.1. [O57685-3]
DR RefSeq; XP_018079766.1; XM_018224277.1. [O57685-1]
DR RefSeq; XP_018079772.1; XM_018224283.1. [O57685-2]
DR RefSeq; XP_018079775.1; XM_018224286.1. [O57685-4]
DR AlphaFoldDB; O57685; -.
DR SMR; O57685; -.
DR DNASU; 379520; -.
DR GeneID; 379520; -.
DR KEGG; xla:379520; -.
DR CTD; 379520; -.
DR Xenbase; XB-GENE-486805; pax2.L.
DR OMA; SINGXEV; -.
DR OrthoDB; 592933at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 379520; Expressed in kidney and 4 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: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..497
FT /note="Paired box protein Pax-2-A"
FT /id="PRO_0000289132"
FT DNA_BIND 16..142
FT /note="Paired"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT REGION 19..75
FT /note="PAI subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT REGION 94..142
FT /note="RED subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT REGION 143..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 166..376
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_052436"
FT VAR_SEQ 166..205
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9486533"
FT /id="VSP_052435"
FT VAR_SEQ 206..376
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9486533"
FT /id="VSP_052437"
FT VAR_SEQ 307..376
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9486533"
FT /id="VSP_052438"
FT VAR_SEQ 412..444
FT /note="Missing (in isoform 2, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:9486533, ECO:0000303|Ref.2"
FT /id="VSP_052439"
FT VAR_SEQ 445
FT /note="S -> FLGS (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:9486533, ECO:0000303|Ref.2"
FT /id="VSP_052440"
FT CONFLICT 91
FT /note="A -> T (in Ref. 1; CAA71208)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="Q -> R (in Ref. 1; CAA71208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 53204 MW; 2815A8C329878237 CRC64;
MDMHCKADPF SAMHPGHGGV NQLGGVFVNG RPLPDVVRQR IVELAHQGVR PCDISRQLRV
SHGCVSKILG RYYETGSIKP GVIGGSKPKV ATPKVVDKIA EYKRQNPTMF AWEIRDRLLA
EGICDNDTVP SVSSINRIIR TKVQQPFHPT PDGSGTPVGT PGHTLVPSTA SPPVSSASND
PVGSYSINGI LGIPRSNGEK RKRDEDGSDG SGPNGDSQSS VESLRKHLRA DNFTQQQLEA
LDRVFERPSY PDVFQTAEHI KSEQASEYSL PALTPGLDEV KSSLSASGNA DLGSNVSGPQ
SYPVVTESFA SHLYVKQEPH EASLTPFTPS SLASSGLADI QPFQMALTVD ASTPTYSSFT
HHGPHYGQFG SQPLIAGRDM SSTTLPGYPP HVPPTGQGSY PTSTLAGMVP GTNVSVHHSV
QPVECCSCLS SSKPCLFHCR TGSGSEFSGN PYSHPQYTTY NEAWRFSNPA LLSSPYYYSA
TSRGSAPPTA ATAYDRH
