PV1_XENLA
ID PV1_XENLA Reviewed; 282 AA.
AC O42173;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Homeobox protein pv.1;
DE AltName: Full=Posterior-ventral 1 transcription factor;
GN Name=pv.1 {ECO:0000312|EMBL:AAB71353.1};
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:AAB71353.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC TISSUE=Gastrula {ECO:0000269|PubMed:8692829};
RX PubMed=8692829; DOI=10.1073/pnas.93.13.6415;
RA Ault K.T., Dirksen M.-L., Jamrich M.;
RT "A novel homeobox gene PV.1 mediates induction of ventral mesoderm in
RT Xenopus embryos.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6415-6420(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAB71353.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9405105; DOI=10.1006/dbio.1997.8737;
RA Ault K.T., Xu R.-H., Kung H.-F., Jamrich M.;
RT "The homeobox gene PV.1 mediates specification of the prospective neural
RT ectoderm in Xenopus embryos.";
RL Dev. Biol. 192:162-171(1997).
RN [3] {ECO:0000305}
RP FUNCTION, AND INDUCTION.
RX PubMed=10191050; DOI=10.1006/dbio.1999.9205;
RA Xu R.-H., Ault K.T., Kim J., Park M.-J., Hwang Y.-S., Peng Y., Sredni D.,
RA Kung H.-F.;
RT "Opposite effects of FGF and BMP-4 on embryonic blood formation: roles of
RT PV.1 and GATA-2.";
RL Dev. Biol. 208:352-361(1999).
RN [4] {ECO:0000305}
RP DNA-BINDING.
RX PubMed=10926781; DOI=10.1006/dbio.2000.9778;
RA Mochizuki T., Karavanov A.A., Curtiss P.E., Ault K.T., Sugimoto N.,
RA Watabe T., Shiokawa K., Jamrich M., Cho K.W.Y., Dawid I.B., Taira M.;
RT "Xlim-1 and LIM domain binding protein 1 cooperate with various
RT transcription factors in the regulation of the goosecoid promoter.";
RL Dev. Biol. 224:470-485(2000).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=11944926; DOI=10.1006/bbrc.2002.6740;
RA Hwang Y.-S., Seo J.-J., Cha S.-W., Lee H.-S., Lee S.-Y., Roh D.-H.,
RA Kung H.-F., Kim J., Park M.-J.;
RT "Antimorphic PV.1 causes secondary axis by inducing ectopic organizer.";
RL Biochem. Biophys. Res. Commun. 292:1081-1086(2002).
RN [6] {ECO:0000305}
RP FUNCTION, AND DOMAIN.
RX PubMed=12890483; DOI=10.1016/s0006-291x(03)01321-4;
RA Hwang Y.-S., Lee H.-S., Roh D.-H., Cha S.-W., Lee S.-Y., Seo J.-J., Kim J.,
RA Park M.-J.;
RT "Active repression of organizer genes by C-terminal domain of PV.1.";
RL Biochem. Biophys. Res. Commun. 308:79-86(2003).
CC -!- FUNCTION: Transcriptional repressor. Acts in a ventral signaling
CC pathway downstream of bmp4, which suppresses dorsal mesoderm formation
CC and leads to both ventral mesoderm and ventral ectoderm formation. Acts
CC in the ectoderm to simultaneously specify epidermal lineages and
CC restrict neuralization. Represses transcription of dorsal-specific
CC genes. Binds to DNA, with preference for the target sequences 5'-
CC TAATGC-3' and 5'-TAATTG-3'. Acts in a pathway downstream of bmp4 and
CC fgf to negatively regulate erythroid specification.
CC {ECO:0000269|PubMed:10191050, ECO:0000269|PubMed:10926781,
CC ECO:0000269|PubMed:11944926, ECO:0000269|PubMed:12890483,
CC ECO:0000269|PubMed:8692829, ECO:0000269|PubMed:9405105}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the ventral marginal zone of
CC blastulae. At early gastrulation, expression begins to spread to the
CC animal pole (ectoderm), and at stage 11.5 is expressed in a gradient
CC across the animal cap, with levels highest in the ventral region. At
CC the end of gastrulation, predominantly localized to the ventral and
CC lateral regions of the closing slit blastopore. Also expressed at a low
CC level in ventral endoderm. {ECO:0000269|PubMed:8692829,
CC ECO:0000269|PubMed:9405105}.
CC -!- DEVELOPMENTAL STAGE: Expression begins in the late blastula, peaks at
CC stage 11 (early gastrula) and decreases thereafter.
CC {ECO:0000269|PubMed:8692829}.
CC -!- INDUCTION: By bmp4 and its downstream effector smad1. Fgf enhances
CC bmp4-induced expression. {ECO:0000269|PubMed:10191050,
CC ECO:0000269|PubMed:8692829, ECO:0000269|PubMed:9405105}.
CC -!- DOMAIN: The repressor activity is mostly localized to the C-terminal
CC region. {ECO:0000269|PubMed:12890483}.
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DR EMBL; AF012925; AAB71353.1; -; mRNA.
DR RefSeq; NP_001081704.1; NM_001088235.1.
DR AlphaFoldDB; O42173; -.
DR SMR; O42173; -.
DR GeneID; 398007; -.
DR KEGG; xla:398007; -.
DR CTD; 398007; -.
DR Xenbase; XB-GENE-920512; ventx1.1.L.
DR OrthoDB; 1369499at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 398007; Expressed in gastrula and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0030509; P:BMP signaling pathway; IMP:UniProtKB.
DR GO; GO:0048264; P:determination of ventral identity; IMP:UniProtKB.
DR GO; GO:0001707; P:mesoderm formation; IMP:UniProtKB.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; IMP:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR020479; Homeobox_metazoa.
DR Pfam; PF00046; Homeodomain; 1.
DR PRINTS; PR00024; HOMEOBOX.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Homeobox; Nucleus; Reference proteome.
FT CHAIN 1..282
FT /note="Homeobox protein pv.1"
FT /id="PRO_0000286588"
FT DNA_BIND 129..188
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 17..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 282 AA; 31846 MW; 507AAEE91E884E2F CRC64;
MVQQGFSIDL ILARSREEAA DGKDSMSSRP HIPCAPQPLP PNKYAKEMPR RKDGQDVQEH
SSWSLGEQGK KLQYSSPSSA ALHRSWGSSD DFSSVGSEDD STEGSPSPMR NSQETETDHR
GESPKSDLQR HLRTAFTPQQ ISKLEQAFNK QRYLGASERK KLATSLRLSE IQVKTWFQNR
RMKLKRQIQD QQHNMVPPPV CYPQTFPYYP GVLPVPLNSG SFYQPPAHPF QAPQNSYIPD
PRFIPQPLPH HIRMSVALQQ QYPPLGLPPG RYFTGLASKN DG
