HWA_XENLA
ID HWA_XENLA Reviewed; 341 AA.
AC A0A1L8I316;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Protein huluwa {ECO:0000303|PubMed:30467143};
GN Name=hwa {ECO:0000303|PubMed:30467143};
GN ORFNames=XELAEV_18008547mg {ECO:0000303|PubMed:27762356};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J;
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
RN [2]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=30467143; DOI=10.1126/science.aat1045;
RA Yan L., Chen J., Zhu X., Sun J., Wu X., Shen W., Zhang W., Tao Q., Meng A.;
RT "Maternal Huluwa dictates the embryonic body axis through beta-catenin in
RT vertebrates.";
RL Science 362:0-0(2018).
CC -!- FUNCTION: Key maternal determinant of the dorsal organizer and body
CC axis formation in vertebrates that acts by promoting stabilization of
CC beta-catenin (ctnnb1) (PubMed:30467143). Localizes on the plasma
CC membrane of the future dorsal blastomeres in early blastulas and binds
CC to and promotes the tankyrase-mediated degradation of axin (axin1 and
CC axin2). Axin degradation results in stabilization and nuclear
CC translocation of beta-catenin (ctnnb1) for activating organizer-
CC specific target gene expression (By similarity).
CC {ECO:0000250|UniProtKB:E9QDC5, ECO:0000269|PubMed:30467143}.
CC -!- SUBUNIT: Interacts with axin1; leading to promote the tankyrase-
CC mediated degradation of axin. Interacts with axin2; leading to promote
CC the tankyrase-mediated degradation of axin.
CC {ECO:0000250|UniProtKB:E9QDC5}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:E9QDC5};
CC Single-pass membrane protein {ECO:0000255}. Note=Enriched on the plasma
CC membrane of blastomeres only in a small region in which the dorsal
CC organizer will form. {ECO:0000250|UniProtKB:E9QDC5}.
CC -!- DEVELOPMENTAL STAGE: Transcripts are present in granules at the vegetal
CC cortex of oocytes andmove dorsally along with cortical rotation after
CC fertilization. {ECO:0000269|PubMed:30467143}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein results in
CC embryos lacking the body axis and dorsal tissues (PubMed:30467143).
CC Reduced dorsal marker expression but enhanced ventral marker expression
CC (PubMed:30467143). {ECO:0000269|PubMed:30467143}.
CC -!- SIMILARITY: Belongs to the huluwa family. {ECO:0000305}.
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DR EMBL; CM004466; OCU02777.1; -; Genomic_DNA.
DR RefSeq; XP_018122910.1; XM_018267421.1.
DR AlphaFoldDB; A0A1L8I316; -.
DR GeneID; 108718903; -.
DR KEGG; xla:108718903; -.
DR CTD; 108718903; -.
DR Xenbase; XB-GENE-22062235; hwa.L.
DR OrthoDB; 1141438at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 108718903; Expressed in egg cell and 7 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:UniProtKB.
DR GO; GO:0000578; P:embryonic axis specification; IMP:UniProtKB.
DR GO; GO:2000055; P:positive regulation of Wnt signaling pathway involved in dorsal/ventral axis specification; ISS:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
PE 2: Evidence at transcript level;
KW Cell membrane; Developmental protein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..341
FT /note="Protein huluwa"
FT /id="PRO_0000446380"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 206..211
FT /note="VPPNSP motif"
FT /evidence="ECO:0000250|UniProtKB:E9QDC5"
SQ SEQUENCE 341 AA; 37501 MW; C7E265C68898F556 CRC64;
MVTLSPAYLP SDGGTQAASA APSVEENWVV QPSLTLLVLL LVPCVLLLFF LNCFLLFHRL
PAFSLRKRAS RRKVGQYPCV RVGHSGQARL EPPYMLSPGV VLREGRLGSD TISQGFEATL
ALEEGVCGRQ NTPQSRGSCC QGGSIPSDQI CCSPRPRCAT PLPCCAPRRA WNAPAYVKKR
LRPKVWKVRE DELGSSCELD TRHNHVPPNT PAADNALGVT PKVKFCHTSS TQRKSHVGMV
PFTLGGSELL EDPSVIPRED TAEHLDASSS LPGPGLDSDF GVSAGISLHI LSSDSDSGSQ
SWTSGMEWDY YDPCYMRRNR LRRDARHNRH LPMMCSKQYW I
