HWA_DANRE
ID HWA_DANRE Reviewed; 294 AA.
AC E9QDC5;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Protein huluwa {ECO:0000303|PubMed:30467143};
GN Name=hwa {ECO:0000303|PubMed:30467143};
GN ORFNames=si:dkey-121h17.7 {ECO:0000312|ZFIN:ZDB-GENE-091204-94};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH AXIN1 AND AXIN2,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 164-VAL--PRO-169 AND 184-SER--THR-190.
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) (PubMed:30467143). Axin degradation results in stabilization and
CC nuclear translocation of beta-catenin (ctnnb1) for activating
CC organizer-specific target gene expression (PubMed:30467143).
CC {ECO:0000269|PubMed:30467143}.
CC -!- SUBUNIT: Interacts with axin1; leading to promote the tankyrase-
CC mediated degradation of axin (PubMed:30467143). Interacts with axin2;
CC leading to promote the tankyrase-mediated degradation of axin
CC (PubMed:30467143). {ECO:0000269|PubMed:30467143}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30467143};
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:0000269|PubMed:30467143}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally (PubMed:30467143).
CC Transcripts are first distributed evenly in blastomeres
CC (PubMed:30467143). During the early cleavage period, transcripts in the
CC vegetal pole region are transported toward the animal pole from one
CC side of the yolk (PubMed:30467143). Transcript levels decrease 2 hours
CC post fertilization (PubMed:30467143). The protein is enriched in a
CC small region of blastomeres, in which the dorsal organizer will form
CC (at protein level) (PubMed:30467143). {ECO:0000269|PubMed:30467143}.
CC -!- DISRUPTION PHENOTYPE: Maternal mutant embryos lack the body axis:
CC embryos develop normally during cleavage and blastula stages but lack
CC the embryonic shield at the shield stage (PubMed:30467143). The dorsal
CC organizer is absent and embryos fail to form the head and other
CC dorsoanterior tissues (PubMed:30467143). {ECO:0000269|PubMed:30467143}.
CC -!- MISCELLANEOUS: Was named huluwa after the Chinese animation TV series
CC huluwa, known as Calabash Brothers in western countries.
CC {ECO:0000269|PubMed:30467143}.
CC -!- SIMILARITY: Belongs to the huluwa family. {ECO:0000305}.
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DR EMBL; CR382296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_703380.2; XM_698288.7.
DR AlphaFoldDB; E9QDC5; -.
DR SMR; E9QDC5; -.
DR IntAct; E9QDC5; 3.
DR PaxDb; E9QDC5; -.
DR Ensembl; ENSDART00000139288; ENSDARP00000123053; ENSDARG00000094542.
DR GeneID; 555985; -.
DR KEGG; dre:555985; -.
DR CTD; 555985; -.
DR ZFIN; ZDB-GENE-091204-94; hwa.
DR eggNOG; ENOG502RZ6F; Eukaryota.
DR GeneTree; ENSGT01000000214630; -.
DR HOGENOM; CLU_946497_0_0_1; -.
DR OMA; GYPVTNL; -.
DR OrthoDB; 1141438at2759; -.
DR PRO; PR:E9QDC5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 21.
DR Bgee; ENSDARG00000094542; Expressed in ovary and 17 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IDA:UniProtKB.
DR GO; GO:0000578; P:embryonic axis specification; IDA:UniProtKB.
DR GO; GO:2000055; P:positive regulation of Wnt signaling pathway involved in dorsal/ventral axis specification; IDA:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IDA:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:ZFIN.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..294
FT /note="Protein huluwa"
FT /id="PRO_0000446379"
FT TOPO_DOM 1..23
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30467143"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30467143"
FT REGION 154..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 164..169
FT /note="VPPNSP motif"
FT /evidence="ECO:0000305|PubMed:30467143"
FT MOTIF 184..190
FT /note="SLRRSST motif"
FT /evidence="ECO:0000305|PubMed:30467143"
FT MUTAGEN 164..169
FT /note="Missing: Loss of function."
FT /evidence="ECO:0000269|PubMed:30467143"
FT MUTAGEN 184..190
FT /note="Missing: Loss of function."
FT /evidence="ECO:0000269|PubMed:30467143"
SQ SEQUENCE 294 AA; 32250 MW; 5497721A2C0D7F6A CRC64;
MSQLGSAVPS SNLPEGLPVS SLALLILVLI PCVLLLLLLN CLFVGYKLFR MTRRKRDRYG
SEMSLMHSSY STRQRITRFS DEPPVAPNRK TNYVSVSEPM LAPPITSSLT SSAERRATGQ
RAMFLRPDGA TYAGSESLRV PHWRTSAPVL VQSSDSDMER VNTVPPNSPV LRVTPNGFSV
PMTSLRRSST MELESTSLDK IHVECESASI IPQENSCYVV SSSSSARGSG LDSDFGASAG
VSLRILSMDS DGFPGSAWAS ALEWDYYDPS YVTQNHVPKH RPQAPPITTK QYWV
