N4B3A_XENLA
ID N4B3A_XENLA Reviewed; 573 AA.
AC A0A1L8GXY6;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=NEDD4-binding protein 3-A {ECO:0000305};
GN Name=n4bp3-a {ECO:0000305};
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 {ECO:0000312|Proteomes:UP000186698};
RN [1] {ECO:0000312|Proteomes:UP000186698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J {ECO:0000312|Proteomes:UP000186698};
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] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=24044555; DOI=10.1186/1749-8104-8-18;
RA Schmeisser M.J., Kuehl S.J., Schoen M., Beth N.H., Weis T.M.,
RA Grabrucker A.M., Kuehl M., Boeckers T.M.;
RT "The Nedd4-binding protein 3 (N4BP3) is crucial for axonal and dendritic
RT branching in developing neurons.";
RL Neural Dev. 8:18-18(2013).
RN [3] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=28104388; DOI=10.1016/j.ydbio.2017.01.009;
RA Kiem L.M., Dietmann P., Linnemann A., Schmeisser M.J., Kuehl S.J.;
RT "The Nedd4 binding protein 3 is required for anterior neural development in
RT Xenopus laevis.";
RL Dev. Biol. 423:66-76(2017).
CC -!- FUNCTION: Plays a role in axon and dendrite arborization during cranial
CC nerve development (PubMed:24044555). Also important for neural crest
CC migration and early development of other anterior structures including
CC eye, brain and cranial cartilage (PubMed:28104388).
CC {ECO:0000269|PubMed:24044555, ECO:0000269|PubMed:28104388}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q3LUD3}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q3LUD3}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q3LUD3}. Note=In developing neurons, accumulates
CC in early growth cones and at branching points of axons and dendrites.
CC {ECO:0000250|UniProtKB:Q3LUD3}.
CC -!- DEVELOPMENTAL STAGE: Detected from early embryogenesis onwards (stages
CC 11-35) (PubMed:24044555, PubMed:28104388). Expressed in the mesoderm
CC during gastrulation (PubMed:24044555). Expressed in migrating neural
CC crest cells, where it partially colocalizes with twist1
CC (PubMed:28104388). As development proceeds, shows marked expression in
CC developing anterior structures including brain, pharyngeal arches, eye
CC (including retina and lens), otic vesicle, heart, pronephros, liver and
CC cranial ganglia (PubMed:24044555, PubMed:28104388).
CC {ECO:0000269|PubMed:24044555, ECO:0000269|PubMed:28104388}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown severely impairs cranial
CC nerve development, with shorter or missing cranial ganglia and reduced
CC nerve arborization (PubMed:24044555). Neural crest migration is
CC impaired, although neural crest induction is not significantly affected
CC (PubMed:28104388). Brain size is reduced and cranial cartilage
CC development is severely disrupted, leading to smaller head size
CC (PubMed:28104388). Eyes are smaller and deformed, with coloboma
CC formation and disrupted retinal lamination (PubMed:28104388). In eye,
CC expression of the genes rax, pax6 and otx2 is reduced
CC (PubMed:28104388). In brain, expression of the genes emx1, pax6, otx2,
CC en2 and egr2 is reduced (PubMed:28104388). Tissues show increased
CC apoptosis and reduced cell proliferation (PubMed:28104388).
CC {ECO:0000269|PubMed:24044555, ECO:0000269|PubMed:28104388}.
CC -!- SIMILARITY: Belongs to the N4BP3 family. {ECO:0000305}.
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DR EMBL; CM004470; OCT88708.1; -; Genomic_DNA.
DR RefSeq; XP_018107756.1; XM_018252267.1.
DR AlphaFoldDB; A0A1L8GXY6; -.
DR SMR; A0A1L8GXY6; -.
DR GeneID; 108710992; -.
DR KEGG; xla:108710992; -.
DR CTD; 108710992; -.
DR Xenbase; XB-GENE-17343789; n4bp3.L.
DR OMA; TCEPDTR; -.
DR OrthoDB; 697945at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 108710992; Expressed in heart and 18 other tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR InterPro; IPR033571; N4BP3.
DR PANTHER; PTHR32274; PTHR32274; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Coiled coil; Cytoplasmic vesicle; Developmental protein;
KW Neurogenesis; Reference proteome.
FT CHAIN 1..573
FT /note="NEDD4-binding protein 3-A"
FT /id="PRO_0000441857"
FT REGION 168..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 289..539
FT /evidence="ECO:0000255"
FT COMPBIAS 168..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 65251 MW; 17F5248732023799 CRC64;
MAAAQTFNSN CDPGNFHKLQ SFPSESVTYT CKMGSVSSLI DKQDFPHDGF NLDFKPFPEP
NCKRGLHQKE LLSYLNITKK EVKSNKKFHS GLGFRREHSV EGGENDYPVF YHKDHRGTEF
SKSSLPERGH LDKSRFGPSA LRSNVKAFMS IQSLYQSGNK LSKSNGSLNT MSCVSSPPCR
GPLQPSNSHS NNQSESGNDE EDDSLSDSRQ NSINSLNSYS PGFSVARGQI SASLGHINHI
GGSLDQASRG TRDTMAGEKG TLSCRSMATL SRLQCSGEPP PPYEYSQSVE DVARQLEERL
HEKGMEARQL RRNASDNDDP FTKVFEDKRR LWMEELDELK QMYMSKLQQI SQQALRSQRA
LQLQLYKVQQ EKKRLQEELN SLRGESEELR QKQSQSDNSG PKLEDSKWEI SQKAGEISLL
KQQLRDSQAE INQKLGEVVS LKSQLREAKV LVKEKEKESA ELSTRLQALE NAKSQAPVDL
PRDNSDTIDL ERLRAELMLE RRQNEAQMLT FETERKVWKE EKDKVLRYQK EIQSSYREMY
HRNQVLERQV LELRQGVGQS PSSPAIWMDT VET