ID   N4B3B_XENLA             Reviewed;         573 AA.
AC   A0A1L8GUX5;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=NEDD4-binding protein 3-B {ECO:0000305};
GN   Name=n4bp3-b {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; CM004471; OCT87647.1; -; Genomic_DNA.
DR   RefSeq; XP_018111575.1; XM_018256086.1.
DR   AlphaFoldDB; A0A1L8GUX5; -.
DR   SMR; A0A1L8GUX5; -.
DR   GeneID; 108713222; -.
DR   KEGG; xla:108713222; -.
DR   CTD; 108713222; -.
DR   Xenbase; XB-GENE-6486425; n4bp3.S.
DR   OMA; EFSCPTT; -.
DR   OrthoDB; 697945at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 108713222; 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-B"
FT                   /id="PRO_0000441858"
FT   REGION          119..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          287..474
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        119..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  65125 MW;  14E5805FF29C1148 CRC64;
     MAAAQTFSAN CDPVNFHNLQ SYPSESVTYS CKMGNVSSLM EKQDFPNEGF NLDFRPFPEP
     SCKRGLHQKE FLSYLNITKK EGKNNKKFPS GLGFRREHSL QAEENDYPVF YHKDHRGTEF
     SKSSLPERGH SDKSRFGPSA LKSNVKAFMS IQSLHQSTNK LSKSNGSLNT LGCVGSPPCR
     GPLQPSNSHS NNPSESGNDE DDDSLSDSKQ NSINSLNSYS PSFTVARGQI SASLGHINHI
     GGSLDRASRG LRDTMAGEKG TLSCRNMATL SRLQCSGEPP PPYEYSESVE DVARQLEKRL
     QEKGMEAQQL RRNASDNDDP FTQVFEDKRR LWMEELDELK QMYMSKLQQI SQQALRSQRA
     LQLQLYKVQQ EKKRLQEELN SLQGENEELR QKQSQSDNSG PNLEDSKWEI SQKAGEISFL
     KQQLRDSQAE INLKLGEVVS LKVQLREAKA LVKEKEKESA ELSDCLQALE DVKSQTPVDL
     PRDSSDTIDV ERLRAELMLE RRQNEAQILI FETERKVWKE EKDKVLRYQK EIQSSYLEMY
     QRNQALERQV LELRQGVGQS LSSPASWMDT VET