BIB_DROME
ID BIB_DROME Reviewed; 696 AA.
AC P23645; Q9VL53;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Neurogenic protein big brain;
GN Name=bib; ORFNames=CG4722;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=1692392; DOI=10.1038/345163a0;
RA Rao Y., Jan L.Y., Jan Y.N.;
RT "Similarity of the product of the Drosophila neurogenic gene big brain to
RT transmembrane channel proteins.";
RL Nature 345:163-167(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION.
RX PubMed=1483394; DOI=10.1242/dev.116.1.31;
RA Rao Y., Bodmer R., Jan L.Y., Jan Y.N.;
RT "The big brain gene of Drosophila functions to control the number of
RT neuronal precursors in the peripheral nervous system.";
RL Development 116:31-40(1992).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9367444; DOI=10.1242/dev.124.19.3881;
RA Doherty D., Jan L.Y., Jan Y.N.;
RT "The Drosophila neurogenic gene big brain, which encodes a membrane-
RT associated protein, acts cell autonomously and can act synergistically with
RT Notch and Delta.";
RL Development 124:3881-3893(1997).
RN [7]
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF GLU-71.
RX PubMed=11923418; DOI=10.1523/jneurosci.22-07-02530.2002;
RA Yanochko G.M., Yool A.J.;
RT "Regulated cationic channel function in Xenopus oocytes expressing
RT Drosophila big brain.";
RL J. Neurosci. 22:2530-2540(2002).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLU-71; ASP-253 AND GLU-274.
RX PubMed=14990474; DOI=10.1016/s0006-3495(04)74215-0;
RA Yanochko G.M., Yool A.J.;
RT "Block by extracellular divalent cations of Drosophila big brain channels
RT expressed in Xenopus oocytes.";
RL Biophys. J. 86:1470-1478(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; THR-47; SER-300; SER-394
RP AND SER-576, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Essential for proper differentiation of ectoderm. Acts
CC synergistically with neurogenic locus proteins Notch and Delta during
CC the separation of neural and epidermal cell lineages in response to the
CC lateral inhibition signal. Voltage-insensitive monovalent cation
CC channel. Ion transport is blocked by the presence of divalent cations.
CC {ECO:0000269|PubMed:11923418, ECO:0000269|PubMed:1483394,
CC ECO:0000269|PubMed:14990474, ECO:0000269|PubMed:1692392,
CC ECO:0000269|PubMed:9367444}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9367444}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:9367444}.
CC -!- TISSUE SPECIFICITY: Detected in all tissues with neurogenic abilities,
CC for example the neurogenic ectoderm. {ECO:0000269|PubMed:9367444}.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA).
CC -!- PTM: Phosphorylated at its C-terminus. {ECO:0000269|PubMed:11923418,
CC ECO:0000269|PubMed:18327897}.
CC -!- MISCELLANEOUS: Separation of neuroblasts from the ectoderm into the
CC inner part of embryo is one of the first steps of CNS development in
CC insects, this process is under control of the neurogenic genes.
CC Mutation in bib gene underlies 'big brain' development defect.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X53275; CAB37863.1; -; mRNA.
DR EMBL; AE014134; AAF52844.1; -; Genomic_DNA.
DR EMBL; AY051981; AAK93405.1; -; mRNA.
DR PIR; S09699; S09699.
DR RefSeq; NP_476837.1; NM_057489.5.
DR AlphaFoldDB; P23645; -.
DR SMR; P23645; -.
DR BioGRID; 60424; 7.
DR DIP; DIP-21188N; -.
DR IntAct; P23645; 1.
DR STRING; 7227.FBpp0079519; -.
DR TCDB; 1.A.8.8.3; the major intrinsic protein (mip) family.
DR iPTMnet; P23645; -.
DR PaxDb; P23645; -.
DR EnsemblMetazoa; FBtr0079929; FBpp0079519; FBgn0000180.
DR GeneID; 34330; -.
DR KEGG; dme:Dmel_CG4722; -.
DR CTD; 34330; -.
DR FlyBase; FBgn0000180; bib.
DR VEuPathDB; VectorBase:FBgn0000180; -.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_021773_0_0_1; -.
DR InParanoid; P23645; -.
DR OMA; PPQMMPD; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P23645; -.
DR SignaLink; P23645; -.
DR BioGRID-ORCS; 34330; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34330; -.
DR PRO; PR:P23645; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000180; Expressed in wing disc and 29 other tissues.
DR ExpressionAtlas; P23645; baseline and differential.
DR Genevisible; P23645; DM.
DR GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005261; F:cation channel activity; IDA:FlyBase.
DR GO; GO:0015267; F:channel activity; ISS:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:FlyBase.
DR GO; GO:0007498; P:mesoderm development; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; ISS:FlyBase.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR19139; PTHR19139; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Ion channel; Ion transport;
KW Membrane; Neurogenesis; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..696
FT /note="Neurogenic protein big brain"
FT /id="PRO_0000064097"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..696
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 314..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 126..128
FT /note="NPA 1"
FT MOTIF 238..240
FT /note="NPA 2"
FT COMPBIAS 436..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 273
FT /note="Phosphotyrosine; by Src"
FT /evidence="ECO:0000255"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 367
FT /note="Phosphotyrosine; by Abl"
FT /evidence="ECO:0000255"
FT MOD_RES 384
FT /note="Phosphotyrosine; by Src"
FT /evidence="ECO:0000255"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 478
FT /note="Phosphotyrosine; by Src"
FT /evidence="ECO:0000255"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 610
FT /note="Phosphotyrosine; by Abl"
FT /evidence="ECO:0000255"
FT MUTAGEN 71
FT /note="E->D: Partial loss of transport activity and
FT increased sensitivity to blocking by the magnesium ion."
FT /evidence="ECO:0000269|PubMed:11923418,
FT ECO:0000269|PubMed:14990474"
FT MUTAGEN 71
FT /note="E->K: Loss of expression in cell membrane."
FT /evidence="ECO:0000269|PubMed:11923418,
FT ECO:0000269|PubMed:14990474"
FT MUTAGEN 71
FT /note="E->N: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:11923418,
FT ECO:0000269|PubMed:14990474"
FT MUTAGEN 71
FT /note="E->Q: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:11923418,
FT ECO:0000269|PubMed:14990474"
FT MUTAGEN 253
FT /note="D->N: No effect on transport activity."
FT /evidence="ECO:0000269|PubMed:14990474"
FT MUTAGEN 274
FT /note="E->Q: No effect on transport activity."
FT /evidence="ECO:0000269|PubMed:14990474"
FT CONFLICT 198
FT /note="F -> S (in Ref. 1; CAB37863)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="P -> S (in Ref. 1; CAB37863)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="Missing (in Ref. 1; CAB37863)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="Q -> QQQQQQ (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 696 AA; 76509 MW; 14DEA6064FAFAB72 CRC64;
MADESLHTVP LEHNIDYHIV TLFERLEAMR KDSHGGGHGV NNRLSSTLQA PKRSMQAEIR
TLEFWRSIIS ECLASFMYVF IVCGAAAGVG VGASVSSVLL ATALASGLAM ATLTQCFLHI
SGAHINPAVT LALCVVRSIS PIRAAMYITA QCGGGIAGAA LLYGVTVPGY QGNLQAAISH
SAALAAWERF GVEFILTFLV VLCYFVSTDP MKKFMGNSAA SIGCAYSACC FVSMPYLNPA
RSLGPSFVLN KWDSHWVYWF GPLVGGMASG LVYEYIFNSR NRNLRHNKGS IDNDSSSIHS
EDELNYDMDM EKPNKYQQSQ GTYPRGQSNG NGGGQAAGNG QHQAANMGQM PGVVANAGQG
NYCQNLYTAP PLSSKYDQQQ EPLYGGTRSL YCRSPTLTRS NLNRSQSVYA KSNTAINRDI
VPRPGPLVPA QSLYPMRTQQ QQQQQQQQQQ QVAPAPQSSH LQNQNVQNQM QQRSESIYGM
RGSMRGQQQP IQQQQQQQQQ QQLQQQQPNM GVQQQQMQPP PQMMSDPQQQ PQGFQPVYGT
RTNPTPMDGN HKYDRRDPQQ MYGVTGPRNR GQSAQSDDSS YGSYHGSAVT PPARHPSVEP
SPPPPPMLMY APPPQPNAAH PQPIRTQSER KVSAPVVVSQ PAACAVTYTT SQGSAVTAQQ
QQQQQQQQQQ QQQQQQQQMM MQQQQQHYGM LPLRPN
