BICD_CAEEL
ID BICD_CAEEL Reviewed; 737 AA.
AC V6CJ04; V6CK55;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Protein bicaudal D homolog {ECO:0000305};
GN Name=bicd-1 {ECO:0000303|PubMed:20005871, ECO:0000312|WormBase:C43G2.2a};
GN ORFNames=C43G2.2 {ECO:0000312|WormBase:C43G2.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH DLC-1 AND EGAL-1, INTERACTION
RP WITH EGAL-1 AND UNC-83, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=20005871; DOI=10.1016/j.ydbio.2009.12.004;
RA Fridolfsson H.N., Ly N., Meyerzon M., Starr D.A.;
RT "UNC-83 coordinates kinesin-1 and dynein activities at the nuclear envelope
RT during nuclear migration.";
RL Dev. Biol. 338:237-250(2010).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21205795; DOI=10.1242/dev.060939;
RA Aguirre-Chen C., Buelow H.E., Kaprielian Z.;
RT "C. elegans bicd-1, homolog of the Drosophila dynein accessory factor
RT Bicaudal D, regulates the branching of PVD sensory neuron dendrites.";
RL Development 138:507-518(2011).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27697906; DOI=10.1242/dev.141192;
RA Bone C.R., Chang Y.T., Cain N.E., Murphy S.P., Starr D.A.;
RT "Nuclei migrate through constricted spaces using microtubule motors and
RT actin networks in C. elegans hypodermal cells.";
RL Development 143:4193-4202(2016).
CC -!- FUNCTION: Part of a complex with dlc-1 and egal-1, which is recruited
CC to the nuclear envelope by unc-83, where in turn, it recruits dynein to
CC the nuclear surface and regulates nuclear migration in hypodermal
CC precursor cells (PubMed:20005871) (Probable). Required for the
CC formation of dendritic branches of PVD sensory neurons
CC (PubMed:21205795). {ECO:0000269|PubMed:20005871,
CC ECO:0000269|PubMed:21205795, ECO:0000305|PubMed:27697906}.
CC -!- SUBUNIT: Component of a dynein-regulating complex composed of at least
CC bicd-1, dlc-1 and egal-1. Interacts with egal-1 and unc-83.
CC {ECO:0000269|PubMed:20005871}.
CC -!- INTERACTION:
CC V6CJ04; Q17902: egal-1; NbExp=2; IntAct=EBI-2006416, EBI-328330;
CC V6CJ04; Q23064-3: unc-83; NbExp=2; IntAct=EBI-2006416, EBI-2902257;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000305|PubMed:20005871}.
CC Perikaryon {ECO:0000269|PubMed:21205795}. Cell projection, dendrite
CC {ECO:0000269|PubMed:21205795}. Note=Probably recruited to the nuclear
CC envelope by unc-83. {ECO:0000305|PubMed:20005871}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C43G2.2a};
CC IsoId=V6CJ04-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C43G2.2b};
CC IsoId=V6CJ04-2; Sequence=VSP_059365;
CC -!- TISSUE SPECIFICITY: Expressed in the excretory cell, body wall muscles,
CC vulval muscle cells, PVD and FLP sensory neurons and AVF interneurons.
CC {ECO:0000269|PubMed:21205795}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic development.
CC {ECO:0000269|PubMed:20005871}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in increased
CC dendritic branch formation in PVD sensory neurons (PubMed:21205795).
CC RNAi-mediated knockdown in a bicd-1 (ok949) mutant background results
CC in failed nuclei migrations in larval hypodermal P-cells
CC (PubMed:27697906). {ECO:0000269|PubMed:21205795,
CC ECO:0000269|PubMed:27697906}.
CC -!- SIMILARITY: Belongs to the BicD family. {ECO:0000305}.
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DR EMBL; BX284604; CDK13418.1; -; Genomic_DNA.
DR EMBL; BX284604; CDK13419.1; -; Genomic_DNA.
DR RefSeq; NP_001293734.1; NM_001306805.1. [V6CJ04-1]
DR RefSeq; NP_001293735.1; NM_001306806.1. [V6CJ04-2]
DR AlphaFoldDB; V6CJ04; -.
DR SMR; V6CJ04; -.
DR ComplexPortal; CPX-1388; bicd-1-dlc-1-egal-1 microtubule-associated dynein motor complex.
DR IntAct; V6CJ04; 6.
DR STRING; 6239.C43G2.2; -.
DR PaxDb; V6CJ04; -.
DR PeptideAtlas; V6CJ04; -.
DR EnsemblMetazoa; C43G2.2a.1; C43G2.2a.1; WBGene00016611. [V6CJ04-1]
DR EnsemblMetazoa; C43G2.2b.1; C43G2.2b.1; WBGene00016611. [V6CJ04-2]
DR GeneID; 183417; -.
DR KEGG; cel:CELE_C43G2.2; -.
DR CTD; 183417; -.
DR WormBase; C43G2.2a; CE49379; WBGene00016611; bicd-1. [V6CJ04-1]
DR WormBase; C43G2.2b; CE49263; WBGene00016611; bicd-1. [V6CJ04-2]
DR eggNOG; KOG0999; Eukaryota.
DR GeneTree; ENSGT00940000154471; -.
DR OMA; ANGECRR; -.
DR OrthoDB; 542877at2759; -.
DR Reactome; R-CEL-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR PRO; PR:V6CJ04; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00016611; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; IC:ComplexPortal.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IEA:InterPro.
DR GO; GO:0034452; F:dynactin binding; IBA:GO_Central.
DR GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR GO; GO:0072393; P:microtubule anchoring at microtubule organizing center; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0030473; P:nuclear migration along microtubule; IC:ComplexPortal.
DR GO; GO:0033365; P:protein localization to organelle; IBA:GO_Central.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:WormBase.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IBA:GO_Central.
DR InterPro; IPR018477; BICD.
DR PANTHER; PTHR31233; PTHR31233; 1.
DR Pfam; PF09730; BicD; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Neurogenesis; Nucleus;
KW Reference proteome.
FT CHAIN 1..737
FT /note="Protein bicaudal D homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000443514"
FT REGION 72..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..255
FT /evidence="ECO:0000255"
FT COILED 292..319
FT /evidence="ECO:0000255"
FT COILED 547..684
FT /evidence="ECO:0000255"
FT COMPBIAS 76..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 686..698
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059365"
SQ SEQUENCE 737 AA; 84113 MW; A0A4803FAE0F6473 CRC64;
MAESELEKLR QDIAILTEKY EQAKEDIHKA ANAGLELLRQ KEDLEKRLAE MQAELDLART
EIDKTNQTLA EYRSQHQRST RSELENEESL LEESSAKEEE YLQRIAKLEA DLKKKEQELA
EKKEELESIE KKHSKEIDSG AALEDERRKL RAELKETKER EQRLISEYSE LEEENIGLQK
TVANLRGSQV EYESLRIDNN RLEETIEIMK MAAEEDEILR VIADKQLEEA LLTAQQERDQ
RLAMKRELEQ TRNAEHISSL NDMLFGLERL GEDGELPPPQ PGASDLFSEL QGSSDVKVRE
LEAAKEGLQE ELKSREKIFI EFVTGLADTL NIHRPTNELD YMHARQQKDV VLEKIQNIAR
DTDRHDKEGE EKRSGILKAD LRTLVLVAGE KSAQLAAAQD AMIQVSDQLY QFYHQMTQNQ
GVQTEKSVQE IVKKLRLLAR ANAEDVPRVS LADEGVESGT ETDVNASRSI PLNSDRLVIA
PSFAKEIEKK LASVKIGDVL SETDLRQRIL TEGNAISETT ESLKKMIQVV KRTSEQAFNQ
AVMASGAENE IEMQNMKLRS LLSTKRDQIS TLRTVLKSNK LTAESALTSM REKYESEKKM
MMEINDKMRR ELKQLKEDAA TFASHRAMFT ARGEELKSKV EELSNELRAN EEEKKTLNQL
LRLAIQQKLT LTQRLEEVEV DRDRQVFKRS STRAPTRETY QPPRAVRYPG STTTAQQPAP
SSSGGSRGGP RRGDNQQ
