DTBP1_CHICK
ID DTBP1_CHICK Reviewed; 351 AA.
AC Q5ZKM0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Dysbindin;
DE AltName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 8;
DE Short=BLOC-1 subunit 8;
DE AltName: Full=Dysbindin-1;
DE AltName: Full=Dystrobrevin-binding protein 1;
GN Name=DTNBP1; Synonyms=Bloc1s8; ORFNames=RCJMB04_10b8;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Component of the BLOC-1 complex, a complex that is required
CC for normal biogenesis of lysosome-related organelles (LRO), such as
CC platelet dense granules and melanosomes. Plays a role in intracellular
CC vesicle trafficking. Plays a role in synaptic vesicle trafficking and
CC in neurotransmitter release. May be required for normal dopamine
CC homeostasis in the cerebral cortex, hippocampus, and hypothalamus.
CC Plays a role in the regulation of cell surface exposure of DRD2.
CC Contributes to the regulation of dopamine signaling. May play a role in
CC actin cytoskeleton reorganization and neurite outgrowth (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the biogenesis of lysosome-related organelles
CC complex 1 (BLOC-1). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Melanosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus
CC {ECO:0000250}. Postsynaptic density {ECO:0000250}. Endoplasmic
CC reticulum {ECO:0000250}. Note=Detected at axon terminals and in
CC dendrites. Detected at synapses, at postsynaptic density, at
CC presynaptic vesicle membranes and microtubules. Detected at
CC tubulovesicular elements in the vicinity of the Golgi apparatus and of
CC melanosomes. Detected in neuron cell bodies, axons and dendrites (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dysbindin family. {ECO:0000305}.
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DR EMBL; AJ720064; CAG31723.1; -; mRNA.
DR RefSeq; NP_001006372.1; NM_001006372.1.
DR AlphaFoldDB; Q5ZKM0; -.
DR SMR; Q5ZKM0; -.
DR STRING; 9031.ENSGALP00000030426; -.
DR PaxDb; Q5ZKM0; -.
DR Ensembl; ENSGALT00000031062; ENSGALP00000030426; ENSGALG00000012703.
DR GeneID; 420840; -.
DR KEGG; gga:420840; -.
DR CTD; 84062; -.
DR VEuPathDB; HostDB:geneid_420840; -.
DR eggNOG; ENOG502QRS9; Eukaryota.
DR GeneTree; ENSGT00940000156479; -.
DR HOGENOM; CLU_071074_0_0_1; -.
DR InParanoid; Q5ZKM0; -.
DR OrthoDB; 862376at2759; -.
DR PhylomeDB; Q5ZKM0; -.
DR PRO; PR:Q5ZKM0; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000012703; Expressed in brain and 13 other tissues.
DR ExpressionAtlas; Q5ZKM0; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031083; C:BLOC-1 complex; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0060155; P:platelet dense granule organization; IBA:GO_Central.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; ISS:UniProtKB.
DR GO; GO:0060159; P:regulation of dopamine receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IBA:GO_Central.
DR InterPro; IPR007531; Dysbindin.
DR PANTHER; PTHR16294; PTHR16294; 1.
DR Pfam; PF04440; Dysbindin; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Endosome; Membrane; Nucleus; Reference proteome; Synapse.
FT CHAIN 1..351
FT /note="Dysbindin"
FT /id="PRO_0000267211"
FT REGION 291..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 106..179
FT /evidence="ECO:0000255"
FT COMPBIAS 291..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 351 AA; 39593 MW; 6CB21B3582FD9D3B CRC64;
MLETLRERLL SVQQDFTSGL KTLGDKSREA KKSRQRTAQC SPEFSAGLEL LSRYEDAWAA
LHKGAKDCAK AGELVDSEVV MLSAHWEKKR NSLVELQDQL QQIPGFLADL ECLTASLARL
EANFEEMETH LLCLEDLCEQ CELERYKCVQ TLQLENYKKT KRKELENFKA ELDAEHAQKV
LDMEHTQQMK LKERQKFFEE AFQQDMEQYL STGYLQIAER REPIGSMSSM EVNVDMLEQM
DLMDMSDQEA LDVFLNSGGE DNNMLSPMLG PDSSTYVNEI SLQVPSQSEL RHKLSSLSST
CTDSASQEAS EGESPVVQSD EEEVQVDTAL AAVAERKGAS DVSDESDSQT I
