DTBP1_BOVIN
ID DTBP1_BOVIN Reviewed; 342 AA.
AC Q2HJA5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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. In concert with the AP-3
CC complex, the BLOC-1 complex is required to target membrane protein
CC cargos into vesicles assembled at cell bodies for delivery into
CC neurites and nerve terminals. The BLOC-1 complex, in association with
CC SNARE proteins, is also proposed to be involved in neurite extension.
CC Associates with the BLOC-2 complex to facilitate the transport of TYRP1
CC independent of AP-3 function. Plays a role in synaptic vesicle
CC trafficking and in neurotransmitter release. Plays a role in the
CC regulation of cell surface exposure of DRD2. May play a role in actin
CC cytoskeleton reorganization and neurite outgrowth. May modulate MAPK8
CC phosphorylation. Appears to promote neuronal transmission and viability
CC through regulating the expression of SNAP25 and SYN1, modulating PI3-
CC kinase-Akt signaling and influencing glutamatergic release. Regulates
CC the expression of SYN1 through binding to its promoter. Modulates
CC prefrontal cortical activity via the dopamine/D2 pathway (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via its coiled coil domain) with KXD1. Interacts
CC with CMYA5, PI4K2 and RNF151 (By similarity). Component of the
CC biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed
CC of at least BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6,
CC DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Interacts directly in the complex
CC with BLOC1S5, BLOC1S6 and SNAPIN/BLOC1S8. The BLOC-1 complex associates
CC with the AP-3 protein complex and membrane protein cargos. This BLOC-1
CC complex also associates with the BLOC-2 complex in endosomes. Binds to
CC DTNA and DTNB but may not be a physiological binding partner. Interacts
CC with the DNA-dependent protein kinase complex DNA-PK; the interaction
CC phosphorylates DTNBP1 in vitro. Interacts directly in this complex with
CC XRCC5 and XRCC6. Interacts with AP3M1, AP3B2 and TRIM32. Interacts with
CC XPO1; the interaction exports DTNBP1 out of the nucleus (By
CC similarity). {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; Peripheral membrane protein; Cytoplasmic
CC side. Endosome membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Melanosome membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Nucleus {ECO:0000250}. Postsynaptic density.
CC Presynaptic cell membrane. Endoplasmic reticulum {ECO:0000250}.
CC Note=Mainly cytoplasmic but shuttles between the cytoplasm and nucleus.
CC Exported out of the nucleus via its NES in a XPO1-dependent manner.
CC Nuclear localization is required for regulation of the expression of
CC genes such as SYN1 (By similarity). Detected in neuron cell bodies,
CC axons and 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. Occasionally detected at the membrane of pigmented
CC melanosomes in cultured melanoma cells. The BLOC-1 complex associates
CC with the BLOC-2 complex in early endosome-associated tubules.
CC Associated with the AP-3 complex at presynaptic terminals (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by TRIM32. Ubiquitination leads to DTNBP1
CC degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dysbindin family. {ECO:0000305}.
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DR EMBL; BC113232; AAI13233.1; -; mRNA.
DR RefSeq; NP_001039412.1; NM_001045947.1.
DR AlphaFoldDB; Q2HJA5; -.
DR SMR; Q2HJA5; -.
DR STRING; 9913.ENSBTAP00000051067; -.
DR PaxDb; Q2HJA5; -.
DR PRIDE; Q2HJA5; -.
DR Ensembl; ENSBTAT00000057192; ENSBTAP00000051067; ENSBTAG00000012939.
DR GeneID; 506612; -.
DR KEGG; bta:506612; -.
DR CTD; 84062; -.
DR VEuPathDB; HostDB:ENSBTAG00000012939; -.
DR VGNC; VGNC:28233; DTNBP1.
DR eggNOG; ENOG502QRS9; Eukaryota.
DR GeneTree; ENSGT00940000156479; -.
DR InParanoid; Q2HJA5; -.
DR OrthoDB; 862376at2759; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000012939; Expressed in temporal cortex and 104 other tissues.
DR ExpressionAtlas; Q2HJA5; 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:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
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:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
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:0014059; P:regulation of dopamine secretion; 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 Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Endosome; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Synapse; Ubl conjugation.
FT CHAIN 1..342
FT /note="Dysbindin"
FT /id="PRO_0000267209"
FT REGION 263..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 83..180
FT /evidence="ECO:0000255"
FT MOTIF 243..256
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EV8"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EV8"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EV8"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91WZ8"
SQ SEQUENCE 342 AA; 38207 MW; A22BEF406CF5DB92 CRC64;
MLETLRERLL SVQQDFTSGL KTLSDKSREA KAKNKPRTVP CLPKYSAGLE LLSRYEDTWA
ALHRRAKECA SAGERVDSEV VMLSAHWEKK QASLRDLQQQ LQQLPGLIAD LESLTASLTH
LEASFEEVEN HLLNLEDLCG QCELERHKHM QSQQLENYKK NKRKELETFK AELDAEHSQK
VLEMEQTQQL KLKERQKFFE EAFQQDMEQY LSTGYLQIAE RREPMGSMSS MEVNVDMLEQ
MDLMDISDQE ALDVFLNSGG EENTLLSPIS GPEASPGQDA VTLQVPTPSQ APATPPSSSS
PGTDPASRDP SEGGESPVVQ SDEEGVEVDT ALATLHSDDS DS
