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Dysbindin (Biogenesis of lysosome-related organelles complex 1 subunit 8) (BLOC-1 subunit 8) (Dysbindin-1) (Dystrobrevin-binding protein 1) (Hermansky-Pudlak syndrome 7 protein homolog) (HPS7 protein homolog)

 DTBP1_MOUSE             Reviewed;         352 AA.
Q91WZ8; Q3TWK1; Q6WXQ1; Q80ZN4; Q9CY43;
28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 127.
RecName: Full=Dysbindin;
AltName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 8;
Short=BLOC-1 subunit 8;
AltName: Full=Dysbindin-1;
AltName: Full=Dystrobrevin-binding protein 1;
AltName: Full=Hermansky-Pudlak syndrome 7 protein homolog;
Short=HPS7 protein homolog;
Name=Dtnbp1; Synonyms=Bloc1s8, Sdy;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
INTERACTION WITH DTNA AND DTNB, AND SUBCELLULAR LOCATION.
STRAIN=C57BL/6J; TISSUE=Brain, and Liver;
PubMed=11316798; DOI=10.1074/jbc.M010418200;
Benson M.A., Newey S.E., Martin-Rendon E., Hawkes R., Blake D.J.;
"Dysbindin, a novel coiled-coil-containing protein that interacts with
the dystrobrevins in muscle and brain.";
J. Biol. Chem. 276:24232-24241(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, ALTERNATIVE
SPLICING, TISSUE SPECIFICITY, INTERACTION WITH DTNB; BLOC1S5 AND
BLOC1S6, AND DISEASE.
STRAIN=DBA/2J; TISSUE=Kidney;
PubMed=12923531; DOI=10.1038/ng1229;
Li W., Zhang Q., Oiso N., Novak E.K., Gautam R., O'Brien E.P.,
Tinsley C.L., Blake D.J., Spritz R.A., Copeland N.G., Jenkins N.A.,
Amato D., Roe B.A., Starcevic M., Dell'Angelica E.C., Elliott R.W.,
Mishra V., Kingsmore S.F., Paylor R.E., Swank R.T.;
"Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant
dysbindin, a member of the biogenesis of lysosome-related organelles
complex 1 (BLOC-1).";
Nat. Genet. 35:84-89(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N-3; TISSUE=Limb, Liver, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
DISEASE.
PubMed=1936982;
Swank R.T., Sweet H.O., Davisson M.T., Reddington M., Novak E.K.;
"Sandy: a new mouse model for platelet storage pool deficiency.";
Genet. Res. 58:51-62(1991).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=15345706; DOI=10.1093/hmg/ddh280;
Numakawa T., Yagasaki Y., Ishimoto T., Okada T., Suzuki T., Iwata N.,
Ozaki N., Taguchi T., Tatsumi M., Kamijima K., Straub R.E.,
Weinberger D.R., Kunugi H., Hashimoto R.;
"Evidence of novel neuronal functions of dysbindin, a susceptibility
gene for schizophrenia.";
Hum. Mol. Genet. 13:2699-2708(2004).
[7]
INTERACTION WITH CMYA5.
PubMed=14688250; DOI=10.1074/jbc.M312664200;
Benson M.A., Tinsley C.L., Blake D.J.;
"Myospryn is a novel binding partner for dysbindin in muscle.";
J. Biol. Chem. 279:10450-10458(2004).
[8]
FUNCTION, AND SUBUNIT.
PubMed=16448387; DOI=10.1042/BJ20051965;
Nazarian R., Starcevic M., Spencer M.J., Dell'Angelica E.C.;
"Reinvestigation of the dysbindin subunit of BLOC-1 (biogenesis of
lysosome-related organelles complex-1) as a dystrobrevin-binding
protein.";
Biochem. J. 395:587-598(2006).
[9]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH SNAPIN.
PubMed=16980328; DOI=10.1093/hmg/ddl246;
Talbot K., Cho D.S., Ong W.Y., Benson M.A., Han L.Y., Kazi H.A.,
Kamins J., Hahn C.G., Blake D.J., Arnold S.E.;
"Dysbindin-1 is a synaptic and microtubular protein that binds brain
snapin.";
Hum. Mol. Genet. 15:3041-3054(2006).
[10]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=16837549; DOI=10.1091/mbc.E06-05-0379;
Di Pietro S.M., Falcon-Perez J.M., Tenza D., Setty S.R., Marks M.S.,
Raposo G., Dell'Angelica E.C.;
"BLOC-1 interacts with BLOC-2 and the AP-3 complex to facilitate
protein trafficking on endosomes.";
Mol. Biol. Cell 17:4027-4038(2006).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16760431; DOI=10.1091/mbc.E06-02-0103;
Salazar G., Craige B., Styers M.L., Newell-Litwa K.A., Doucette M.M.,
Wainer B.H., Falcon-Perez J.M., Dell'Angelica E.C., Peden A.A.,
Werner E., Faundez V.;
"BLOC-1 complex deficiency alters the targeting of adaptor protein
complex-3 cargoes.";
Mol. Biol. Cell 17:4014-4026(2006).
[12]
INTERACTION WITH RNF151, AND SUBCELLULAR LOCATION.
PubMed=17577571; DOI=10.1016/j.abb.2007.05.013;
Nian H., Fan C., Liao S., Shi Y., Zhang K., Liu Y., Han C.;
"RNF151, a testis-specific RING finger protein, interacts with
dysbindin.";
Arch. Biochem. Biophys. 465:157-163(2007).
[13]
FUNCTION, AND DISEASE.
PubMed=18555792; DOI=10.1016/j.bbrc.2008.06.016;
Hattori S., Murotani T., Matsuzaki S., Ishizuka T., Kumamoto N.,
Takeda M., Tohyama M., Yamatodani A., Kunugi H., Hashimoto R.;
"Behavioral abnormalities and dopamine reductions in sdy mutant mice
with a deletion in Dtnbp1, a susceptibility gene for schizophrenia.";
Biochem. Biophys. Res. Commun. 373:298-302(2008).
[14]
DISEASE, AND FUNCTION.
PubMed=18504299; DOI=10.1083/jcb.200711021;
Chen X.W., Feng Y.Q., Hao C.J., Guo X.L., He X., Zhou Z.Y., Guo N.,
Huang H.P., Xiong W., Zheng H., Zuo P.L., Zhang C.X., Li W., Zhou Z.;
"DTNBP1, a schizophrenia susceptibility gene, affects kinetics of
transmitter release.";
J. Cell Biol. 181:791-801(2008).
[15]
DISEASE.
PubMed=18945333; DOI=10.1186/1756-6606-1-11;
Takao K., Toyama K., Nakanishi K., Hattori S., Takamura H., Takeda M.,
Miyakawa T., Hashimoto R.;
"Impaired long-term memory retention and working memory in sdy mutant
mice with a deletion in Dtnbp1, a susceptibility gene for
schizophrenia.";
Mol. Brain 1:11-11(2008).
[16]
REVIEW.
Talbot K., Ong W.-Y., Blake D.J., Tang J., Louneva N., Carlson G.C.,
Arnold S.E.;
"Dysbindin-1 and its protein family with special attention to the
potential role of dysbindin-1 in neuronal functions and the
pathophysiology of schizophrenia.";
(In) Javitt D.C., Kantrowitz J. (eds.);
Handbook of neurochemistry and molecular neurobiology (3rd ed.),
pp.27:107-241, Springer Science, New York (2009).
[17]
DISEASE, AND FUNCTION.
PubMed=18984010; DOI=10.1016/j.bbr.2008.10.011;
Bhardwaj S.K., Baharnoori M., Sharif-Askari B., Kamath A.,
Williams S., Srivastava L.K.;
"Behavioral characterization of dysbindin-1 deficient sandy mice.";
Behav. Brain Res. 197:435-441(2009).
[18]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19094965; DOI=10.1016/j.bbrc.2008.12.017;
Kubota K., Kumamoto N., Matsuzaki S., Hashimoto R., Hattori T.,
Okuda H., Takamura H., Takeda M., Katayama T., Tohyama M.;
"Dysbindin engages in c-Jun N-terminal kinase activity and
cytoskeletal organization.";
Biochem. Biophys. Res. Commun. 379:191-195(2009).
[19]
DISEASE.
PubMed=19220483; DOI=10.1111/j.1601-183X.2009.00477.x;
Cox M.M., Tucker A.M., Tang J., Talbot K., Richer D.C., Yeh L.,
Arnold S.E.;
"Neurobehavioral abnormalities in the dysbindin-1 mutant, sandy, on a
C57BL/6J genetic background.";
Genes Brain Behav. 8:390-397(2009).
[20]
REVIEW ON DISEASE.
PubMed=20302821; DOI=10.1016/S0079-6123(09)17910-4;
Talbot K.;
"The sandy (sdy) mouse: a dysbindin-1 mutant relevant to schizophrenia
research.";
Prog. Brain Res. 179:87-94(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340 AND SER-343, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[22]
DISEASE, AND FUNCTION.
PubMed=20921223; DOI=10.1074/jbc.M110.107912;
Fei E., Ma X., Zhu C., Xue T., Yan J., Xu Y., Zhou J., Wang G.;
"Nucleocytoplasmic shuttling of dysbindin-1, a schizophrenia-related
protein, regulates synapsin I expression.";
J. Biol. Chem. 285:38630-38640(2010).
[23]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19546860; DOI=10.1038/mp.2009.58;
Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R.,
Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C.,
Dell'Angelica E.C.;
"The dysbindin-containing complex (BLOC-1) in brain: developmental
regulation, interaction with SNARE proteins and role in neurite
outgrowth.";
Mol. Psychiatry 15:204-215(2010).
[24]
TISSUE SPECIFICITY, INTERACTION WITH THE AP-C COMPLEX, AND FUNCTION.
PubMed=19428785; DOI=10.1016/j.neuint.2009.01.014;
Taneichi-Kuroda S., Taya S., Hikita T., Fujino Y., Kaibuchi K.;
"Direct interaction of dysbindin with the AP-3 complex via its mu
subunit.";
Neurochem. Int. 54:431-438(2009).
[25]
FUNCTION.
PubMed=20045719; DOI=10.1016/j.neulet.2009.12.071;
Nagai T., Kitahara Y., Shiraki A., Hikita T., Taya S., Kaibuchi K.,
Yamada K.;
"Dysfunction of dopamine release in the prefrontal cortex of dysbindin
deficient sandy mice: an in vivo microdialysis study.";
Neurosci. Lett. 470:134-138(2010).
[26]
INTERACTION WITH AP3B2.
PubMed=19142223; DOI=10.1371/journal.pone.0004199;
Oyama S., Yamakawa H., Sasagawa N., Hosoi Y., Futai E., Ishiura S.;
"Dysbindin-1, a schizophrenia-related protein, functionally interacts
with the DNA-dependent protein kinase complex in an isoform-dependent
manner.";
PLoS ONE 4:E4199-E4199(2009).
[27]
FUNCTION.
PubMed=19887632; DOI=10.1073/pnas.0904289106;
Ji Y., Yang F., Papaleo F., Wang H.X., Gao W.J., Weinberger D.R.,
Lu B.;
"Role of dysbindin in dopamine receptor trafficking and cortical GABA
function.";
Proc. Natl. Acad. Sci. U.S.A. 106:19593-19598(2009).
[28]
FUNCTION, ASSOCIATION WITH THE AP-3 COMPLEX, AND INTERACTION WITH
PI4K2A.
PubMed=21998198; DOI=10.1091/mbc.E11-07-0592;
Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A.,
Craige B., Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.;
"The schizophrenia susceptibility factor dysbindin and its associated
complex sort cargoes from cell bodies to the synapse.";
Mol. Biol. Cell 22:4854-4867(2011).
[29]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=20956979; DOI=10.1038/mp.2010.106;
Papaleo F., Yang F., Garcia S., Chen J., Lu B., Crawley J.N.,
Weinberger D.R.;
"Dysbindin-1 modulates prefrontal cortical activity and schizophrenia-
like behaviors via dopamine/D2 pathways.";
Mol. Psychiatry 17:85-98(2012).
[30]
INTERACTION WITH KXD1.
PubMed=22554196; DOI=10.1111/j.1600-0854.2012.01375.x;
Yang Q., He X., Yang L., Zhou Z., Cullinane A.R., Wei A., Zhang Z.,
Hao Z., Zhang A., He M., Feng Y., Gao X., Gahl W.A., Huizing M.,
Li W.;
"The BLOS1-interacting protein KXD1 is involved in the biogenesis of
lysosome-related organelles.";
Traffic 13:1160-1169(2012).
-!- FUNCTION: Component of the BLOC-1 complex, a complex that is
required for normal biogenesis of lysosome-related organelles
(LRO), such as platelet dense granules and melanosomes. In concert
with the AP-3 complex, the BLOC-1 complex is required to target
membrane protein cargos into vesicles assembled at cell bodies for
delivery into neurites and nerve terminals. The BLOC-1 complex, in
association with SNARE proteins, is also proposed to be involved
in neurite extension. Associates with the BLOC-2 complex to
facilitate the transport of TYRP1 independent of AP-3 function.
Plays a role in synaptic vesicle trafficking and in
neurotransmitter release. Plays a role in the regulation of cell
surface exposure of DRD2. May play a role in actin cytoskeleton
reorganization and neurite outgrowth. May modulate MAPK8
phosphorylation. Appears to promote neuronal transmission and
viability through regulating the expression of SNAP25 and SYN1,
modulating PI3-kinase-Akt signaling and influencing glutamatergic
release. Regulates the expression of SYN1 through binding to its
promoter. Modulates prefrontal cortical activity via the
dopamine/D2 pathway. {ECO:0000269|PubMed:12923531,
ECO:0000269|PubMed:15345706, ECO:0000269|PubMed:16448387,
ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:16837549,
ECO:0000269|PubMed:18504299, ECO:0000269|PubMed:18555792,
ECO:0000269|PubMed:18984010, ECO:0000269|PubMed:19094965,
ECO:0000269|PubMed:19428785, ECO:0000269|PubMed:19546860,
ECO:0000269|PubMed:19887632, ECO:0000269|PubMed:20045719,
ECO:0000269|PubMed:20921223, ECO:0000269|PubMed:20956979,
ECO:0000269|PubMed:21998198}.
-!- SUBUNIT: Interacts with AP3M1 and TRIM32. Interacts (isoform 1 and
isoform 2 only) with the DNA-dependent protein kinase complex DNA-
PK; the interaction phosphorylates DTNBP1 in vitro. Interacts
directly in this complex with XRCC5 and XRCC6. Interacts with
XPO1; the interaction exports DTNBP1 out of the nucleus (By
similarity). Component of the biogenesis of lysosome-related
organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2,
BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and
SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3
protein complex and membrane protein cargos. This BLOC-1 complex
also associates with the BLOC-2 complex in endosomes. Binds to
DTNA and DTNB but may not be a physiological binding partner
(PubMed:16448387 and PubMed:16980328). Interacts (via its coiled
coil domain) with KXD1. Interacts with AP3B2, BLOC1S5, BLOC1S6,
CMYA5, PI4K2, RNF151 and SNAPIN/BLOC1S8. Interacts with XPO1; the
interaction exports DTNBP1 out of the nucleus. {ECO:0000250,
ECO:0000269|PubMed:11316798, ECO:0000269|PubMed:12923531,
ECO:0000269|PubMed:14688250, ECO:0000269|PubMed:16448387,
ECO:0000269|PubMed:16837549, ECO:0000269|PubMed:16980328,
ECO:0000269|PubMed:17577571, ECO:0000269|PubMed:19142223,
ECO:0000269|PubMed:19428785, ECO:0000269|PubMed:19546860,
ECO:0000269|PubMed:21998198, ECO:0000269|PubMed:22554196}.
-!- INTERACTION:
Q70KF4:Cmya5; NbExp=5; IntAct=EBI-643186, EBI-782290;
Q9D2N4:Dtna; NbExp=3; IntAct=EBI-643186, EBI-296019;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Cytoplasmic vesicle
membrane; Peripheral membrane protein; Cytoplasmic side. Endosome
membrane; Peripheral membrane protein; Cytoplasmic side.
Melanosome membrane; Peripheral membrane protein; Cytoplasmic
side. Cell junction, synapse, postsynaptic cell membrane,
postsynaptic density. Endoplasmic reticulum {ECO:0000250}.
Nucleus. Note=Mainly cytoplasmic but shuttles between the
cytoplasm and nucleus. Exported out of the nucleus via its NES in
a XPO1-dependent manner. Nuclear localization is required for
regulation of the expression of genes such as SYN1. Detected in
neuron cell bodies, axons and dendrites. Mainly located to the
postsynaptic density. Detected at tubulovesicular elements in the
vicinity of the Golgi apparatus and of melanosomes. Occasionally
detected at the membrane of pigmented melanosomes in cultured
melanoma cells (By similarity). The BLOC-1 complex associates with
the BLOC-2 complex in early endosome-associated tubules.
Associated with the AP-3 complex at presynaptic terminals.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Cytoplasmic vesicle
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, secretory
vesicle, synaptic vesicle membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Endosome membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Melanosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Cell junction, synapse,
postsynaptic cell membrane. Endoplasmic reticulum {ECO:0000250}.
Note=Exclusivley cytoplasmic. Predominantly found in the
postsynaptic density (PSD). Little association with synaptic
vesicles (By similarity). The BLOC-1 complex associates with the
BLOC-2 complex in early endosome-associated tubules. vesicle
membranes and microtubules. Associated with the AP-3 complex at
presynaptic terminals. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Dysbindin 1-A;
IsoId=Q91WZ8-1; Sequence=Displayed;
Name=2;
IsoId=Q91WZ8-2; Sequence=VSP_009024;
Name=3; Synonyms=Dysbindin 1-C;
IsoId=Q91WZ8-3; Sequence=VSP_021939;
-!- TISSUE SPECIFICITY: Detected in brain, in hippocampus and dentate
gyrus neurons. Detected at axon bundles and axon terminals,
notably in the cerebellum and hippocampus. Detected in neuropil in
hippocampus, lateral septum, basal ganglia and substantia nigra.
Highly expressed in pyramidal cells of hippocampus CA2 and CA3.
Detected at the heart and skeletal muscle sarcolemma (at protein
level). Ubiquitously expressed. The highest expression is observed
in testis, liver, kidney, brain, heart and lung. Expressed at
lower levels in stomach and small intestine.
{ECO:0000269|PubMed:11316798, ECO:0000269|PubMed:12923531,
ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:16980328,
ECO:0000269|PubMed:19428785, ECO:0000269|PubMed:19546860}.
-!- PTM: Ubiquitinated by TRIM32. Ubiquitination leads to DTNBP1
degradation. {ECO:0000250}.
-!- DISEASE: Note=Defects in Dtnbp1 are the cause of the sandy (sdy)
mutant phenotype, a model for human Hermansky-Pudlak syndrome
(HPS). Sdy mice lack dysbindin expression; they have a
characteristic sandy coat color and have much fewer melanosomes in
the retinal pigment epithelium and choroid. They are fully viable,
but present behavioral abnormalities. They have prolonged bleeding
times due to platelet storage pool deficiency, and lysosomal
storage defects. The number of electron-opaque platelet dense
granules is severely reduced, and the platelet serotonin content
is strongly reduced. Secretion of lysosomal enzymes from kidney
and from thrombin-stimulated platelets is depressed 2- and 3-fold,
and ceroid pigment is present in kidney. Sandy mice also display
impaired long-term memory retention and working memory and
schizophrenia-like behavioral abnormalities. Vesicle morphology
and kinetics of transmitter release are affected in both
neuroendocrine cells and hippocampal synapses, characterized by
larger vesicle size, slower quantal release, fewer release events
and reduced readily releasable pool (RRP). Expression levels of
SYN1 are lower in both the cortex and the hippocampal formation
(HF). {ECO:0000269|PubMed:12923531, ECO:0000269|PubMed:18504299,
ECO:0000269|PubMed:18555792, ECO:0000269|PubMed:18945333,
ECO:0000269|PubMed:18984010, ECO:0000269|PubMed:19220483,
ECO:0000269|PubMed:1936982, ECO:0000269|PubMed:20921223}.
-!- DISRUPTION PHENOTYPE: Null mice exhibit cognitive abnormalities
including schizophrenia-related behaviors such as impaired working
memory under stressful conditions. There is higher acoustic
startle reactivity to stimuli. Pyramidal neurons are hypoexcitable
on dopamine-2 receptor stimulation. There is reduced expression of
Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) and
CaMKKbeta in the medial prefrontal cortex mPFC. There is increased
expression levels of cell surface dopamine receptor D2 in cortical
neurons. Expression levels of SYN1 are lower in both cortex and in
the hippocampal formation (HF). {ECO:0000269|PubMed:15345706,
ECO:0000269|PubMed:19094965, ECO:0000269|PubMed:20956979}.
-!- SIMILARITY: Belongs to the dysbindin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH48682.1; Type=Frameshift; Positions=1; Evidence={ECO:0000305};
Sequence=BAE35265.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AJ404859; CAC37976.1; -; mRNA.
EMBL; AY265461; AAP91871.1; -; mRNA.
EMBL; AK010924; BAB27270.2; -; mRNA.
EMBL; AK159656; BAE35265.1; ALT_INIT; mRNA.
EMBL; BC018350; AAH18350.1; -; mRNA.
EMBL; BC048682; AAH48682.1; ALT_FRAME; mRNA.
EMBL; BC058574; AAH58574.1; -; mRNA.
CCDS; CCDS36647.1; -. [Q91WZ8-1]
RefSeq; NP_080048.2; NM_025772.4. [Q91WZ8-1]
UniGene; Mm.352311; -.
SMR; Q91WZ8; -.
BioGrid; 220491; 3.
CORUM; Q91WZ8; -.
IntAct; Q91WZ8; 4.
MINT; MINT-197141; -.
STRING; 10090.ENSMUSP00000072170; -.
iPTMnet; Q91WZ8; -.
PhosphoSitePlus; Q91WZ8; -.
EPD; Q91WZ8; -.
PaxDb; Q91WZ8; -.
PeptideAtlas; Q91WZ8; -.
PRIDE; Q91WZ8; -.
Ensembl; ENSMUST00000072329; ENSMUSP00000072170; ENSMUSG00000057531. [Q91WZ8-1]
Ensembl; ENSMUST00000222583; ENSMUSP00000152812; ENSMUSG00000057531. [Q91WZ8-3]
GeneID; 94245; -.
KEGG; mmu:94245; -.
UCSC; uc007qgw.1; mouse. [Q91WZ8-1]
CTD; 84062; -.
MGI; MGI:2137586; Dtnbp1.
eggNOG; ENOG410IF9S; Eukaryota.
eggNOG; ENOG4111YM1; LUCA.
GeneTree; ENSGT00390000010667; -.
HOGENOM; HOG000272621; -.
HOVERGEN; HBG051416; -.
InParanoid; Q91WZ8; -.
KO; K20189; -.
OMA; NYNAGAD; -.
PhylomeDB; Q91WZ8; -.
TreeFam; TF332997; -.
Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
ChiTaRS; Dtnbp1; mouse.
PRO; PR:Q91WZ8; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000057531; -.
CleanEx; MM_DTNBP1; -.
ExpressionAtlas; Q91WZ8; baseline and differential.
Genevisible; Q91WZ8; MM.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0031083; C:BLOC-1 complex; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0030426; C:growth cone; IDA:UniProtKB.
GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
GO; GO:0030496; C:midbody; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
GO; GO:0016528; C:sarcoplasm; IDA:MGI.
GO; GO:0030672; C:synaptic vesicle membrane; IDA:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:UniProtKB.
GO; GO:0007596; P:blood coagulation; IMP:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
GO; GO:0007517; P:muscle organ development; TAS:MGI.
GO; GO:0032091; P:negative regulation of protein binding; IMP:MGI.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:MGI.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; IDA:UniProtKB.
GO; GO:0006996; P:organelle organization; IDA:UniProtKB.
GO; GO:0060155; P:platelet dense granule organization; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IMP:UniProtKB.
GO; GO:0060159; P:regulation of dopamine receptor signaling pathway; ISS:UniProtKB.
GO; GO:0014059; P:regulation of dopamine secretion; IMP:UniProtKB.
GO; GO:0043506; P:regulation of JUN kinase activity; IMP:CACAO.
InterPro; IPR007531; Dysbindin.
PANTHER; PTHR16294; PTHR16294; 1.
Pfam; PF04440; Dysbindin; 1.
1: Evidence at protein level;
Albinism; Alternative splicing; Cell junction; Cell membrane;
Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Endoplasmic reticulum; Endosome; Hermansky-Pudlak syndrome; Membrane;
Nucleus; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Sensory transduction; Synapse; Ubl conjugation.
CHAIN 1 352 Dysbindin.
/FTId=PRO_0000191002.
REGION 173 325 Dysbindin.
COILED 88 176 {ECO:0000255}.
MOTIF 243 256 Nuclear export signal. {ECO:0000250}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000250|UniProtKB:Q96EV8}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000250|UniProtKB:Q96EV8}.
MOD_RES 340 340 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 81 Missing (in isoform 3).
{ECO:0000303|PubMed:12923531}.
/FTId=VSP_021939.
VAR_SEQ 171 222 Missing (in isoform 2).
{ECO:0000303|PubMed:11316798}.
/FTId=VSP_009024.
CONFLICT 251 251 A -> T (in Ref. 3; BAE35265).
{ECO:0000305}.
CONFLICT 280 280 E -> G (in Ref. 3; BAE35265).
{ECO:0000305}.
SEQUENCE 352 AA; 39651 MW; EE60FB10ECE95361 CRC64;
MLETLRERLL SVQQDFTSGL KTLSDKSREA KVKGKPRTAP RLPKYSAGLE LLSRYEDAWA
ALHRRAKECA DAGELVDSEV VMLSAHWEKK RTSLNELQGQ LQQLPALLQD LESLMASLAH
LETSFEEVEN HLLHLEDLCG QCELERHKQA QAQHLESYKK SKRKELEAFK AELDTEHTQK
ALEMEHTQQL KLKERQKFFE EAFQQDMEQY LSTGYLQIAE RREPMGSMSS MEVNVDVLEQ
MDLMDISDQE ALDVFLNSGG EDNIVMSPGV EMESNPNQNE MSLQIPSPSE SASQPPASPS
ACTDLDTADA PLIQSDEEEV QVDTALVTLH TDRKSTPGVS DDSDQCDSTQ DI


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