BL1S5_MOUSE
ID BL1S5_MOUSE Reviewed; 185 AA.
AC Q8R015; Q3TCP2; Q8CAC9;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 5;
DE Short=BLOC-1 subunit 5;
DE AltName: Full=Protein Muted homolog;
GN Name=Bloc1s5; Synonyms=Mu, Muted;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISEASE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11912185; DOI=10.1093/hmg/11.6.697;
RA Zhang Q., Li W., Novak E.K., Karim A., Mishra V.S., Kingsmore S.F.,
RA Roe B.A., Suzuki T., Swank R.T.;
RT "The gene for the muted (mu) mouse, a model for Hermansky-Pudlak syndrome,
RT defines a novel protein which regulates vesicle trafficking.";
RL Hum. Mol. Genet. 11:697-706(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Hypothalamus, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, INTERACTION WITH BLOC1S6, AND IDENTIFICATION IN THE BLOC-1
RP COMPLEX.
RX PubMed=12019270; DOI=10.1074/jbc.m204011200;
RA Falcon-Perez J.M., Starcevic M., Gautam R., Dell'Angelica E.C.;
RT "BLOC-1, a novel complex containing the pallidin and muted proteins
RT involved in the biogenesis of melanosomes and platelet-dense granules.";
RL J. Biol. Chem. 277:28191-28199(2002).
RN [5]
RP IDENTIFICATION IN THE BLOC-1 COMPLEX, AND INTERACTION WITH BLOC1S4 AND
RP BLOC1S6.
RX PubMed=12576321; DOI=10.1182/blood-2003-01-0020;
RA Ciciotte S.L., Gwynn B., Moriyama K., Huizing M., Gahl W.A.,
RA Bonifacino J.S., Peters L.L.;
RT "Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a novel
RT protein that is part of the pallidin-muted complex (BLOC-1).";
RL Blood 101:4402-4407(2003).
RN [6]
RP INTERACTION WITH DTNBP1.
RX PubMed=12923531; DOI=10.1038/ng1229;
RA Li W., Zhang Q., Oiso N., Novak E.K., Gautam R., O'Brien E.P.,
RA Tinsley C.L., Blake D.J., Spritz R.A., Copeland N.G., Jenkins N.A.,
RA Amato D., Roe B.A., Starcevic M., Dell'Angelica E.C., Elliott R.W.,
RA Mishra V., Kingsmore S.F., Paylor R.E., Swank R.T.;
RT "Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a
RT member of the biogenesis of lysosome-related organelles complex 1 (BLOC-
RT 1).";
RL Nat. Genet. 35:84-89(2003).
RN [7]
RP FUNCTION.
RX PubMed=16760431; DOI=10.1091/mbc.e06-02-0103;
RA Salazar G., Craige B., Styers M.L., Newell-Litwa K.A., Doucette M.M.,
RA Wainer B.H., Falcon-Perez J.M., Dell'Angelica E.C., Peden A.A., Werner E.,
RA Faundez V.;
RT "BLOC-1 complex deficiency alters the targeting of adaptor protein complex-
RT 3 cargoes.";
RL Mol. Biol. Cell 17:4014-4026(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION.
RX PubMed=19546860; DOI=10.1038/mp.2009.58;
RA Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R.,
RA Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C.,
RA Dell'Angelica E.C.;
RT "The dysbindin-containing complex (BLOC-1) in brain: developmental
RT regulation, interaction with SNARE proteins and role in neurite
RT outgrowth.";
RL Mol. Psychiatry 15:204-215(2010).
RN [10]
RP FUNCTION, ASSOCIATION WITH THE AP-3 COMPLEX, AND INTERACTION WITH PI4K2A
RP AND BLOC1S6.
RX PubMed=21998198; DOI=10.1091/mbc.e11-07-0592;
RA Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B.,
RA Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.;
RT "The schizophrenia susceptibility factor dysbindin and its associated
RT complex sort cargoes from cell bodies to the synapse.";
RL Mol. Biol. Cell 22:4854-4867(2011).
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 Plays a role in intracellular vesicle trafficking.
CC {ECO:0000269|PubMed:11912185, ECO:0000269|PubMed:12019270,
CC ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860,
CC ECO:0000269|PubMed:21998198}.
CC -!- SUBUNIT: Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3,
CC BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8 (By
CC similarity). Component of the biogenesis of lysosome-related organelles
CC complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4,
CC BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex
CC associates with the AP-3 protein complex and membrane protein cargos.
CC Interacts with BLOC1S4, BLOC1S6, DTNBP1/BLOC1S7 and PI4K2A.
CC {ECO:0000250, ECO:0000269|PubMed:12019270, ECO:0000269|PubMed:12576321,
CC ECO:0000269|PubMed:12923531, ECO:0000269|PubMed:21998198}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R015-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R015-2; Sequence=VSP_008196;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, spleen, lung, kidney and
CC testis. {ECO:0000269|PubMed:11912185}.
CC -!- DISEASE: Note=Defects in Muted are the cause of the Muted (mu) mutant,
CC which is characterized by light eyes at birth, hypopigmentation of the
CC coat, platelet storage pool deficiency and lysosomal hyposecretion.
CC {ECO:0000269|PubMed:11912185}.
CC -!- SIMILARITY: Belongs to the BLOC1S5 family. {ECO:0000305}.
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DR EMBL; AF426433; AAL99384.1; -; mRNA.
DR EMBL; AK039050; BAC30220.1; -; mRNA.
DR EMBL; AK075808; BAC35976.1; -; mRNA.
DR EMBL; AK147762; BAE28121.1; -; mRNA.
DR EMBL; AK170614; BAE41913.1; -; mRNA.
DR EMBL; BC023184; AAH23184.1; -; mRNA.
DR EMBL; BC024720; AAH24720.1; -; mRNA.
DR CCDS; CCDS26464.1; -. [Q8R015-1]
DR RefSeq; NP_620702.1; NM_139063.1. [Q8R015-1]
DR AlphaFoldDB; Q8R015; -.
DR SMR; Q8R015; -.
DR BioGRID; 201605; 2.
DR ComplexPortal; CPX-1913; BLOC-1 complex.
DR CORUM; Q8R015; -.
DR STRING; 10090.ENSMUSP00000036614; -.
DR iPTMnet; Q8R015; -.
DR PhosphoSitePlus; Q8R015; -.
DR EPD; Q8R015; -.
DR MaxQB; Q8R015; -.
DR PaxDb; Q8R015; -.
DR PRIDE; Q8R015; -.
DR ProteomicsDB; 273692; -. [Q8R015-1]
DR ProteomicsDB; 273693; -. [Q8R015-2]
DR DNASU; 17828; -.
DR Ensembl; ENSMUST00000035899; ENSMUSP00000036614; ENSMUSG00000038982. [Q8R015-1]
DR Ensembl; ENSMUST00000224902; ENSMUSP00000153368; ENSMUSG00000038982. [Q8R015-2]
DR GeneID; 17828; -.
DR KEGG; mmu:17828; -.
DR UCSC; uc007qdu.1; mouse. [Q8R015-1]
DR UCSC; uc007qdv.1; mouse. [Q8R015-2]
DR CTD; 63915; -.
DR MGI; MGI:2178598; Bloc1s5.
DR VEuPathDB; HostDB:ENSMUSG00000038982; -.
DR eggNOG; ENOG502S2QH; Eukaryota.
DR GeneTree; ENSGT00390000016974; -.
DR HOGENOM; CLU_110751_0_0_1; -.
DR InParanoid; Q8R015; -.
DR OMA; IQWEDFM; -.
DR OrthoDB; 1593497at2759; -.
DR PhylomeDB; Q8R015; -.
DR TreeFam; TF332943; -.
DR BioGRID-ORCS; 17828; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Bloc1s5; mouse.
DR PRO; PR:Q8R015; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8R015; protein.
DR Bgee; ENSMUSG00000038982; Expressed in epithelium of lens and 241 other tissues.
DR ExpressionAtlas; Q8R015; baseline and differential.
DR Genevisible; Q8R015; MM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031083; C:BLOC-1 complex; IDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; ISS:UniProtKB.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:UniProtKB.
DR GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
DR GO; GO:0035646; P:endosome to melanosome transport; ISS:UniProtKB.
DR GO; GO:0032438; P:melanosome organization; IC:ComplexPortal.
DR GO; GO:0032402; P:melanosome transport; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; NAS:UniProtKB.
DR GO; GO:0032474; P:otolith morphogenesis; IMP:MGI.
DR GO; GO:0050942; P:positive regulation of pigment cell differentiation; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:MGI.
DR InterPro; IPR017243; Bloc1s5.
DR PANTHER; PTHR31784; PTHR31784; 1.
DR Pfam; PF14942; Muted; 1.
DR PIRSF; PIRSF037610; BLOC-1_complex_muted_subunit; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8TDH9"
FT CHAIN 2..185
FT /note="Biogenesis of lysosome-related organelles complex 1
FT subunit 5"
FT /id="PRO_0000096653"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDH9"
FT VAR_SEQ 127..185
FT /note="VINDYLTASEKRRLVQWEEFVSGQPQRRAEVDEEHRRAVERLREQYAAMEKD
FT LAKFSTF -> GLLDPGLVDLGTLLTMSCRDPPVSDEPSCNAARNYSCLLHSRI (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008196"
SQ SEQUENCE 185 AA; 21283 MW; 0351D1A4AA7DC5CD CRC64;
MSGGGTETPV ACDAAQGGKK RDSLGTPGAA HLIIKDLGEI HSRLLDHRPV TQGEIRYFVK
EFEEKRGLRE LRVLKNLENT IQETNECLLP KCRETMECGL GETLQRLQAA NDSICRLQQR
EQERKKVIND YLTASEKRRL VQWEEFVSGQ PQRRAEVDEE HRRAVERLRE QYAAMEKDLA
KFSTF
