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Q8R015

- BL1S5_MOUSE

UniProt

Q8R015 - BL1S5_MOUSE

Protein

Biogenesis of lysosome-related organelles complex 1 subunit 5

Gene

Bloc1s5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    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. Plays a role in intracellular vesicle trafficking.5 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. anterograde axon cargo transport Source: UniProtKB
    2. anterograde synaptic vesicle transport Source: UniProtKB
    3. developmental pigmentation Source: MGI
    4. endosome to melanosome transport Source: UniProtKB
    5. melanosome transport Source: UniProtKB
    6. neuron projection development Source: UniProtKB
    7. otolith morphogenesis Source: MGI
    8. positive regulation of pigment cell differentiation Source: UniProtKB
    9. vesicle-mediated transport Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biogenesis of lysosome-related organelles complex 1 subunit 5
    Short name:
    BLOC-1 subunit 5
    Alternative name(s):
    Protein Muted homolog
    Gene namesi
    Name:Bloc1s5
    Synonyms:Mu, Muted
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:2178598. Bloc1s5.

    Subcellular locationi

    GO - Cellular componenti

    1. BLOC-1 complex Source: UniProtKB
    2. transport vesicle Source: UniProtKB

    Pathology & Biotechi

    Involvement in diseasei

    Defects in Muted are the cause of the Muted (mu) mutant, which is characterized by light eyes at birth, hypopigmentation of the coat, platelet storage pool deficiency and lysosomal hyposecretion.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 185184Biogenesis of lysosome-related organelles complex 1 subunit 5PRO_0000096653Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ8R015.
    PRIDEiQ8R015.

    PTM databases

    PhosphoSiteiQ8R015.

    Expressioni

    Tissue specificityi

    Detected in heart, brain, spleen, lung, kidney and testis.1 Publication

    Gene expression databases

    BgeeiQ8R015.
    CleanExiMM_MUTED.
    GenevestigatoriQ8R015.

    Interactioni

    Subunit structurei

    Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8 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. Interacts with BLOC1S4, BLOC1S6, DTNBP1/BLOC1S7 and PI4K2A.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi201605. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8R015.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the BLOC1S5 family.Curated

    Phylogenomic databases

    eggNOGiNOG43601.
    GeneTreeiENSGT00390000016974.
    HOGENOMiHOG000290689.
    HOVERGENiHBG045594.
    InParanoidiQ8R015.
    OMAiEQYSEME.
    OrthoDBiEOG7RZ5RX.
    PhylomeDBiQ8R015.
    TreeFamiTF332943.

    Family and domain databases

    InterProiIPR017243. Bloc1s5.
    [Graphical view]
    PANTHERiPTHR31784. PTHR31784. 1 hit.
    PfamiPF14942. Muted. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037610. BLOC-1_complex_muted_subunit. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8R015-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSGGGTETPV ACDAAQGGKK RDSLGTPGAA HLIIKDLGEI HSRLLDHRPV    50
    TQGEIRYFVK EFEEKRGLRE LRVLKNLENT IQETNECLLP KCRETMECGL 100
    GETLQRLQAA NDSICRLQQR EQERKKVIND YLTASEKRRL VQWEEFVSGQ 150
    PQRRAEVDEE HRRAVERLRE QYAAMEKDLA KFSTF 185
    Length:185
    Mass (Da):21,283
    Last modified:June 1, 2002 - v1
    Checksum:i0351D1A4AA7DC5CD
    GO
    Isoform 2 (identifier: Q8R015-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         127-185: VINDYLTASE...EKDLAKFSTF → GLLDPGLVDL...NYSCLLHSRI

    Note: No experimental confirmation available.

    Show »
    Length:169
    Mass (Da):18,770
    Checksum:iB1635F8B4AB96054
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei127 – 18559VINDY…KFSTF → GLLDPGLVDLGTLLTMSCRD PPVSDEPSCNAARNYSCLLH SRI in isoform 2. 1 PublicationVSP_008196Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF426433 mRNA. Translation: AAL99384.1.
    AK039050 mRNA. Translation: BAC30220.1.
    AK075808 mRNA. Translation: BAC35976.1.
    AK147762 mRNA. Translation: BAE28121.1.
    AK170614 mRNA. Translation: BAE41913.1.
    BC023184 mRNA. Translation: AAH23184.1.
    BC024720 mRNA. Translation: AAH24720.1.
    CCDSiCCDS26464.1. [Q8R015-1]
    RefSeqiNP_620702.1. NM_139063.1. [Q8R015-1]
    UniGeneiMm.261554.

    Genome annotation databases

    EnsembliENSMUST00000035899; ENSMUSP00000036614; ENSMUSG00000038982. [Q8R015-1]
    GeneIDi17828.
    KEGGimmu:17828.
    UCSCiuc007qdu.1. mouse. [Q8R015-1]
    uc007qdv.1. mouse. [Q8R015-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF426433 mRNA. Translation: AAL99384.1 .
    AK039050 mRNA. Translation: BAC30220.1 .
    AK075808 mRNA. Translation: BAC35976.1 .
    AK147762 mRNA. Translation: BAE28121.1 .
    AK170614 mRNA. Translation: BAE41913.1 .
    BC023184 mRNA. Translation: AAH23184.1 .
    BC024720 mRNA. Translation: AAH24720.1 .
    CCDSi CCDS26464.1. [Q8R015-1 ]
    RefSeqi NP_620702.1. NM_139063.1. [Q8R015-1 ]
    UniGenei Mm.261554.

    3D structure databases

    ProteinModelPortali Q8R015.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201605. 2 interactions.

    PTM databases

    PhosphoSitei Q8R015.

    Proteomic databases

    PaxDbi Q8R015.
    PRIDEi Q8R015.

    Protocols and materials databases

    DNASUi 17828.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000035899 ; ENSMUSP00000036614 ; ENSMUSG00000038982 . [Q8R015-1 ]
    GeneIDi 17828.
    KEGGi mmu:17828.
    UCSCi uc007qdu.1. mouse. [Q8R015-1 ]
    uc007qdv.1. mouse. [Q8R015-2 ]

    Organism-specific databases

    CTDi 63915.
    MGIi MGI:2178598. Bloc1s5.

    Phylogenomic databases

    eggNOGi NOG43601.
    GeneTreei ENSGT00390000016974.
    HOGENOMi HOG000290689.
    HOVERGENi HBG045594.
    InParanoidi Q8R015.
    OMAi EQYSEME.
    OrthoDBi EOG7RZ5RX.
    PhylomeDBi Q8R015.
    TreeFami TF332943.

    Miscellaneous databases

    NextBioi 292525.
    PROi Q8R015.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8R015.
    CleanExi MM_MUTED.
    Genevestigatori Q8R015.

    Family and domain databases

    InterProi IPR017243. Bloc1s5.
    [Graphical view ]
    PANTHERi PTHR31784. PTHR31784. 1 hit.
    Pfami PF14942. Muted. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037610. BLOC-1_complex_muted_subunit. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The gene for the muted (mu) mouse, a model for Hermansky-Pudlak syndrome, defines a novel protein which regulates vesicle trafficking."
      Zhang Q., Li W., Novak E.K., Karim A., Mishra V.S., Kingsmore S.F., Roe B.A., Suzuki T., Swank R.T.
      Hum. Mol. Genet. 11:697-706(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISEASE, TISSUE SPECIFICITY.
      Strain: C57BL/6J.
    2. "The transcriptional landscape of the mammalian genome."
      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.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J and NOD.
      Tissue: Hypothalamus and Pancreas.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Eye.
    4. "BLOC-1, a novel complex containing the pallidin and muted proteins involved in the biogenesis of melanosomes and platelet-dense granules."
      Falcon-Perez J.M., Starcevic M., Gautam R., Dell'Angelica E.C.
      J. Biol. Chem. 277:28191-28199(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BLOC1S6, IDENTIFICATION IN THE BLOC-1 COMPLEX.
    5. "Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a novel protein that is part of the pallidin-muted complex (BLOC-1)."
      Ciciotte S.L., Gwynn B., Moriyama K., Huizing M., Gahl W.A., Bonifacino J.S., Peters L.L.
      Blood 101:4402-4407(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BLOC-1 COMPLEX, INTERACTION WITH BLOC1S4 AND BLOC1S6.
    6. "Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (BLOC-1)."
      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.
      Nat. Genet. 35:84-89(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DTNBP1.
    7. Cited for: FUNCTION.
    8. "The dysbindin-containing complex (BLOC-1) in brain: developmental regulation, interaction with SNARE proteins and role in neurite outgrowth."
      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.
      Mol. Psychiatry 15:204-215(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The schizophrenia susceptibility factor dysbindin and its associated complex sort cargoes from cell bodies to the synapse."
      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.
      Mol. Biol. Cell 22:4854-4867(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH THE AP-3 COMPLEX, INTERACTION WITH PI4K2A AND BLOC1S6.

    Entry informationi

    Entry nameiBL1S5_MOUSE
    AccessioniPrimary (citable) accession number: Q8R015
    Secondary accession number(s): Q3TCP2, Q8CAC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 9, 2003
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3