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Protein

Biogenesis of lysosome-related organelles complex 1 subunit 5

Gene

Bloc1s5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 - Biological processi

  • anterograde axon cargo transport Source: UniProtKB
  • anterograde synaptic vesicle transport Source: UniProtKB
  • developmental pigmentation Source: MGI
  • endosome to melanosome transport Source: UniProtKB
  • melanosome transport Source: UniProtKB
  • neuron projection development Source: UniProtKB
  • otolith morphogenesis Source: MGI
  • positive regulation of pigment cell differentiation Source: UniProtKB
  • vesicle-mediated transport Source: MGI
Complete GO annotation...

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 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:2178598. Bloc1s5.

Subcellular locationi

GO - Cellular componenti

  • BLOC-1 complex Source: UniProtKB
  • transport vesicle Source: UniProtKB
Complete GO annotation...

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.

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

MaxQBiQ8R015.
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.
GenevisibleiQ8R015. MM.

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.
STRINGi10090.ENSMUSP00000036614.

Structurei

3D structure databases

ProteinModelPortaliQ8R015.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the BLOC1S5 family.Curated

Phylogenomic databases

eggNOGiNOG43601.
GeneTreeiENSGT00390000016974.
HOGENOMiHOG000290689.
HOVERGENiHBG045594.
InParanoidiQ8R015.
OMAiVIQGEIR.
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. AlignAdd to basket

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

        10         20         30         40         50
MSGGGTETPV ACDAAQGGKK RDSLGTPGAA HLIIKDLGEI HSRLLDHRPV
60 70 80 90 100
TQGEIRYFVK EFEEKRGLRE LRVLKNLENT IQETNECLLP KCRETMECGL
110 120 130 140 150
GETLQRLQAA NDSICRLQQR EQERKKVIND YLTASEKRRL VQWEEFVSGQ
160 170 180
PQRRAEVDEE HRRAVERLRE QYAAMEKDLA KFSTF
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ8R015.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201605. 2 interactions.
STRINGi10090.ENSMUSP00000036614.

PTM databases

PhosphoSiteiQ8R015.

Proteomic databases

MaxQBiQ8R015.
PaxDbiQ8R015.
PRIDEiQ8R015.

Protocols and materials databases

DNASUi17828.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi63915.
MGIiMGI:2178598. Bloc1s5.

Phylogenomic databases

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

Miscellaneous databases

NextBioi292525.
PROiQ8R015.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R015.
CleanExiMM_MUTED.
GenevisibleiQ8R015. MM.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 89 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.