Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9R0C0 (BL1S6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biogenesis of lysosome-related organelles complex 1 subunit 6

Short name=BLOC-1 subunit 6
Alternative name(s):
Pallid protein
Pallidin
Syntaxin 13-interacting protein
Gene names
Name:Bloc1s6
Synonyms:P2, Pa, Pldn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. May play a role in intracellular vesicle trafficking, particularly in the vesicle-docking and fusion process. Ref.10 Ref.11 Ref.12 Ref.13

Subunit structure

Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Interacts with SNAP47 By similarity. Homodimer. 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. Interacts with BLOC1S4, BLOC1S5, DTNBP1/BLOC1S7, F-actin, SNAP25 isoform 1 and STX12. Ref.1 Ref.6 Ref.8 Ref.9 Ref.11 Ref.12

Subcellular location

Cytoplasm. Endomembrane system; Peripheral membrane protein. Note: It can exist as a soluble protein as well as a peripheral membrane protein. Ref.6

Tissue specificity

Expressed in liver, kidney and spleen (at protein level). Ubiquitously expressed, with the highest expression levels observed in brain, heart, liver and kidney. Ref.1 Ref.6 Ref.7

Post-translational modification

Phosphorylated By similarity.

Involvement in disease

Defects in Pldn are the cause of the pallid (pa) phenotype that is characterized by an altered formation or function of intracellular storage granules in melanocytes, platelets, and lysosomes in kidney. Pallid mice have a prolonged bleeding time owing to the inability of immature platelet dense granules to accumulate normal amounts of ATP, ADP, and serotonin. Pa animals also suffer from pigment dilution, kidney lysosomal enzyme elevation and serum alpha1-antitrypsin activity deficiency. Finally, pallid mice exhibit defects in otolith formation that lead to balance abnormalities. Ref.1

Sequence similarities

Belongs to the BLOC1S6 family.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterograde axon cargo transport

Inferred from mutant phenotype Ref.13. Source: UniProtKB

anterograde synaptic vesicle transport

Inferred from mutant phenotype Ref.13. Source: UniProtKB

blood coagulation

Inferred from mutant phenotype PubMed 6696991. Source: MGI

endosome to melanosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

melanocyte differentiation

Inferred from mutant phenotype PubMed 2379821. Source: MGI

melanosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

membrane fusion

Inferred from physical interaction Ref.1. Source: MGI

neuron projection development

Inferred from mutant phenotype Ref.12. Source: UniProtKB

pigmentation

Inferred from mutant phenotype PubMed 2379821PubMed 7089489. Source: MGI

positive regulation of natural killer cell activation

Inferred from mutant phenotype PubMed 7089489. Source: MGI

positive regulation of pigment cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

secretion of lysosomal enzymes

Inferred from mutant phenotype PubMed 7089489. Source: MGI

vesicle docking involved in exocytosis

Traceable author statement Ref.1. Source: MGI

vesicle fusion

Traceable author statement Ref.1. Source: MGI

   Cellular_componentBLOC-1 complex

Inferred from direct assay Ref.8Ref.11Ref.12. Source: UniProtKB

SNARE complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

endosome

Inferred from direct assay Ref.1. Source: MGI

extrinsic component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

transport vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionactin filament binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9R0C0-1)

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.
Isoform 2 (identifier: Q9R0C0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     76-80: QNQVV → TKLCY
     81-172: Missing.
Note: May be due to a competing acceptor splice site.
Isoform 3 (identifier: Q9R0C0-3)

The sequence of this isoform is not available.
Note: May be due to exon 2 skipping.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 172172Biogenesis of lysosome-related organelles complex 1 subunit 6
PRO_0000058459

Regions

Coiled coil63 – 167105 Potential

Natural variations

Alternative sequence76 – 805QNQVV → TKLCY in isoform 2.
VSP_009295
Alternative sequence81 – 17292Missing in isoform 2.
VSP_009296
Natural variant141T → M in strain: C57BL/6J-pa mutants. Ref.1
Natural variant321T → M in strain: BALB/c, CBA and C57BL/6J-pa mutants. Ref.1 Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6B8068DF091B07D2

FASTA17219,682
        10         20         30         40         50         60 
MSVPEPPPPD GVLTGPSDSL EAGEPTPGLS DTSPDEGLIE DFPVDDRAVE HLVGGLLSHY 

        70         80         90        100        110        120 
LPDLQRSKRA LQELTQNQVV LLDTLEQEIS KFKECHSMLD INALFTEAKH YHAKLVTIRK 

       130        140        150        160        170 
EMLLLHEKTS KLKKRALKLQ QKRQREELER EQQREKEFER EKQLTAKPAK RT 

« Hide

Isoform 2 [UniParc].

Checksum: 7CF7F688AEE5DBE5
Show »

FASTA808,569
Isoform 3 (Sequence not available).

References

« Hide 'large scale' references
[1]"The pallid gene encodes a novel, syntaxin 13-interacting protein involved in platelet storage pool deficiency."
Huang L., Kuo Y.-M., Gitschier J.
Nat. Genet. 23:329-332(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH STX12, ALTERNATIVE SPLICING, DISEASE, VARIANTS MET-14 AND MET-32.
Strain: C57BL/6J.
Tissue: Brain.
[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. expand/collapse author list , 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] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Heart and Hypothalamus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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] (ISOFORM 2), VARIANT MET-32.
Tissue: Mammary tumor.
[5]"The pallidin (Pldn) gene and the role of SNARE proteins in melanosome biogenesis."
Falcon-Perez J.M., Dell'Angelica E.C.
Pigment Cell Res. 15:82-86(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, ALTERNATIVE SPLICING.
[6]"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: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH F-ACTIN, HOMODIMERIZATION.
[7]"Pallidin is a component of a multi-protein complex involved in the biogenesis of lysosome-related organelles."
Moriyama K., Bonifacino J.S.
Traffic 3:666-677(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"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 BLOC1S5.
[9]"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.
[10]"BLOC-1 complex deficiency alters the targeting of adaptor protein complex-3 cargoes."
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.
Mol. Biol. Cell 17:4014-4026(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"BLOC-1 is required for cargo-specific sorting from vacuolar early endosomes toward lysosome-related organelles."
Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V., Theos A.C., Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C., Dell'Angelica E.C., Raposo G., Marks M.S.
Mol. Biol. Cell 18:768-780(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BLOC-1 COMPLEX, FUNCTION.
[12]"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: IDENTIFICATION IN THE BLOC-1 COMPLEX, FUNCTION, INTERACTION WITH SNAP25.
[13]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF079530 mRNA. Translation: AAF09262.1.
AF082574 expand/collapse EMBL AC list , AF082571, AF082572, AF082573 Genomic DNA. Translation: AAF42469.1.
AK038381 mRNA. Translation: BAC29977.1.
AK077720 mRNA. Translation: BAC36979.1.
AK147116 mRNA. Translation: BAE27688.1.
AK160580 mRNA. Translation: BAE35887.1.
AL928950 Genomic DNA. Translation: CAM26697.1.
BC016554 mRNA. Translation: AAH16554.1.
RefSeqNP_062762.1. NM_019788.3.
UniGeneMm.268921.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202009. 2 interactions.
IntActQ9R0C0. 2 interactions.
MINTMINT-4107741.

PTM databases

PhosphoSiteQ9R0C0.

Proteomic databases

PaxDbQ9R0C0.
PRIDEQ9R0C0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005954; ENSMUSP00000005954; ENSMUSG00000005804. [Q9R0C0-1]
GeneID18457.
KEGGmmu:18457.
UCSCuc008mbf.1. mouse. [Q9R0C0-1]

Organism-specific databases

CTD26258.
MGIMGI:1927580. Bloc1s6.

Phylogenomic databases

eggNOGNOG87432.
GeneTreeENSGT00510000047812.
HOGENOMHOG000231944.
HOVERGENHBG049426.
InParanoidA2ATW6.
OMAMLHEKTT.
OrthoDBEOG74TX2D.
PhylomeDBQ9R0C0.
TreeFamTF325188.

Gene expression databases

BgeeQ9R0C0.
CleanExMM_PLDN.
GenevestigatorQ9R0C0.

Family and domain databases

InterProIPR017242. BLOC-1_pallidin.
IPR028119. Snapin/Pallidin/Snn1.
[Graphical view]
PANTHERPTHR31328. PTHR31328. 1 hit.
PfamPF14712. Snapin_Pallidin. 1 hit.
[Graphical view]
PIRSFPIRSF037609. BLOC-1_complex_pallidin. 1 hit.
ProtoNetSearch...

Other

NextBio294148.
PROQ9R0C0.
SOURCESearch...

Entry information

Entry nameBL1S6_MOUSE
AccessionPrimary (citable) accession number: Q9R0C0
Secondary accession number(s): A2ATW6, Q3TUT4, Q91VG4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot