Q9CWG9 (BL1S2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Biogenesis of lysosome-related organelles complex 1 subunit 2
Short name=BLOC-1 subunit 2

Gene names

Name:	Bloc1s2
Synonyms:	Blos2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	143 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Plays a role in intracellular vesicle trafficking. May play a role in cell proliferation. Ref.5 Ref.7 Ref.8
Subunit structure	Interacts with gamma-tubulin. Interacts directly with BLOC1S1, BLOC1S3, BLOC1S4, BLOC1S5 and SNAPIN. 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 IFT57. Ref.4 Ref.6
Subcellular location	Cytoplasm › cytoskeleton › centrosome By similarity. Note: Localizes to the centrosomes in a microtubule-dependent manner By similarity.
Sequence similarities	Belongs to the BLOC1S2 family.
Sequence caution	The sequence AAH65806.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Domain	Coiled coil
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anterograde axon cargo transport Inferred from mutant phenotype Ref.8. Source: UniProtKB anterograde synaptic vesicle transport Inferred from mutant phenotype Ref.8. Source: UniProtKB neuron projection development Non-traceable author statement Ref.7. Source: UniProtKB
Cellular_component	BLOC-1 complex Inferred from sequence or structural similarity. Source: UniProtKB microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 143	143	Biogenesis of lysosome-related organelles complex 1 subunit 2		PRO_0000234545
Regions
	Coiled coil	80 – 128	49	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9CWG9 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 4E1ED89D9F1E7A4C	FASTA	143	16,300
	10 20 30 40 50 60 MAAAAEGVPA TRREEQPPRD DAAVETAEEA KEPAEADINE LCRDMFSKMA TYLTGELTAT 70 80 90 100 110 120 SEDYKLLENM NKLTSLKYLE MKDIAINISR NLKDLNQKYA ELQPYLDQIN MIEEQVAALE 130 140 QAAYKLDAYS KKLEAKYKKL EKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Strain: C57BL/6J.
[2]	"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. , 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.
[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: Mammary gland.
[4]	"Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1)." Starcevic M., Dell'Angelica E.C. J. Biol. Chem. 279:28393-28401(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE BLOC-1 COMPLEX.
[5]	"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.
[6]	"BLOC1S2 interacts with the HIPPI protein and sensitizes NCH89 glioblastoma cells to apoptosis." Gdynia G., Lehmann-Koch J., Sieber S., Tagscherer K.E., Fassl A., Zentgraf H., Matsuzawa S., Reed J.C., Roth W. Apoptosis 13:437-447(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IFT57.
[7]	"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.
[8]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK010745 mRNA. Translation: BAB27155.1. AL928960 Genomic DNA. Translation: CAM23662.1. BC065806 mRNA. Translation: AAH65806.1. Different initiation.
IPI	IPI00109103.
RefSeq	NP_082883.1. NM_028607.1.
UniGene	Mm.124685.
3D structure databases
ProteinModelPortal	Q9CWG9.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000078042.
Proteomic databases
PaxDb	Q9CWG9.
PRIDE	Q9CWG9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026219; ENSMUSP00000026219; ENSMUSG00000025201. ENSMUST00000079033; ENSMUSP00000078042; ENSMUSG00000057506.
GeneID	73689.
KEGG	mmu:73689.
UCSC	uc008hpl.2. mouse.
Organism-specific databases
CTD	73689.
MGI	MGI:1920939. Bloc1s2.
Phylogenomic databases
eggNOG	NOG251755.
GeneTree	ENSGT00390000005889.
HOGENOM	HOG000111279.
HOVERGEN	HBG079627.
InParanoid	A2ATZ7.
KO	K16750.
OMA	IALENRV.
OrthoDB	EOG43210M.
Gene expression databases
Bgee	Q9CWG9.
Genevestigator	Q9CWG9.
GermOnline	ENSMUSG00000025201. Mus musculus. ENSMUSG00000057506. Mus musculus.
Family and domain databases
InterPro	IPR019269. BLOC1_su2. [Graphical view]
Pfam	PF10046. BLOC1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	338807.
SOURCE	Search...

Entry information

Entry name

BL1S2_MOUSE

Accession

Primary (citable) accession number: Q9CWG9
Secondary accession number(s): A2ATZ7, Q6P062

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program