BL1S2_MOUSE
ID BL1S2_MOUSE Reviewed; 143 AA.
AC Q9CWG9; A2ATZ7; Q6P062;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 2;
DE Short=BLOC-1 subunit 2;
GN Name=Bloc1s2; Synonyms=Blos2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 IDENTIFICATION IN THE BLOC-1 COMPLEX.
RX PubMed=15102850; DOI=10.1074/jbc.m402513200;
RA Starcevic M., Dell'Angelica E.C.;
RT "Identification of snapin and three novel proteins (BLOS1, BLOS2, and
RT BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related
RT organelles complex-1 (BLOC-1).";
RL J. Biol. Chem. 279:28393-28401(2004).
RN [5]
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 [6]
RP INTERACTION WITH IFT57.
RX PubMed=18188704; DOI=10.1007/s10495-007-0176-3;
RA Gdynia G., Lehmann-Koch J., Sieber S., Tagscherer K.E., Fassl A.,
RA Zentgraf H., Matsuzawa S., Reed J.C., Roth W.;
RT "BLOC1S2 interacts with the HIPPI protein and sensitizes NCH89 glioblastoma
RT cells to apoptosis.";
RL Apoptosis 13:437-447(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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 [8]
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 [9]
RP FUNCTION, AND ASSOCIATION WITH THE AP-3 COMPLEX.
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 (By similarity). In concert
CC with the AP-3 complex, the BLOC-1 complex is required to target
CC membrane protein cargos into vesicles assembled at cell bodies for
CC delivery into neurites and nerve terminals (PubMed:16760431,
CC PubMed:21998198). The BLOC-1 complex, in association with SNARE
CC proteins, is also proposed to be involved in neurite extension
CC (PubMed:19546860). As part of the BORC complex may play a role in
CC lysosomes movement and localization at the cell periphery. Associated
CC with the cytosolic face of lysosomes, the BORC complex may recruit
CC ARL8B and couple lysosomes to microtubule plus-end-directed kinesin
CC motor (By similarity). {ECO:0000250|UniProtKB:Q6QNY1,
CC ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860,
CC ECO:0000269|PubMed:21998198}.
CC -!- SUBUNIT: 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. Octamer composed
CC of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6,
CC DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Interacts directly with BLOC1S1,
CC BLOC1S3, BLOC1S4, BLOC1S5 and SNAPIN (PubMed:15102850). The BLOC-1
CC complex associates with the AP-3 protein complex and membrane protein
CC cargos (PubMed:21998198). Component of the BLOC-one-related complex
CC (BORC) which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7,
CC BORCS8, KXD1 and SNAPIN (By similarity). Interacts with gamma-tubulin
CC (By similarity). Interacts with IFT57 (PubMed:18188704).
CC {ECO:0000250|UniProtKB:Q6QNY1, ECO:0000269|PubMed:15102850,
CC ECO:0000269|PubMed:18188704, ECO:0000269|PubMed:21998198}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q6QNY1}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q6QNY1}. Note=Localizes to the centrosomes in a
CC microtubule-dependent manner. {ECO:0000250|UniProtKB:Q6QNY1}.
CC -!- SIMILARITY: Belongs to the BLOC1S2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH65806.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK010745; BAB27155.1; -; mRNA.
DR EMBL; AL928960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065806; AAH65806.1; ALT_INIT; mRNA.
DR CCDS; CCDS50445.1; -.
DR RefSeq; NP_082883.1; NM_028607.1.
DR AlphaFoldDB; Q9CWG9; -.
DR SMR; Q9CWG9; -.
DR BioGRID; 216191; 3.
DR ComplexPortal; CPX-1913; BLOC-1 complex.
DR ComplexPortal; CPX-5061; BORC complex.
DR CORUM; Q9CWG9; -.
DR STRING; 10090.ENSMUSP00000078042; -.
DR iPTMnet; Q9CWG9; -.
DR PhosphoSitePlus; Q9CWG9; -.
DR EPD; Q9CWG9; -.
DR MaxQB; Q9CWG9; -.
DR PaxDb; Q9CWG9; -.
DR PeptideAtlas; Q9CWG9; -.
DR PRIDE; Q9CWG9; -.
DR ProteomicsDB; 273787; -.
DR Antibodypedia; 55739; 109 antibodies from 21 providers.
DR Ensembl; ENSMUST00000079033; ENSMUSP00000078042; ENSMUSG00000057506.
DR GeneID; 73689; -.
DR KEGG; mmu:73689; -.
DR UCSC; uc008hpl.2; mouse.
DR CTD; 282991; -.
DR MGI; MGI:1920939; Bloc1s2.
DR VEuPathDB; HostDB:ENSMUSG00000057506; -.
DR eggNOG; KOG4559; Eukaryota.
DR GeneTree; ENSGT00390000005889; -.
DR HOGENOM; CLU_110820_0_1_1; -.
DR InParanoid; Q9CWG9; -.
DR OMA; CSDMFEK; -.
DR OrthoDB; 1505524at2759; -.
DR PhylomeDB; Q9CWG9; -.
DR TreeFam; TF313861; -.
DR BioGRID-ORCS; 73689; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Bloc1s2; mouse.
DR PRO; PR:Q9CWG9; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9CWG9; protein.
DR Bgee; ENSMUSG00000057506; Expressed in embryonic brain and 62 other tissues.
DR ExpressionAtlas; Q9CWG9; baseline and differential.
DR Genevisible; Q9CWG9; MM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031083; C:BLOC-1 complex; IDA:MGI.
DR GO; GO:0099078; C:BORC complex; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0000930; C:gamma-tubulin complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043015; F:gamma-tubulin binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0032438; P:melanosome organization; IC:ComplexPortal.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; NAS:UniProtKB.
DR GO; GO:0072384; P:organelle transport along microtubule; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051036; P:regulation of endosome size; IC:ComplexPortal.
DR GO; GO:0062196; P:regulation of lysosome size; IC:ComplexPortal.
DR InterPro; IPR019269; BLOC1_su2.
DR PANTHER; PTHR46479; PTHR46479; 1.
DR Pfam; PF10046; BLOC1_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Lysosome; Membrane;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6QNY1"
FT CHAIN 2..143
FT /note="Biogenesis of lysosome-related organelles complex 1
FT subunit 2"
FT /id="PRO_0000234545"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 80..128
FT /evidence="ECO:0000255"
FT COMPBIAS 12..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6QNY1"
SQ SEQUENCE 143 AA; 16300 MW; 4E1ED89D9F1E7A4C CRC64;
MAAAAEGVPA TRREEQPPRD DAAVETAEEA KEPAEADINE LCRDMFSKMA TYLTGELTAT
SEDYKLLENM NKLTSLKYLE MKDIAINISR NLKDLNQKYA ELQPYLDQIN MIEEQVAALE
QAAYKLDAYS KKLEAKYKKL EKR
