BL1S1_MOUSE
ID BL1S1_MOUSE Reviewed; 125 AA.
AC O55102; Q9DC96;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 1;
DE Short=BLOC-1 subunit 1;
DE AltName: Full=GCN5-like protein 1;
GN Name=Bloc1s1; Synonyms=Gcn5l1;
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 [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9426003; DOI=10.1016/s0378-1119(97)00486-1;
RA Driessen C.A.G.G., Winkens H.J., Kuhlmann L.D., Janssen B.P.M.,
RA van Vught A.H.M., Deutman A.F., Janssen J.J.M.;
RT "Cloning and structural analysis of the murine GCN5L1 gene.";
RL Gene 203:27-31(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, 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 [7]
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 [8]
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).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=22309213; DOI=10.1042/bj20120118;
RA Scott I., Webster B.R., Li J.H., Sack M.N.;
RT "Identification of a molecular component of the mitochondrial acetyl
RT transferase program; a novel role for GCN5L1.";
RL Biochem. J. 443:655-661(2012).
RN [10]
RP INTERACTION WITH KXD1.
RX PubMed=22554196; DOI=10.1111/j.1600-0854.2012.01375.x;
RA Yang Q., He X., Yang L., Zhou Z., Cullinane A.R., Wei A., Zhang Z., Hao Z.,
RA Zhang A., He M., Feng Y., Gao X., Gahl W.A., Huizing M., Li W.;
RT "The BLOS1-interacting protein KXD1 is involved in the biogenesis of
RT lysosome-related organelles.";
RL Traffic 13:1160-1169(2012).
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. In concert with the AP-3
CC complex, the BLOC-1 complex is required to target membrane protein
CC cargos into vesicles assembled at cell bodies for delivery into
CC neurites and nerve terminals. The BLOC-1 complex, in association with
CC SNARE proteins, is also proposed to be involved in neurite extension
CC (PubMed:16760431, PubMed:19546860, PubMed:21998198). As part of the
CC BORC complex may play a role in lysosomes movement and localization at
CC the cell periphery. The BORC complex is most probably associated with
CC the cytosolic face of lysosomes, may recruit ARL8B and couple lysosomes
CC to microtubule plus-end-directed kinesin motor (By similarity).
CC {ECO:0000250|UniProtKB:P78537, ECO:0000269|PubMed:16760431,
CC ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198}.
CC -!- FUNCTION: May negatively regulate aerobic respiration through
CC mitochondrial protein lysine-acetylation. May counteract the action of
CC the deacetylase SIRT3 by acetylating and regulating proteins of the
CC mitochondrial respiratory chain including ATP5F1A and NDUFA9.
CC {ECO:0000250|UniProtKB:P78537}.
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 (PubMed:15102850). The BLOC-1 complex
CC associates with the AP-3 protein complex and membrane protein cargos
CC (PubMed:21998198). Interacts with ATP5F1A and NDUFA9; involved in their
CC acetylation on lysine residues (By similarity). Interacts with KXD1
CC (PubMed:22554196). {ECO:0000250|UniProtKB:P78537,
CC ECO:0000269|PubMed:15102850, ECO:0000269|PubMed:21998198,
CC ECO:0000269|PubMed:22554196}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22309213}. Mitochondrion matrix
CC {ECO:0000269|PubMed:22309213}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P78537}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P78537}.
CC -!- SIMILARITY: Belongs to the BLOC1S1 family. {ECO:0000305}.
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DR EMBL; Y13778; CAA74108.1; -; Genomic_DNA.
DR EMBL; Y13779; CAA74108.1; JOINED; Genomic_DNA.
DR EMBL; Y13780; CAA74108.1; JOINED; Genomic_DNA.
DR EMBL; Y13781; CAA74108.1; JOINED; Genomic_DNA.
DR EMBL; AK003035; BAB22523.1; -; mRNA.
DR EMBL; BC034662; AAH34662.1; -; mRNA.
DR CCDS; CCDS24299.1; -.
DR PIR; JC6514; JC6514.
DR RefSeq; NP_056555.2; NM_015740.3.
DR RefSeq; XP_006513292.1; XM_006513229.3.
DR AlphaFoldDB; O55102; -.
DR SMR; O55102; -.
DR ComplexPortal; CPX-1913; BLOC-1 complex.
DR ComplexPortal; CPX-5061; BORC complex.
DR CORUM; O55102; -.
DR STRING; 10090.ENSMUSP00000026405; -.
DR iPTMnet; O55102; -.
DR PhosphoSitePlus; O55102; -.
DR EPD; O55102; -.
DR MaxQB; O55102; -.
DR PaxDb; O55102; -.
DR PRIDE; O55102; -.
DR ProteomicsDB; 273786; -.
DR DNASU; 14533; -.
DR Ensembl; ENSMUST00000026405; ENSMUSP00000026405; ENSMUSG00000090247.
DR GeneID; 14533; -.
DR KEGG; mmu:14533; -.
DR UCSC; uc007hoz.1; mouse.
DR CTD; 2647; -.
DR MGI; MGI:1195276; Bloc1s1.
DR VEuPathDB; HostDB:ENSMUSG00000090247; -.
DR eggNOG; KOG3390; Eukaryota.
DR GeneTree; ENSGT00390000002689; -.
DR HOGENOM; CLU_115602_3_0_1; -.
DR InParanoid; O55102; -.
DR OMA; HSATNFA; -.
DR OrthoDB; 1603359at2759; -.
DR PhylomeDB; O55102; -.
DR TreeFam; TF314443; -.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 14533; 10 hits in 74 CRISPR screens.
DR ChiTaRS; Bloc1s1; mouse.
DR PRO; PR:O55102; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O55102; protein.
DR Bgee; ENSMUSG00000090247; Expressed in white adipose tissue and 63 other tissues.
DR ExpressionAtlas; O55102; baseline and differential.
DR Genevisible; O55102; 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:0098574; C:cytoplasmic side of lysosomal membrane; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:CACAO.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0009060; P:aerobic respiration; ISS:UniProtKB.
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:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0032438; P:melanosome organization; IC:ComplexPortal.
DR GO; GO:0031175; P:neuron projection development; NAS:UniProtKB.
DR GO; GO:0072384; P:organelle transport along microtubule; IC:ComplexPortal.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; ISS:UniProtKB.
DR GO; GO:0051036; P:regulation of endosome size; IC:ComplexPortal.
DR GO; GO:0062196; P:regulation of lysosome size; IC:ComplexPortal.
DR InterPro; IPR009395; BLOC1S1.
DR PANTHER; PTHR13073; PTHR13073; 1.
DR Pfam; PF06320; GCN5L1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Lysosome; Membrane; Mitochondrion;
KW Reference proteome.
FT CHAIN 1..125
FT /note="Biogenesis of lysosome-related organelles complex 1
FT subunit 1"
FT /id="PRO_0000156332"
FT COILED 1..31
FT /evidence="ECO:0000255"
FT CONFLICT 26
FT /note="E -> Y (in Ref. 1; CAA74108)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="T -> I (in Ref. 1; CAA74108)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="D -> V (in Ref. 1; CAA74108)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 125 AA; 14281 MW; 754897B17BC9479D CRC64;
MLSRLLKEHQ AKQNERKELQ EKRRREAIAA ATCLTEALVD HLNVGVAQAY MNQRKLDHEV
KTLQVQAAQF AKQTGQWIGM VENFNQALKE IGDVENWARS IELDMRTIAT ALEYVYKGQL
QSAPS
