BL1S3_MOUSE
ID BL1S3_MOUSE Reviewed; 195 AA.
AC Q5U5M8; Q8C6R4; Q8R0Z3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 3;
DE Short=BLOC-1 subunit 3;
DE AltName: Full=Reduced pigmentation protein;
GN Name=Bloc1s3; Synonyms=Blos3, Rp;
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 / MRNA], INVOLVEMENT IN RP, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
RP BLOC1S4; BLOC1S5 AND BLOC1S6.
RX PubMed=15265785; DOI=10.1182/blood-2004-04-1538;
RA Gwynn B., Martina J.A., Bonifacino J.S., Sviderskaya E.V., Lamoreux M.L.,
RA Bennett D.C., Moriyama K., Huizing M., Helip-Wooley A., Gahl W.A.,
RA Webb L.S., Lambert A.J., Peters L.L.;
RT "Reduced pigmentation (rp), a mouse model of Hermansky-Pudlak syndrome,
RT encodes a novel component of the BLOC-1 complex.";
RL Blood 104:3181-3189(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Oviduct, and Thymus;
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 TISSUE=Kidney, and Mammary tumor;
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 IN THE BLOC-1 COMPLEX.
RX PubMed=17182842; DOI=10.1091/mbc.e06-12-1066;
RA Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V., Theos A.C.,
RA Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C.,
RA Dell'Angelica E.C., Raposo G., Marks M.S.;
RT "BLOC-1 is required for cargo-specific sorting from vacuolar early
RT endosomes toward lysosome-related organelles.";
RL Mol. Biol. Cell 18:768-780(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59 AND SER-61, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, 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. 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 Plays a role in intracellular vesicle trafficking.
CC {ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860,
CC ECO:0000269|PubMed:21998198}.
CC -!- SUBUNIT: Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3,
CC BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Interacts
CC directly with BLOC1S2 (By similarity). Component of the biogenesis of
CC lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1,
CC BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and
CC SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein
CC complex and membrane protein cargos. Interacts with BLOC1S4, BLOC1S5
CC and BLOC1S6. {ECO:0000250, ECO:0000269|PubMed:15102850,
CC ECO:0000269|PubMed:15265785, ECO:0000269|PubMed:17182842}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15265785}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:15265785}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15265785}.
CC -!- DISEASE: Note=Defects in Bloc1s3 are the cause of the reduced
CC pigmentation (rp) mutation phenotype, a mouse model for human
CC Hermansky-Pudlak syndrome (HPS). Rp mice are characterized by abnormal
CC melanosomes and display altered expression levels of the proteins of
CC the BLOC-1 complex. {ECO:0000269|PubMed:15265785}.
CC -!- SIMILARITY: Belongs to the BLOC1S3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY515509; AAS83987.1; -; Genomic_DNA.
DR EMBL; BK005392; DAA05717.1; -; mRNA.
DR EMBL; AK054006; BAC35618.1; -; mRNA.
DR EMBL; AK153811; BAE32192.1; -; mRNA.
DR EMBL; BC025913; AAH25913.1; -; mRNA.
DR EMBL; BC043666; AAH43666.1; -; mRNA.
DR CCDS; CCDS20904.1; -.
DR RefSeq; NP_808360.2; NM_177692.3.
DR RefSeq; XP_006539894.1; XM_006539831.3.
DR RefSeq; XP_006539895.1; XM_006539832.3.
DR AlphaFoldDB; Q5U5M8; -.
DR SMR; Q5U5M8; -.
DR BioGRID; 231329; 4.
DR ComplexPortal; CPX-1913; BLOC-1 complex.
DR CORUM; Q5U5M8; -.
DR STRING; 10090.ENSMUSP00000076624; -.
DR iPTMnet; Q5U5M8; -.
DR PhosphoSitePlus; Q5U5M8; -.
DR EPD; Q5U5M8; -.
DR jPOST; Q5U5M8; -.
DR MaxQB; Q5U5M8; -.
DR PaxDb; Q5U5M8; -.
DR PeptideAtlas; Q5U5M8; -.
DR PRIDE; Q5U5M8; -.
DR ProteomicsDB; 273745; -.
DR Antibodypedia; 59249; 79 antibodies from 15 providers.
DR DNASU; 232946; -.
DR Ensembl; ENSMUST00000077408; ENSMUSP00000076624; ENSMUSG00000057667.
DR GeneID; 232946; -.
DR KEGG; mmu:232946; -.
DR UCSC; uc009fma.1; mouse.
DR CTD; 388552; -.
DR MGI; MGI:2678952; Bloc1s3.
DR VEuPathDB; HostDB:ENSMUSG00000057667; -.
DR eggNOG; ENOG502RZCG; Eukaryota.
DR GeneTree; ENSGT00390000008756; -.
DR HOGENOM; CLU_116012_0_0_1; -.
DR InParanoid; Q5U5M8; -.
DR OMA; DIITSCN; -.
DR OrthoDB; 1289841at2759; -.
DR PhylomeDB; Q5U5M8; -.
DR TreeFam; TF336303; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 232946; 12 hits in 74 CRISPR screens.
DR ChiTaRS; Bloc1s3; mouse.
DR PRO; PR:Q5U5M8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q5U5M8; protein.
DR Bgee; ENSMUSG00000057667; Expressed in granulocyte and 224 other tissues.
DR Genevisible; Q5U5M8; MM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031083; C:BLOC-1 complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030133; C:transport vesicle; ISS:UniProtKB.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IMP:CACAO.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
DR GO; GO:0035646; P:endosome to melanosome transport; ISS:UniProtKB.
DR GO; GO:0001654; P:eye development; ISO:MGI.
DR GO; GO:0032438; P:melanosome organization; IMP:MGI.
DR GO; GO:0032402; P:melanosome transport; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; NAS:UniProtKB.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:0030168; P:platelet activation; ISO:MGI.
DR GO; GO:0060155; P:platelet dense granule organization; IMP:MGI.
DR GO; GO:0032816; P:positive regulation of natural killer cell activation; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0033299; P:secretion of lysosomal enzymes; IMP:MGI.
DR InterPro; IPR017245; BLOC-1_complex_su-3.
DR PANTHER; PTHR31974; PTHR31974; 1.
DR Pfam; PF15753; BLOC1S3; 1.
DR PIRSF; PIRSF037630; BLOC-1_complex_subunit_3; 1.
PE 1: Evidence at protein level;
KW Albinism; Cytoplasm; Hermansky-Pudlak syndrome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..195
FT /note="Biogenesis of lysosome-related organelles complex 1
FT subunit 3"
FT /id="PRO_0000234549"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 195 AA; 20398 MW; 869345D5418A2A0F CRC64;
MESSQGRRRR PGTVVPGEAA ETDSELSASS SEEELYLGPS GPTRGRPTGL RVAGEAAETD
SEPEPEPTVV PVDLPPLVVQ RDPAETWGTE ETPAMAPARS LLQLRLAESQ TRLDHDVAAA
VSGVYRRAGR DVAALAGRLA AAQATGLAAA HSVRLARGDL CALAERLDIV AGCRLLPDIR
GVPGMEPEQD PGPRA
