BL1S3_HUMAN
ID BL1S3_HUMAN Reviewed; 202 AA.
AC Q6QNY0; B2RXB8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 3;
DE Short=BLOC-1 subunit 3;
GN Name=BLOC1S3; Synonyms=BLOS3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE BLOC-1 COMPLEX, AND
RP INTERACTION WITH BLOC1S2.
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
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 FUNCTION, AND INVOLVEMENT IN HPS8.
RX PubMed=16385460; DOI=10.1086/499338;
RA Morgan N.V., Pasha S., Johnson C.A., Ainsworth J.R., Eady R.A.J.,
RA Dawood B., McKeown C., Trembath R.C., Wilde J., Watson S.P., Maher E.R.;
RT "A germline mutation in BLOC1S3/reduced pigmentation causes a novel variant
RT of Hermansky-Pudlak syndrome (HPS8).";
RL Am. J. Hum. Genet. 78:160-166(2006).
RN [5]
RP FUNCTION.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 AND SER-65, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 AND SER-65, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 AND SER-65, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION IN THE BLOC-1 COMPLEX, AND COMPOSITION OF THE BLOC-1
RP COMPLEX.
RX PubMed=22203680; DOI=10.1074/jbc.m111.325746;
RA Lee H.H., Nemecek D., Schindler C., Smith W.J., Ghirlando R., Steven A.C.,
RA Bonifacino J.S., Hurley J.H.;
RT "Assembly and architecture of biogenesis of lysosome-related organelles
RT complex-1 (BLOC-1).";
RL J. Biol. Chem. 287:5882-5890(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 AND SER-65, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 AND SER-65, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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:16385460, ECO:0000269|PubMed:17182842}.
CC -!- SUBUNIT: Interacts with BLOC1S4, BLOC1S5 and BLOC1S6 (By similarity).
CC Component of the biogenesis of lysosome-related organelles complex 1
CC (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5,
CC BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one
CC copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6,
CC DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with
CC the AP-3 protein complex and membrane protein cargos. Interacts
CC directly with BLOC1S2. {ECO:0000250, ECO:0000269|PubMed:15102850,
CC ECO:0000269|PubMed:22203680}.
CC -!- INTERACTION:
CC Q6QNY0; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-465930, EBI-465872;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISEASE: Hermansky-Pudlak syndrome 8 (HPS8) [MIM:614077]: A form of
CC Hermansky-Pudlak syndrome, a genetically heterogeneous autosomal
CC recessive disorder characterized by oculocutaneous albinism, bleeding
CC due to platelet storage pool deficiency, and lysosomal storage defects.
CC This syndrome results from defects of diverse cytoplasmic organelles
CC including melanosomes, platelet dense granules and lysosomes. Ceroid
CC storage in the lungs is associated with pulmonary fibrosis, a common
CC cause of premature death in individuals with HPS.
CC {ECO:0000269|PubMed:16385460}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the BLOC1S3 family. {ECO:0000305}.
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DR EMBL; AY531266; AAT00462.1; -; mRNA.
DR EMBL; AK296695; BAG59289.1; -; mRNA.
DR EMBL; BC151151; AAI51152.1; -; mRNA.
DR EMBL; BC151152; AAI51153.1; -; mRNA.
DR CCDS; CCDS12656.1; -.
DR RefSeq; NP_997715.1; NM_212550.4.
DR AlphaFoldDB; Q6QNY0; -.
DR SMR; Q6QNY0; -.
DR BioGRID; 132736; 15.
DR ComplexPortal; CPX-1910; BLOC-1 complex.
DR CORUM; Q6QNY0; -.
DR IntAct; Q6QNY0; 10.
DR STRING; 9606.ENSP00000393840; -.
DR GlyGen; Q6QNY0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6QNY0; -.
DR PhosphoSitePlus; Q6QNY0; -.
DR BioMuta; BLOC1S3; -.
DR DMDM; 74749299; -.
DR EPD; Q6QNY0; -.
DR jPOST; Q6QNY0; -.
DR MassIVE; Q6QNY0; -.
DR MaxQB; Q6QNY0; -.
DR PaxDb; Q6QNY0; -.
DR PeptideAtlas; Q6QNY0; -.
DR PRIDE; Q6QNY0; -.
DR ProteomicsDB; 67306; -.
DR Antibodypedia; 59249; 79 antibodies from 15 providers.
DR DNASU; 388552; -.
DR Ensembl; ENST00000433642.3; ENSP00000393840.1; ENSG00000189114.8.
DR Ensembl; ENST00000587722.1; ENSP00000468281.1; ENSG00000189114.8.
DR GeneID; 388552; -.
DR KEGG; hsa:388552; -.
DR MANE-Select; ENST00000433642.3; ENSP00000393840.1; NM_212550.5; NP_997715.1.
DR UCSC; uc002pax.5; human.
DR CTD; 388552; -.
DR DisGeNET; 388552; -.
DR GeneCards; BLOC1S3; -.
DR GeneReviews; BLOC1S3; -.
DR HGNC; HGNC:20914; BLOC1S3.
DR HPA; ENSG00000189114; Low tissue specificity.
DR MalaCards; BLOC1S3; -.
DR MIM; 609762; gene.
DR MIM; 614077; phenotype.
DR neXtProt; NX_Q6QNY0; -.
DR OpenTargets; ENSG00000189114; -.
DR Orphanet; 231531; Hermansky-Pudlak syndrome due to BLOC-1 deficiency.
DR PharmGKB; PA134884924; -.
DR VEuPathDB; HostDB:ENSG00000189114; -.
DR eggNOG; ENOG502RZCG; Eukaryota.
DR GeneTree; ENSGT00390000008756; -.
DR HOGENOM; CLU_116012_0_0_1; -.
DR InParanoid; Q6QNY0; -.
DR OMA; DIITSCN; -.
DR OrthoDB; 1289841at2759; -.
DR PhylomeDB; Q6QNY0; -.
DR TreeFam; TF336303; -.
DR PathwayCommons; Q6QNY0; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; Q6QNY0; -.
DR SIGNOR; Q6QNY0; -.
DR BioGRID-ORCS; 388552; 16 hits in 1077 CRISPR screens.
DR GenomeRNAi; 388552; -.
DR Pharos; Q6QNY0; Tbio.
DR PRO; PR:Q6QNY0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6QNY0; protein.
DR Bgee; ENSG00000189114; Expressed in oocyte and 157 other tissues.
DR ExpressionAtlas; Q6QNY0; baseline and differential.
DR Genevisible; Q6QNY0; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031083; C:BLOC-1 complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0035646; P:endosome to melanosome transport; IDA:UniProtKB.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR GO; GO:0032438; P:melanosome organization; NAS:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; IDA:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0043473; P:pigmentation; IMP:UniProtKB.
DR GO; GO:0030168; P:platelet activation; IMP:UniProtKB.
DR GO; GO:0060155; P:platelet dense granule organization; NAS:UniProtKB.
DR GO; GO:0032816; P:positive regulation of natural killer cell activation; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0033299; P:secretion of lysosomal enzymes; IEA:Ensembl.
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..202
FT /note="Biogenesis of lysosome-related organelles complex 1
FT subunit 3"
FT /id="PRO_0000234548"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 63
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
SQ SEQUENCE 202 AA; 21256 MW; EB072B856AB6B4CF CRC64;
MASQGRRRRP LRRPETVVPG EATETDSERS ASSSEEEELY LGPSGPTRGR PTGLRVAGEA
AETDSEPEPE PEPTAAPRDL PPLVVQRESA EEAWGTEEAP APAPARSLLQ LRLAESQARL
DHDVAAAVSG VYRRAGRDVA ALASRLAAAQ AAGLAAAHSV RLARGDLCAL AERLDIVAGC
RLLPDIRGVP GTEPEKDPGP RA
