ID BL1S6_MOUSE Reviewed; 172 AA. AC Q9R0C0; A2ATW6; Q3TUT4; Q91VG4; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 161. DE RecName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 6; DE Short=BLOC-1 subunit 6; DE AltName: Full=Pallid protein; DE AltName: Full=Pallidin; DE AltName: Full=Syntaxin 13-interacting protein; GN Name=Bloc1s6; Synonyms=P2, Pa, Pldn; 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] (ISOFORM 1), TISSUE SPECIFICITY, RP INTERACTION WITH STX12, ALTERNATIVE SPLICING, DISEASE, AND VARIANTS MET-14 RP AND MET-32. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=10610180; DOI=10.1038/15507; RA Huang L., Kuo Y.-M., Gitschier J.; RT "The pallid gene encodes a novel, syntaxin 13-interacting protein involved RT in platelet storage pool deficiency."; RL Nat. Genet. 23:329-332(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Heart, and Hypothalamus; 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 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-32. RC TISSUE=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 [5] RP REVIEW, AND ALTERNATIVE SPLICING. RX PubMed=11936273; DOI=10.1034/j.1600-0749.2002.1r082.x; RA Falcon-Perez J.M., Dell'Angelica E.C.; RT "The pallidin (Pldn) gene and the role of SNARE proteins in melanosome RT biogenesis."; RL Pigment Cell Res. 15:82-86(2002). RN [6] RP TISSUE SPECIFICITY, INTERACTION WITH F-ACTIN, AND HOMODIMERIZATION. RX PubMed=12019270; DOI=10.1074/jbc.m204011200; RA Falcon-Perez J.M., Starcevic M., Gautam R., Dell'Angelica E.C.; RT "BLOC-1, a novel complex containing the pallidin and muted proteins RT involved in the biogenesis of melanosomes and platelet-dense granules."; RL J. Biol. Chem. 277:28191-28199(2002). RN [7] RP TISSUE SPECIFICITY. RX PubMed=12191018; DOI=10.1034/j.1600-0854.2002.30908.x; RA Moriyama K., Bonifacino J.S.; RT "Pallidin is a component of a multi-protein complex involved in the RT biogenesis of lysosome-related organelles."; RL Traffic 3:666-677(2002). RN [8] RP IDENTIFICATION IN THE BLOC-1 COMPLEX, AND INTERACTION WITH BLOC1S4 AND RP BLOC1S5. RX PubMed=12576321; DOI=10.1182/blood-2003-01-0020; RA Ciciotte S.L., Gwynn B., Moriyama K., Huizing M., Gahl W.A., RA Bonifacino J.S., Peters L.L.; RT "Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a novel RT protein that is part of the pallidin-muted complex (BLOC-1)."; RL Blood 101:4402-4407(2003). RN [9] RP INTERACTION WITH DTNBP1. RX PubMed=12923531; DOI=10.1038/ng1229; RA Li W., Zhang Q., Oiso N., Novak E.K., Gautam R., O'Brien E.P., RA Tinsley C.L., Blake D.J., Spritz R.A., Copeland N.G., Jenkins N.A., RA Amato D., Roe B.A., Starcevic M., Dell'Angelica E.C., Elliott R.W., RA Mishra V., Kingsmore S.F., Paylor R.E., Swank R.T.; RT "Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a RT member of the biogenesis of lysosome-related organelles complex 1 (BLOC- RT 1)."; RL Nat. Genet. 35:84-89(2003). RN [10] 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 [11] RP IDENTIFICATION IN THE BLOC-1 COMPLEX, AND 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Pancreas, Spleen, RC 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 [13] RP IDENTIFICATION IN THE BLOC-1 COMPLEX, FUNCTION, AND INTERACTION WITH RP SNAP25. 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 [14] RP FUNCTION. 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 May play a role in intracellular vesicle trafficking, particularly in CC the vesicle-docking and fusion process. {ECO:0000269|PubMed:16760431, CC ECO:0000269|PubMed:17182842, 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 with SNAP47 (By similarity). Homodimer. 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. Interacts with BLOC1S4, BLOC1S5, DTNBP1/BLOC1S7, F- CC actin, SNAP25 isoform 1 and STX12. {ECO:0000250, CC ECO:0000269|PubMed:10610180, ECO:0000269|PubMed:12019270, CC ECO:0000269|PubMed:12576321, ECO:0000269|PubMed:12923531, CC ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:19546860}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UL45}. CC Membrane {ECO:0000250|UniProtKB:Q9UL45}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q9UL45}. Note=It can exist as a soluble protein CC as well as a peripheral membrane protein. CC {ECO:0000250|UniProtKB:Q9UL45}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9R0C0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9R0C0-2; Sequence=VSP_009295, VSP_009296; CC Name=3; CC IsoId=Q9R0C0-3; Sequence=Not described; CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney and spleen (at protein CC level). Ubiquitously expressed, with the highest expression levels CC observed in brain, heart, liver and kidney. CC {ECO:0000269|PubMed:10610180, ECO:0000269|PubMed:12019270, CC ECO:0000269|PubMed:12191018}. CC -!- PTM: Phosphorylated. {ECO:0000250}. CC -!- DISEASE: Note=Defects in Pldn are the cause of the pallid (pa) CC phenotype that is characterized by an altered formation or function of CC intracellular storage granules in melanocytes, platelets, and lysosomes CC in kidney. Pallid mice have a prolonged bleeding time owing to the CC inability of immature platelet dense granules to accumulate normal CC amounts of ATP, ADP, and serotonin. Pa animals also suffer from pigment CC dilution, kidney lysosomal enzyme elevation and serum alpha1- CC antitrypsin activity deficiency. Finally, pallid mice exhibit defects CC in otolith formation that lead to balance abnormalities. CC {ECO:0000269|PubMed:10610180}. CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice CC site. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: May be due to exon 2 skipping. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the BLOC1S6 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; AF079530; AAF09262.1; -; mRNA. DR EMBL; AF082574; AAF42469.1; -; Genomic_DNA. DR EMBL; AF082571; AAF42469.1; JOINED; Genomic_DNA. DR EMBL; AF082572; AAF42469.1; JOINED; Genomic_DNA. DR EMBL; AF082573; AAF42469.1; JOINED; Genomic_DNA. DR EMBL; AK038381; BAC29977.1; -; mRNA. DR EMBL; AK077720; BAC36979.1; -; mRNA. DR EMBL; AK147116; BAE27688.1; -; mRNA. DR EMBL; AK160580; BAE35887.1; -; mRNA. DR EMBL; AL928950; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC016554; AAH16554.1; -; mRNA. DR CCDS; CCDS16668.1; -. [Q9R0C0-1] DR RefSeq; NP_062762.1; NM_019788.3. [Q9R0C0-1] DR AlphaFoldDB; Q9R0C0; -. DR SMR; Q9R0C0; -. DR BioGRID; 202009; 3. DR ComplexPortal; CPX-1913; BLOC-1 complex. DR CORUM; Q9R0C0; -. DR STRING; 10090.ENSMUSP00000005954; -. DR PhosphoSitePlus; Q9R0C0; -. DR EPD; Q9R0C0; -. DR MaxQB; Q9R0C0; -. DR PaxDb; 10090-ENSMUSP00000005954; -. DR PeptideAtlas; Q9R0C0; -. DR ProteomicsDB; 281693; -. [Q9R0C0-1] DR ProteomicsDB; 281694; -. [Q9R0C0-2] DR Pumba; Q9R0C0; -. DR Antibodypedia; 24448; 237 antibodies from 31 providers. DR DNASU; 18457; -. DR Ensembl; ENSMUST00000005954.9; ENSMUSP00000005954.9; ENSMUSG00000005804.15. [Q9R0C0-1] DR GeneID; 18457; -. DR KEGG; mmu:18457; -. DR UCSC; uc008mbf.1; mouse. [Q9R0C0-1] DR AGR; MGI:1927580; -. DR CTD; 26258; -. DR MGI; MGI:1927580; Bloc1s6. DR VEuPathDB; HostDB:ENSMUSG00000005804; -. DR eggNOG; ENOG502RZNC; Eukaryota. DR GeneTree; ENSGT00510000047812; -. DR HOGENOM; CLU_115118_1_0_1; -. DR InParanoid; Q9R0C0; -. DR OMA; MMSDVKR; -. DR OrthoDB; 2970759at2759; -. DR PhylomeDB; Q9R0C0; -. DR TreeFam; TF325188; -. DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis. DR BioGRID-ORCS; 18457; 3 hits in 78 CRISPR screens. DR ChiTaRS; Bloc1s6; mouse. DR PRO; PR:Q9R0C0; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q9R0C0; Protein. DR Bgee; ENSMUSG00000005804; Expressed in interventricular septum and 259 other cell types or tissues. 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; ISS:UniProtKB. DR GO; GO:0005768; C:endosome; IDA:MGI. DR GO; GO:0043227; C:membrane-bounded organelle; ISS:UniProtKB. DR GO; GO:0031201; C:SNARE complex; IEA:Ensembl. DR GO; GO:0030133; C:transport vesicle; ISS:UniProtKB. DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0042803; F:protein homodimerization activity; 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:0007596; P:blood coagulation; IMP:MGI. DR GO; GO:0035646; P:endosome to melanosome transport; ISS:UniProtKB. DR GO; GO:0046907; P:intracellular transport; IBA:GO_Central. DR GO; GO:0030318; P:melanocyte differentiation; IMP:MGI. DR GO; GO:0032438; P:melanosome organization; NAS:ComplexPortal. DR GO; GO:0032402; P:melanosome transport; ISS:UniProtKB. DR GO; GO:0061025; P:membrane fusion; IPI:MGI. DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB. DR GO; GO:0043473; P:pigmentation; IMP:MGI. DR GO; GO:0032816; P:positive regulation of natural killer cell activation; IMP:MGI. DR GO; GO:0050942; P:positive regulation of pigment cell differentiation; ISS:UniProtKB. DR GO; GO:0033299; P:secretion of lysosomal enzymes; IMP:MGI. DR GO; GO:0006904; P:vesicle docking involved in exocytosis; TAS:MGI. DR GO; GO:0006906; P:vesicle fusion; TAS:MGI. DR InterPro; IPR017242; BLOC-1_pallidin. DR InterPro; IPR028119; Snapin/Pallidin/Snn1. DR PANTHER; PTHR31328; BIOGENESIS OF LYSOSOME-RELATED ORGANELLES COMPLEX 1 SUBUNIT 6; 1. DR PANTHER; PTHR31328:SF2; BIOGENESIS OF LYSOSOME-RELATED ORGANELLES COMPLEX 1 SUBUNIT 6; 1. DR Pfam; PF14712; Snapin_Pallidin; 1. DR PIRSF; PIRSF037609; BLOC-1_complex_pallidin; 1. DR Genevisible; Q9R0C0; MM. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Cytoplasm; Membrane; Phosphoprotein; KW Reference proteome. FT CHAIN 1..172 FT /note="Biogenesis of lysosome-related organelles complex 1 FT subunit 6" FT /id="PRO_0000058459" FT REGION 1..37 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 141..172 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 63..167 FT /evidence="ECO:0000255" FT VAR_SEQ 76..80 FT /note="QNQVV -> TKLCY (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009295" FT VAR_SEQ 81..172 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009296" FT VARIANT 14 FT /note="T -> M (in strain: C57BL/6J-pa mutants)" FT /evidence="ECO:0000269|PubMed:10610180" FT VARIANT 32 FT /note="T -> M (in strain: BALB/c, CBA and C57BL/6J-pa FT mutants)" FT /evidence="ECO:0000269|PubMed:10610180, FT ECO:0000269|PubMed:15489334" SQ SEQUENCE 172 AA; 19682 MW; 6B8068DF091B07D2 CRC64; MSVPEPPPPD GVLTGPSDSL EAGEPTPGLS DTSPDEGLIE DFPVDDRAVE HLVGGLLSHY LPDLQRSKRA LQELTQNQVV LLDTLEQEIS KFKECHSMLD INALFTEAKH YHAKLVTIRK EMLLLHEKTS KLKKRALKLQ QKRQREELER EQQREKEFER EKQLTAKPAK RT //