BL1S6_MOUSE
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 03-AUG-2022, entry version 153.
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, and
RC 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}.
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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; Q9R0C0; -.
DR PeptideAtlas; Q9R0C0; -.
DR PRIDE; Q9R0C0; -.
DR ProteomicsDB; 281693; -. [Q9R0C0-1]
DR ProteomicsDB; 281694; -. [Q9R0C0-2]
DR Antibodypedia; 24448; 212 antibodies from 31 providers.
DR DNASU; 18457; -.
DR Ensembl; ENSMUST00000005954; ENSMUSP00000005954; ENSMUSG00000005804. [Q9R0C0-1]
DR GeneID; 18457; -.
DR KEGG; mmu:18457; -.
DR UCSC; uc008mbf.1; mouse. [Q9R0C0-1]
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; 1509390at2759; -.
DR PhylomeDB; Q9R0C0; -.
DR TreeFam; TF325188; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 18457; 3 hits in 73 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 256 other tissues.
DR Genevisible; Q9R0C0; 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; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; ISO:MGI.
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; IC: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 Pfam; PF14712; Snapin_Pallidin; 1.
DR PIRSF; PIRSF037609; BLOC-1_complex_pallidin; 1.
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
