BL1S6_HUMAN
ID BL1S6_HUMAN Reviewed; 172 AA.
AC Q9UL45;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 6;
DE Short=BLOC-1 subunit 6;
DE AltName: Full=Pallid protein homolog;
DE AltName: Full=Pallidin;
DE AltName: Full=Syntaxin 13-interacting protein;
GN Name=BLOC1S6; Synonyms=PA, PLDN;
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] (ISOFORM 1).
RC 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 2).
RC TISSUE=Thymus;
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] (ISOFORM 1).
RC TISSUE=Placenta;
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 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 [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH
RP STX12 AND BLOC1S5, AND HOMODIMERIZATION.
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 [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH BLOC1S5 AND
RP 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 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 [8]
RP IDENTIFICATION IN THE BLOC-1 COMPLEX, AND INTERACTION WITH SNAP25; SNAP47
RP AND STX12.
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 RETRACTED PAPER.
RX PubMed=21665000; DOI=10.1016/j.ajhg.2011.05.009;
RA Cullinane A.R., Curry J.A., Carmona-Rivera C., Summers C.G., Ciccone C.,
RA Cardillo N.D., Dorward H., Hess R.A., White J.G., Adams D., Huizing M.,
RA Gahl W.A.;
RT "A BLOC-1 mutation screen reveals that PLDN is mutated in Hermansky-Pudlak
RT Syndrome type 9.";
RL Am. J. Hum. Genet. 88:778-787(2011).
RN [10]
RP RETRACTION NOTICE OF PUBMED:21665000.
RX PubMed=28475864; DOI=10.1016/j.ajhg.2017.04.011;
RA Cullinane A.R., Curry J.A., Carmona-Rivera C., Summers C.G., Ciccone C.,
RA Cardillo N.D., Dorward H., Hess R.A., White J.G., Adams D., Huizing M.,
RA Gahl W.A.;
RT "Retraction Notice to: A BLOC-1 Mutation Screen Reveals that PLDN Is
RT Mutated in Hermansky-Pudlak Syndrome Type 9.";
RL Am. J. Hum. Genet. 100:837-837(2017).
RN [11]
RP FUNCTION, ASSOCIATION WITH THE AP-3 COMPLEX, AND INTERACTION WITH BLOC1S5.
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 [12]
RP INVOLVEMENT IN HPS9, VARIANT HPS9 78-GLN--MET-172 DEL, AND CHARACTERIZATION
RP OF VARIANT HPS9 78-GLN--MET-172 DEL.
RX PubMed=22461475; DOI=10.1182/blood-2012-01-404350;
RA Badolato R., Prandini A., Caracciolo S., Colombo F., Tabellini G.,
RA Giacomelli M., Cantarini M.E., Pession A., Bell C.J., Dinwiddie D.L.,
RA Miller N.A., Hateley S.L., Saunders C.J., Zhang L., Schroth G.P.,
RA Plebani A., Parolini S., Kingsmore S.F.;
RT "Exome sequencing reveals a pallidin mutation in a Hermansky-Pudlak-like
RT primary immunodeficiency syndrome.";
RL Blood 119:3185-3187(2012).
RN [13]
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 [14]
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 May play a role in intracellular vesicle trafficking, particularly in
CC the vesicle-docking and fusion process. {ECO:0000269|PubMed:17182842,
CC ECO:0000269|PubMed:21998198}.
CC -!- SUBUNIT: Interacts with BLOC1S4 and DTNBP1/BLOC1S7 (By similarity).
CC Homodimer. 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. The BLOC-1 complex associates with
CC the AP-3 protein complex and membrane protein cargos. Interacts with
CC BLOC1S5, F-actin, SNAP25 isoform 1 and isoform 2, SNAP47 and STX12.
CC {ECO:0000250, ECO:0000269|PubMed:12019270, ECO:0000269|PubMed:12191018,
CC ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:19546860,
CC ECO:0000269|PubMed:21998198, ECO:0000269|PubMed:22203680}.
CC -!- INTERACTION:
CC Q9UL45; Q9NYB9: ABI2; NbExp=5; IntAct=EBI-465781, EBI-743598;
CC Q9UL45; Q9NYB9-2: ABI2; NbExp=6; IntAct=EBI-465781, EBI-11096309;
CC Q9UL45; P78537: BLOC1S1; NbExp=17; IntAct=EBI-465781, EBI-348630;
CC Q9UL45; Q9NUP1: BLOC1S4; NbExp=5; IntAct=EBI-465781, EBI-465852;
CC Q9UL45; Q9UL45: BLOC1S6; NbExp=3; IntAct=EBI-465781, EBI-465781;
CC Q9UL45; Q504U0: C4orf46; NbExp=3; IntAct=EBI-465781, EBI-6657981;
CC Q9UL45; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-465781, EBI-10171416;
CC Q9UL45; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-465781, EBI-10175300;
CC Q9UL45; Q8N619: CDK5R1; NbExp=3; IntAct=EBI-465781, EBI-10266998;
CC Q9UL45; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-465781, EBI-744115;
CC Q9UL45; Q6QEF8: CORO6; NbExp=3; IntAct=EBI-465781, EBI-10254194;
CC Q9UL45; Q13561: DCTN2; NbExp=3; IntAct=EBI-465781, EBI-715074;
CC Q9UL45; Q96EV8: DTNBP1; NbExp=9; IntAct=EBI-465781, EBI-465804;
CC Q9UL45; Q8IYI6: EXOC8; NbExp=4; IntAct=EBI-465781, EBI-742102;
CC Q9UL45; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-465781, EBI-2514791;
CC Q9UL45; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-465781, EBI-9091197;
CC Q9UL45; Q2T9L4: INSYN1; NbExp=7; IntAct=EBI-465781, EBI-4311436;
CC Q9UL45; A1A4E9: KRT13; NbExp=3; IntAct=EBI-465781, EBI-10171552;
CC Q9UL45; Q14CN4: KRT72; NbExp=3; IntAct=EBI-465781, EBI-1221280;
CC Q9UL45; Q13503: MED21; NbExp=3; IntAct=EBI-465781, EBI-394678;
CC Q9UL45; Q9BV36: MLPH; NbExp=3; IntAct=EBI-465781, EBI-7042162;
CC Q9UL45; P37198: NUP62; NbExp=6; IntAct=EBI-465781, EBI-347978;
CC Q9UL45; Q9H8W4: PLEKHF2; NbExp=4; IntAct=EBI-465781, EBI-742388;
CC Q9UL45; Q9UJ41: RABGEF1; NbExp=3; IntAct=EBI-465781, EBI-913954;
CC Q9UL45; Q9UJ41-4: RABGEF1; NbExp=6; IntAct=EBI-465781, EBI-14093916;
CC Q9UL45; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-465781, EBI-726876;
CC Q9UL45; Q96BD8: SKA1; NbExp=8; IntAct=EBI-465781, EBI-741854;
CC Q9UL45; Q16637: SMN2; NbExp=6; IntAct=EBI-465781, EBI-395421;
CC Q9UL45; O75558: STX11; NbExp=6; IntAct=EBI-465781, EBI-714135;
CC Q9UL45; Q16623: STX1A; NbExp=3; IntAct=EBI-465781, EBI-712466;
CC Q9UL45; A1L190: SYCE3; NbExp=3; IntAct=EBI-465781, EBI-10283466;
CC Q9UL45; P09493-10: TPM1; NbExp=5; IntAct=EBI-465781, EBI-12123928;
CC Q9UL45; Q5VU62: TPM3; NbExp=3; IntAct=EBI-465781, EBI-10184033;
CC Q9UL45; Q9Y3C0: WASHC3; NbExp=8; IntAct=EBI-465781, EBI-712969;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12019270,
CC ECO:0000269|PubMed:12191018}. Membrane {ECO:0000269|PubMed:12019270,
CC ECO:0000269|PubMed:12191018}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12019270}. Note=It can exist as a soluble protein
CC as well as a peripheral membrane protein (PubMed:12019270).
CC {ECO:0000269|PubMed:12019270}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UL45-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UL45-2; Sequence=VSP_009293, VSP_009294;
CC Name=3;
CC IsoId=Q9UL45-3; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12019270,
CC ECO:0000269|PubMed:12191018}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:12191018}.
CC -!- DISEASE: Hermansky-Pudlak syndrome 9 (HPS9) [MIM:614171]: 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:22461475}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to exons 2 and 3 skipping.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BLOC1S6 family. {ECO:0000305}.
CC -!- CAUTION: A paper showing involvement in Hermansky-Pudlak syndrome 9 was
CC retracted due to image duplication. {ECO:0000269|PubMed:21665000,
CC ECO:0000305|PubMed:28475864}.
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DR EMBL; AF080470; AAF08343.1; -; mRNA.
DR EMBL; AK057545; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC004819; AAH04819.1; -; mRNA.
DR CCDS; CCDS10126.1; -. [Q9UL45-1]
DR RefSeq; NP_036520.1; NM_012388.3. [Q9UL45-1]
DR AlphaFoldDB; Q9UL45; -.
DR SMR; Q9UL45; -.
DR BioGRID; 117644; 76.
DR ComplexPortal; CPX-1910; BLOC-1 complex.
DR CORUM; Q9UL45; -.
DR IntAct; Q9UL45; 49.
DR MINT; Q9UL45; -.
DR STRING; 9606.ENSP00000220531; -.
DR iPTMnet; Q9UL45; -.
DR PhosphoSitePlus; Q9UL45; -.
DR BioMuta; BLOC1S6; -.
DR DMDM; 41017511; -.
DR EPD; Q9UL45; -.
DR jPOST; Q9UL45; -.
DR MassIVE; Q9UL45; -.
DR MaxQB; Q9UL45; -.
DR PaxDb; Q9UL45; -.
DR PeptideAtlas; Q9UL45; -.
DR PRIDE; Q9UL45; -.
DR ProteomicsDB; 84945; -. [Q9UL45-1]
DR ProteomicsDB; 84946; -. [Q9UL45-2]
DR Antibodypedia; 24448; 212 antibodies from 31 providers.
DR DNASU; 26258; -.
DR Ensembl; ENST00000220531.9; ENSP00000220531.4; ENSG00000104164.12. [Q9UL45-1]
DR Ensembl; ENST00000567523.5; ENSP00000456624.1; ENSG00000104164.12. [Q9UL45-2]
DR GeneID; 26258; -.
DR KEGG; hsa:26258; -.
DR MANE-Select; ENST00000220531.9; ENSP00000220531.4; NM_012388.4; NP_036520.1.
DR UCSC; uc001zvq.4; human. [Q9UL45-1]
DR CTD; 26258; -.
DR DisGeNET; 26258; -.
DR GeneCards; BLOC1S6; -.
DR GeneReviews; BLOC1S6; -.
DR HGNC; HGNC:8549; BLOC1S6.
DR HPA; ENSG00000104164; Low tissue specificity.
DR MalaCards; BLOC1S6; -.
DR MIM; 604310; gene.
DR MIM; 614171; phenotype.
DR neXtProt; NX_Q9UL45; -.
DR OpenTargets; ENSG00000104164; -.
DR Orphanet; 231531; Hermansky-Pudlak syndrome due to BLOC-1 deficiency.
DR PharmGKB; PA33398; -.
DR VEuPathDB; HostDB:ENSG00000104164; -.
DR eggNOG; ENOG502RZNC; Eukaryota.
DR GeneTree; ENSGT00510000047812; -.
DR HOGENOM; CLU_115118_1_0_1; -.
DR InParanoid; Q9UL45; -.
DR OMA; MMSDVKR; -.
DR PhylomeDB; Q9UL45; -.
DR TreeFam; TF325188; -.
DR PathwayCommons; Q9UL45; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; Q9UL45; -.
DR SIGNOR; Q9UL45; -.
DR BioGRID-ORCS; 26258; 25 hits in 1081 CRISPR screens.
DR ChiTaRS; BLOC1S6; human.
DR GeneWiki; PLDN; -.
DR GenomeRNAi; 26258; -.
DR Pharos; Q9UL45; Tbio.
DR PRO; PR:Q9UL45; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9UL45; protein.
DR Bgee; ENSG00000104164; Expressed in epithelial cell of pancreas and 194 other tissues.
DR ExpressionAtlas; Q9UL45; baseline and differential.
DR Genevisible; Q9UL45; HS.
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:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; TAS:UniProtKB.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
DR GO; GO:0035646; P:endosome to melanosome transport; IDA:UniProtKB.
DR GO; GO:0046907; P:intracellular transport; IBA:GO_Central.
DR GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
DR GO; GO:0032438; P:melanosome organization; NAS:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; IDA:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0032816; P:positive regulation of natural killer cell activation; IEA:Ensembl.
DR GO; GO:0050942; P:positive regulation of pigment cell differentiation; IDA:UniProtKB.
DR GO; GO:0033299; P:secretion of lysosomal enzymes; IEA:Ensembl.
DR GO; GO:0016081; P:synaptic vesicle docking; NAS:UniProtKB.
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 Albinism; Alternative splicing; Coiled coil; Cytoplasm; Disease variant;
KW Hermansky-Pudlak syndrome; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..172
FT /note="Biogenesis of lysosome-related organelles complex 1
FT subunit 6"
FT /id="PRO_0000058458"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 63..167
FT /evidence="ECO:0000255"
FT COMPBIAS 140..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 76..80
FT /note="QNQVV -> TKLYC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009293"
FT VAR_SEQ 81..172
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009294"
FT VARIANT 78..172
FT /note="Missing (in HPS9; reduces NK cell cytolytic
FT activity; increases LAMP1/CD107A and CD63 levels at the
FT cell membrane)"
FT /evidence="ECO:0000269|PubMed:22461475"
FT /id="VAR_081117"
SQ SEQUENCE 172 AA; 19744 MW; 37902FCFD4802294 CRC64;
MSVPGPSSPD GALTRPPYCL EAGEPTPGLS DTSPDEGLIE DLTIEDKAVE QLAEGLLSHY
LPDLQRSKQA LQELTQNQVV LLDTLEQEIS KFKECHSMLD INALFAEAKH YHAKLVNIRK
EMLMLHEKTS KLKKRALKLQ QKRQKEELER EQQREKEFER EKQLTARPAK RM
