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   10-FEB-2021, entry version 168.
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   BioGRID; 117644; 72.
DR   ComplexPortal; CPX-1910; BLOC-1 complex.
DR   CORUM; Q9UL45; -.
DR   IntAct; Q9UL45; 47.
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   PaxDb; Q9UL45; -.
DR   PeptideAtlas; Q9UL45; -.
DR   PRIDE; Q9UL45; -.
DR   ProteomicsDB; 84945; -. [Q9UL45-1]
DR   ProteomicsDB; 84946; -. [Q9UL45-2]
DR   Antibodypedia; 24448; 194 antibodies.
DR   Ensembl; ENST00000220531; ENSP00000220531; ENSG00000104164. [Q9UL45-1]
DR   Ensembl; ENST00000567523; ENSP00000456624; ENSG00000104164. [Q9UL45-2]
DR   GeneID; 26258; -.
DR   KEGG; hsa:26258; -.
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; 280663; Hermansky-Pudlak syndrome type 9.
DR   PharmGKB; PA33398; -.
DR   VEuPathDB; HostDB:ENSG00000104164.10; -.
DR   eggNOG; ENOG502RZNC; Eukaryota.
DR   GeneTree; ENSGT00510000047812; -.
DR   HOGENOM; CLU_115118_1_0_1; -.
DR   InParanoid; Q9UL45; -.
DR   OMA; ARLNDMM; -.
DR   PhylomeDB; Q9UL45; -.
DR   TreeFam; TF325188; -.
DR   PathwayCommons; Q9UL45; -.
DR   Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR   BioGRID-ORCS; 26258; 20 hits in 878 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 224 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: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:0035646; P:endosome to melanosome transport; IDA:UniProtKB.
DR   GO; GO:0046907; P:intracellular transport; IBA:GO_Central.
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:0050942; P:positive regulation of pigment cell differentiation; IDA:UniProtKB.
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   COILED          63..167
FT                   /evidence="ECO:0000255"
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
//