ID   HPS6_RAT                Reviewed;         809 AA.
AC   Q7M733;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=BLOC-2 complex member HPS6 {ECO:0000305};
DE   AltName: Full=Hermansky-Pudlak syndrome 6 protein homolog;
DE   AltName: Full=Ruby-eye protein homolog;
DE   AltName: Full=Ruby-eye-like protein;
DE            Short=Ru;
GN   Name=Hps6;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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   [3]
RP   IDENTIFICATION.
RX   PubMed=12548288; DOI=10.1038/ng1087;
RA   Zhang Q., Zhao B., Li W., Oiso N., Novak E.K., Rusiniak M.E., Gautam R.,
RA   Chintala S., O'Brien E.P., Zhang Y., Roe B.A., Elliott R.W., Eicher E.M.,
RA   Liang P., Kratz C., Legius E., Spritz R.A., O'Sullivan T.N., Copeland N.G.,
RA   Jenkins N.A., Swank R.T.;
RT   "Ru2 and Ru encode mouse orthologs of the genes mutated in human Hermansky-
RT   Pudlak syndrome types 5 and 6.";
RL   Nat. Genet. 33:145-153(2003).
RN   [4]
RP   INTERACTION WITH AP-3 COMPLEX.
RX   PubMed=19010779; DOI=10.1074/jbc.m805991200;
RA   Salazar G., Zlatic S., Craige B., Peden A.A., Pohl J., Faundez V.;
RT   "Hermansky-Pudlak syndrome protein complexes associate with
RT   phosphatidylinositol 4-kinase type II alpha in neuronal and non-neuronal
RT   cells.";
RL   J. Biol. Chem. 284:1790-1802(2009).
CC   -!- FUNCTION: May regulate the synthesis and function of lysosomes and of
CC       highly specialized organelles, such as melanosomes and platelet dense
CC       granules. Acts as cargo adapter for the dynein-dynactin motor complex
CC       to mediate the transport of lysosomes from the cell periphery to the
CC       perinuclear region. Facilitates retrograde lysosomal trafficking by
CC       linking the motor complex to lysosomes, and perinuclear positioning of
CC       lysosomes is crucial for the delivery of endocytic cargos to lysosomes,
CC       for lysosome maturation and functioning.
CC       {ECO:0000250|UniProtKB:Q86YV9}.
CC   -!- SUBUNIT: Component of the biogenesis of lysosome-related organelles
CC       complex-2 (or BLOC2) composed of HPS3, HPS5 and HPS6. Interacts with
CC       HPS5 and HPS3. Interacts with biogenesis of lysosome-related organelles
CC       complex-1 (BLOC1) (By similarity). Interacts with AP-3 complex
CC       (PubMed:19010779). Interacts with DCTN1 and dynein intermediate chain
CC       (By similarity). {ECO:0000250|UniProtKB:Q86YV9,
CC       ECO:0000269|PubMed:19010779}.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane
CC       {ECO:0000250|UniProtKB:Q86YV9}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q86YV9}. Early endosome membrane
CC       {ECO:0000250|UniProtKB:Q86YV9}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:Q86YV9}.
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DR   EMBL; AC093941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK000658; DAA00971.1; -; Genomic_DNA.
DR   EMBL; BC086975; AAH86975.1; -; mRNA.
DR   RefSeq; NP_852097.1; NM_181432.2.
DR   AlphaFoldDB; Q7M733; -.
DR   STRING; 10116.ENSRNOP00000024898; -.
DR   PhosphoSitePlus; Q7M733; -.
DR   PaxDb; Q7M733; -.
DR   PRIDE; Q7M733; -.
DR   Ensembl; ENSRNOT00000024898; ENSRNOP00000024898; ENSRNOG00000018433.
DR   GeneID; 309446; -.
DR   KEGG; rno:309446; -.
DR   UCSC; RGD:631341; rat.
DR   CTD; 79803; -.
DR   RGD; 631341; Hps6.
DR   eggNOG; ENOG502QSBH; Eukaryota.
DR   GeneTree; ENSGT00390000001546; -.
DR   HOGENOM; CLU_019081_0_0_1; -.
DR   InParanoid; Q7M733; -.
DR   OMA; VWCEERQ; -.
DR   OrthoDB; 287250at2759; -.
DR   PhylomeDB; Q7M733; -.
DR   TreeFam; TF331635; -.
DR   PRO; PR:Q7M733; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000018433; Expressed in spleen and 19 other tissues.
DR   Genevisible; Q7M733; RN.
DR   GO; GO:0031084; C:BLOC-2 complex; ISO:RGD.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0030742; F:GTP-dependent protein binding; ISO:RGD.
DR   GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR   GO; GO:0007596; P:blood coagulation; ISO:RGD.
DR   GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR   GO; GO:0030318; P:melanocyte differentiation; ISO:RGD.
DR   GO; GO:0006996; P:organelle organization; ISO:RGD.
DR   GO; GO:0043473; P:pigmentation; ISO:RGD.
DR   GO; GO:0072657; P:protein localization to membrane; ISO:RGD.
DR   InterPro; IPR017218; BLOC-2_complex_Hps6_subunit.
DR   PANTHER; PTHR14696; PTHR14696; 1.
DR   Pfam; PF15702; HPS6; 1.
DR   PIRSF; PIRSF037476; BLOC-2_complex_Hps6; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endoplasmic reticulum; Endosome; Lysosome; Membrane; Microsome;
KW   Reference proteome.
FT   CHAIN           1..809
FT                   /note="BLOC-2 complex member HPS6"
FT                   /id="PRO_0000084058"
FT   REGION          747..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..764
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  87463 MW;  E3D6A10D877C1DBA CRC64;
     MKRAGTLRLL SDLSNFTGAA RLRELLAGDP AILVRCSPDG RHLLLLRPPG SPAPQLLVAV
     RGPGLPLERA WSEGDPSPLD VFFVPWLARP ALILVWESGL TEVWGVGMEP GWKLLQSTEL
     CPDGGARVMA VAATRGRLVW CEERQPGVED QPGQLSMAFN HCVCVKTLDT SGEAGTKLGC
     THILLHHCPS FGLIASRKEL FLVPTSTTWP GVAHVLLIWS PSKGKVIVAA PSLGLSHSKS
     LNPKQGDTWD FRTLLRGLPG FLSPREPLAV HTWAPSSQGL LLLDLKGKVS LVQCHGGTRT
     VGLLQEAPVG LQGSAALGTF HGTLACVLGS TLELLDMSSG RLLERKVLST DRVHLLEPPA
     PGVKNEEDLE TRGALRLLSA LGLFCVCWEA PQGLEVPSDK DLVFEEACGY YQRRSLRGTQ
     LTPEELRHNS MFRAPQALAS ILQGHLPPSA LLTTLRAELR DYRSIEQLKA QLVAGDDEET
     GWTELAEHEV ARLLRTHLTG DQLAQFNTIF QALPTAAWSA TLQALQLQPD RSGRLRSQAP
     PDVWKKVLRA PTAGKEHPNG ILPPFELLCQ CLGQLEPQWL PPFVELAQQQ GGPGWGAEGP
     SLPLYRRALS VLGEEGKRPE ALELELLLGS GRPKAVLQAV RQLIKKEQWE RALEAGLTLD
     SSSPLLRSEI FNLLLAEFAQ HRRLDTHLPL LCRLCPPEVA PDELLLLLRT HLPDDAGATP
     FPEPGAEPGA EPPLTVGLVR ALLEQTGAQG RSSGPVQSTF EDILWDSGTP PPTPPRGPMT
     TLQASDHPGQ EAWGPSGQGL GAADVGVHS