HPS4_HUMAN
ID HPS4_HUMAN Reviewed; 708 AA.
AC Q9NQG7; B1AHQ4; Q5H8V6; Q96LX6; Q9BY93; Q9UH37; Q9UH38;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=BLOC-3 complex member HPS4 {ECO:0000305};
DE AltName: Full=Hermansky-Pudlak syndrome 4 protein;
DE AltName: Full=Light-ear protein homolog;
GN Name=HPS4; Synonyms=KIAA1667;
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), AND INVOLVEMENT IN HPS4.
RX PubMed=11836498; DOI=10.1038/ng835;
RA Suzuki T., Li W., Zhang Q., Karim A., Novak E.K., Sviderskaya E.V.,
RA Hill S.P., Bennett D.C., Levin A.V., Nieuwenhuis H.K., Fong C.-T.,
RA Castellan C., Miterski B., Swank R.T., Spritz R.A.;
RT "Hermansky-Pudlak syndrome is caused by mutations in HPS4, the human
RT homolog of the mouse light-ear gene.";
RL Nat. Genet. 30:321-324(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-229.
RC TISSUE=Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-229;
RP VAL-443; MET-552; TYR-606 AND HIS-625.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS GLY-229;
RP MET-552 AND TYR-606.
RC TISSUE=Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-708 (ISOFORM 1), AND VARIANTS
RP MET-552; TYR-606 AND HIS-625.
RC TISSUE=Brain;
RX PubMed=11258795; DOI=10.1093/dnares/8.1.1;
RA Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT "Identification of novel transcribed sequences on human chromosome 22 by
RT expressed sequence tag mapping.";
RL DNA Res. 8:1-9(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP SUBUNIT, INTERACTION WITH RAB9A AND RAB9B, AND LACK OF INTERACTION WITH
RP RAB5A; RAB7A AND RAB27A.
RX PubMed=20048159; DOI=10.1074/jbc.m109.069088;
RA Kloer D.P., Rojas R., Ivan V., Moriyama K., van Vlijmen T., Murthy N.,
RA Ghirlando R., van der Sluijs P., Hurley J.H., Bonifacino J.S.;
RT "Assembly of the biogenesis of lysosome-related organelles complex-3 (BLOC-
RT 3) and its interaction with Rab9.";
RL J. Biol. Chem. 285:7794-7804(2010).
RN [11]
RP FUNCTION, AND SUBUNIT.
RX PubMed=23084991; DOI=10.1016/j.cub.2012.09.020;
RA Gerondopoulos A., Langemeyer L., Liang J.R., Linford A., Barr F.A.;
RT "BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine
RT nucleotide exchange factor.";
RL Curr. Biol. 22:2135-2139(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
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-3 complex, a complex that acts as a
CC guanine exchange factor (GEF) for RAB32 and RAB38, promotes the
CC exchange of GDP to GTP, converting them from an inactive GDP-bound form
CC into an active GTP-bound form. The BLOC-3 complex plays an important
CC role in the control of melanin production and melanosome biogenesis and
CC promotes the membrane localization of RAB32 and RAB38
CC (PubMed:23084991). {ECO:0000269|PubMed:23084991}.
CC -!- SUBUNIT: Component of the biogenesis of lysosome-related organelles
CC complex-3 (or BLOC-3), a heterodimer of HPS1 and HPS4 (PubMed:20048159,
CC PubMed:23084991). HPS4 and the BLOC-3 complex interact with the GTP-
CC bound form of RAB9A and RAB9B but not with the GDP-bound form of RAB9A
CC and RAB9B. The BLOC-3 complex does not interact with RAB5A, RAB7A and
CC RAB27A (PubMed:20048159). {ECO:0000269|PubMed:20048159,
CC ECO:0000269|PubMed:23084991}.
CC -!- INTERACTION:
CC Q9NQG7; Q92902: HPS1; NbExp=17; IntAct=EBI-704377, EBI-704347;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NQG7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQG7-2; Sequence=VSP_003880, VSP_003881, VSP_003882;
CC Name=3;
CC IsoId=Q9NQG7-3; Sequence=VSP_017082;
CC Name=4;
CC IsoId=Q9NQG7-4; Sequence=VSP_017082, VSP_003880;
CC -!- DISEASE: Hermansky-Pudlak syndrome 4 (HPS4) [MIM:614073]: 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:11836498}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB33337.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB33337.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BC035614; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mutations of the HPS4 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/lemut.htm";
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; AY043416; AAK95330.1; -; mRNA.
DR EMBL; AL365512; CAB97208.1; -; mRNA.
DR EMBL; AK057648; BAB71540.1; -; mRNA.
DR EMBL; AL713795; CAD28549.1; -; mRNA.
DR EMBL; Z99714; CAI17880.1; -; Genomic_DNA.
DR EMBL; Z99714; CAQ09361.1; -; Genomic_DNA.
DR EMBL; BC035614; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB051454; BAB33337.1; ALT_SEQ; mRNA.
DR CCDS; CCDS13835.1; -. [Q9NQG7-1]
DR CCDS; CCDS46677.1; -. [Q9NQG7-3]
DR RefSeq; NP_071364.4; NM_022081.5. [Q9NQG7-1]
DR RefSeq; NP_690054.1; NM_152841.2. [Q9NQG7-3]
DR RefSeq; XP_016884531.1; XM_017029042.1.
DR RefSeq; XP_016884532.1; XM_017029043.1.
DR RefSeq; XP_016884533.1; XM_017029044.1.
DR AlphaFoldDB; Q9NQG7; -.
DR BioGRID; 124600; 1.
DR ComplexPortal; CPX-5043; BLOC-3 complex.
DR CORUM; Q9NQG7; -.
DR IntAct; Q9NQG7; 6.
DR STRING; 9606.ENSP00000381213; -.
DR iPTMnet; Q9NQG7; -.
DR PhosphoSitePlus; Q9NQG7; -.
DR BioMuta; HPS4; -.
DR DMDM; 21362617; -.
DR EPD; Q9NQG7; -.
DR jPOST; Q9NQG7; -.
DR MassIVE; Q9NQG7; -.
DR MaxQB; Q9NQG7; -.
DR PaxDb; Q9NQG7; -.
DR PeptideAtlas; Q9NQG7; -.
DR PRIDE; Q9NQG7; -.
DR ProteomicsDB; 82150; -. [Q9NQG7-1]
DR ProteomicsDB; 82151; -. [Q9NQG7-2]
DR ProteomicsDB; 82152; -. [Q9NQG7-3]
DR ProteomicsDB; 82153; -. [Q9NQG7-4]
DR Antibodypedia; 54828; 53 antibodies from 16 providers.
DR DNASU; 89781; -.
DR Ensembl; ENST00000336873.9; ENSP00000338457.5; ENSG00000100099.21. [Q9NQG7-1]
DR Ensembl; ENST00000398145.7; ENSP00000381213.2; ENSG00000100099.21. [Q9NQG7-1]
DR Ensembl; ENST00000402105.7; ENSP00000384185.3; ENSG00000100099.21. [Q9NQG7-3]
DR GeneID; 89781; -.
DR KEGG; hsa:89781; -.
DR MANE-Select; ENST00000398145.7; ENSP00000381213.2; NM_022081.6; NP_071364.4.
DR UCSC; uc003aci.5; human. [Q9NQG7-1]
DR CTD; 89781; -.
DR DisGeNET; 89781; -.
DR GeneCards; HPS4; -.
DR GeneReviews; HPS4; -.
DR HGNC; HGNC:15844; HPS4.
DR HPA; ENSG00000100099; Low tissue specificity.
DR MalaCards; HPS4; -.
DR MIM; 606682; gene.
DR MIM; 614073; phenotype.
DR neXtProt; NX_Q9NQG7; -.
DR OpenTargets; ENSG00000100099; -.
DR Orphanet; 231500; Hermansky-Pudlak syndrome due to BLOC-3 deficiency.
DR PharmGKB; PA29434; -.
DR VEuPathDB; HostDB:ENSG00000100099; -.
DR eggNOG; ENOG502QSIZ; Eukaryota.
DR GeneTree; ENSGT00390000007349; -.
DR HOGENOM; CLU_028579_0_0_1; -.
DR InParanoid; Q9NQG7; -.
DR OMA; FYNGPVR; -.
DR OrthoDB; 359138at2759; -.
DR PhylomeDB; Q9NQG7; -.
DR TreeFam; TF332819; -.
DR PathwayCommons; Q9NQG7; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q9NQG7; -.
DR SIGNOR; Q9NQG7; -.
DR BioGRID-ORCS; 89781; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; HPS4; human.
DR GeneWiki; HPS4; -.
DR GenomeRNAi; 89781; -.
DR Pharos; Q9NQG7; Tbio.
DR PRO; PR:Q9NQG7; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9NQG7; protein.
DR Bgee; ENSG00000100099; Expressed in cerebellar hemisphere and 174 other tissues.
DR ExpressionAtlas; Q9NQG7; baseline and differential.
DR Genevisible; Q9NQG7; HS.
DR GO; GO:0031085; C:BLOC-3 complex; IPI:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0042827; C:platelet dense granule; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
DR GO; GO:0007599; P:hemostasis; TAS:UniProtKB.
DR GO; GO:0046907; P:intracellular transport; IC:ComplexPortal.
DR GO; GO:0007040; P:lysosome organization; IDA:UniProtKB.
DR GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
DR GO; GO:1903232; P:melanosome assembly; IDA:UniProtKB.
DR GO; GO:0060155; P:platelet dense granule organization; IC:ComplexPortal.
DR GO; GO:0048075; P:positive regulation of eye pigmentation; TAS:UniProtKB.
DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL.
DR GO; GO:0050821; P:protein stabilization; IPI:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR InterPro; IPR043987; CCZ1/INTU/HSP4_longin_1.
DR InterPro; IPR043989; CCZ1/INTU/HSP4_longin_3.
DR InterPro; IPR026091; HPS4.
DR PANTHER; PTHR14407; PTHR14407; 1.
DR Pfam; PF19031; Intu_longin_1; 1.
DR Pfam; PF19033; Intu_longin_3; 1.
PE 1: Evidence at protein level;
KW Albinism; Alternative splicing; Guanine-nucleotide releasing factor;
KW Hermansky-Pudlak syndrome; Phosphoprotein; Reference proteome.
FT CHAIN 1..708
FT /note="BLOC-3 complex member HPS4"
FT /id="PRO_0000084052"
FT REGION 269..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..14
FT /note="MATSTSTEAKSASW -> MAPLCSLAR (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:12529303,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017082"
FT VAR_SEQ 236
FT /note="G -> GKWMLWSFKNRVTHQNPNG (in isoform 2 and isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_003880"
FT VAR_SEQ 463..510
FT /note="RRTRRPLLLPRLDPGQRGNKLPTGEQGLDEDVDGVCESHAAPGLECSS ->
FT KSTVLFSGGCVKGSDTQLCVPGLVWYLEPQFYYVIVRHFFDSMRQTAG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003881"
FT VAR_SEQ 511..708
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003882"
FT VARIANT 229
FT /note="E -> G (in dbSNP:rs713998)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_025006"
FT VARIANT 443
FT /note="L -> V (in dbSNP:rs2014410)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_024158"
FT VARIANT 552
FT /note="V -> M (in dbSNP:rs5752330)"
FT /evidence="ECO:0000269|PubMed:11258795,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_025007"
FT VARIANT 606
FT /note="H -> Y (in dbSNP:rs1894706)"
FT /evidence="ECO:0000269|PubMed:11258795,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_024159"
FT VARIANT 625
FT /note="Q -> H (in dbSNP:rs1894704)"
FT /evidence="ECO:0000269|PubMed:11258795,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_021836"
FT CONFLICT 168
FT /note="V -> A (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="A -> V (in Ref. 3; BAB71540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 708 AA; 76919 MW; E47BCF49FC78830A CRC64;
MATSTSTEAK SASWWNYFFL YDGSKVKEEG DPTRAGICYF YPSQTLLDQQ ELLCGQIAGV
VRCVSDISDS PPTLVRLRKL KFAIKVDGDY LWVLGCAVEL PDVSCKRFLD QLVGFFNFYN
GPVSLAYENC SQEELSTEWD TFIEQILKNT SDLHKIFNSL WNLDQTKVEP LLLLKAARIL
QTCQRSPHIL AGCILYKGLI VSTQLPPSLT AKVLLHRTAP QEQRLPTGED APQEHGAALP
PNVQIIPVFV TKEEAISLHE FPVEQMTRSL ASPAGLQDGS AQHHPKGGST SALKENATGH
VESMAWTTPD PTSPDEACPD GRKENGCLSG HDLESIRPAG LHNSARGEVL GLSSSLGKEL
VFLQEELDLS EIHIPEAQEV EMASGHFAFL HVPVPDGRAP YCKASLSASS SLEPTPPEDT
AISSLRPPSA PEMLTQHGAQ EQLEDHPGHS SQAPIPRADP LPRRTRRPLL LPRLDPGQRG
NKLPTGEQGL DEDVDGVCES HAAPGLECSS GSANCQGAGP SADGISSRLT PAESCMGLVR
MNLYTHCVKG LVLSLLAEEP LLGDSAAIEE VYHSSLASLN GLEVHLKETL PRDEAASTSS
TYNFTHYDRI QSLLMANLPQ VATPQDRRFL QAVSLMHSEF AQLPALYEMT VRNASTAVYA
CCNPIQETYF QQLAPAARSS GFPNPQDGAF SLSGKAKQKL LKHGVNLL
