HPS5_HUMAN
ID HPS5_HUMAN Reviewed; 1129 AA.
AC Q9UPZ3; A8K6J8; A8K8S1; D3DQX9; D3DQY0; O95942; Q8N4U0;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=BLOC-2 complex member HPS5 {ECO:0000305};
DE AltName: Full=Alpha-integrin-binding protein 63;
DE AltName: Full=Hermansky-Pudlak syndrome 5 protein;
DE AltName: Full=Ruby-eye protein 2 homolog;
DE Short=Ru2;
GN Name=HPS5; Synonyms=AIBP63, KIAA1017;
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] (ISOFORMS 1 AND 2), VARIANT MET-417, AND
RP DISEASE.
RC TISSUE=Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-417.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [MRNA] OF 517-1129, AND INTERACTION WITH ALPHA-INTEGRIN
RP CHAINS.
RC TISSUE=Placenta;
RX PubMed=10094488; DOI=10.1016/s0014-5793(99)00151-9;
RA Wixler V., Laplantine E., Geerts D., Sonnenberg A., Petersohn D., Eckes B.,
RA Paulsson M., Aumailley M.;
RT "Identification of novel interaction partners for the conserved membrane
RT proximal region of alpha-integrin cytoplasmic domains.";
RL FEBS Lett. 445:351-355(1999).
RN [8]
RP INTERACTION WITH HPS6 AND HPS3, AND SUBCELLULAR LOCATION.
RX PubMed=15030569; DOI=10.1111/j.1600-0854.2004.0171.x;
RA Di Pietro S.M., Falcon-Perez J.M., Dell'Angelica E.C.;
RT "Characterization of BLOC-2, a complex containing the Hermansky-Pudlak
RT syndrome proteins HPS3, HPS5 and HPS6.";
RL Traffic 5:276-283(2004).
RN [9]
RP FUNCTION.
RX PubMed=17301833; DOI=10.1038/sj.jid.5700737;
RA Helip-Wooley A., Westbroek W., Dorward H.M., Koshoffer A., Huizing M.,
RA Boissy R.E., Gahl W.A.;
RT "Improper trafficking of melanocyte-specific proteins in Hermansky-Pudlak
RT syndrome type-5.";
RL J. Invest. Dermatol. 127:1471-1478(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534 AND SER-695, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [16]
RP INTERACTION WITH HPS6.
RX PubMed=25189619; DOI=10.1242/jcs.141978;
RA Li K., Yang L., Zhang C., Niu Y., Li W., Liu J.J.;
RT "HPS6 interacts with dynactin p150Glued to mediate retrograde trafficking
RT and maturation of lysosomes.";
RL J. Cell Sci. 127:4574-4588(2014).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534, AND IDENTIFICATION BY
RP 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).
RN [18]
RP VARIANTS HPS5 ARG-624 AND ILE-1098, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15296495; DOI=10.1111/j.1600-0854.2004.00208.x;
RA Huizing M., Hess R., Dorward H., Claassen D.A., Helip-Wooley A., Kleta R.,
RA Kaiser-Kupfer M.I., White J.G., Gahl W.A.;
RT "Cellular, molecular and clinical characterization of patients with
RT Hermansky-Pudlak syndrome type 5.";
RL Traffic 5:711-722(2004).
CC -!- FUNCTION: May regulate the synthesis and function of lysosomes and of
CC highly specialized organelles, such as melanosomes and platelet dense
CC granules. Regulates intracellular vesicular trafficking in fibroblasts.
CC May be involved in the regulation of general functions of integrins.
CC {ECO:0000269|PubMed:15296495, ECO:0000269|PubMed:17301833}.
CC -!- SUBUNIT: Component of the biogenesis of lysosome-related organelles
CC complex-2 (or BLOC2) composed of HPS3, HPS5 and HPS6. Interacts with
CC HPS6 (PubMed:15030569, PubMed:25189619). Interacts with HPS3
CC (PubMed:15030569). May interact with all alpha-integrin chains that
CC have an aromatic residue before the first lysine of the conserved
CC KXGFFKR motif, including ITGA2, ITGA3, ITGA5 and ITGA6
CC (PubMed:10094488). {ECO:0000269|PubMed:10094488,
CC ECO:0000269|PubMed:15030569, ECO:0000269|PubMed:25189619}.
CC -!- INTERACTION:
CC Q9UPZ3; A0A0H3NFP4: sifA; Xeno; NbExp=2; IntAct=EBI-10962552, EBI-27055396;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15030569}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UPZ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPZ3-2; Sequence=VSP_007035;
CC -!- TISSUE SPECIFICITY: Widely expressed. Isoform 1:Highly expressed in
CC lungs and testis. Isoform 2:Highly expressed in placenta, kidney,
CC testis ovary, lung and thymus. {ECO:0000269|PubMed:15296495}.
CC -!- DISEASE: Hermansky-Pudlak syndrome 5 (HPS5) [MIM:614074]: 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:15296495}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the HPS5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76861.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF534400; AAO25962.1; -; mRNA.
DR EMBL; AF534401; AAO25963.1; -; mRNA.
DR EMBL; AF534402; AAO25964.1; -; mRNA.
DR EMBL; AB023234; BAA76861.2; ALT_INIT; mRNA.
DR EMBL; AK291663; BAF84352.1; -; mRNA.
DR EMBL; AK292436; BAF85125.1; -; mRNA.
DR EMBL; CH471064; EAW68402.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68404.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68405.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68406.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68407.1; -; Genomic_DNA.
DR EMBL; BC033640; AAH33640.1; -; mRNA.
DR EMBL; AJ131721; CAB38232.1; -; mRNA.
DR CCDS; CCDS7836.1; -. [Q9UPZ3-1]
DR CCDS; CCDS7837.1; -. [Q9UPZ3-2]
DR RefSeq; NP_009147.3; NM_007216.3. [Q9UPZ3-2]
DR RefSeq; NP_852608.1; NM_181507.1. [Q9UPZ3-1]
DR RefSeq; NP_852609.1; NM_181508.1. [Q9UPZ3-2]
DR RefSeq; XP_016872638.1; XM_017017149.1. [Q9UPZ3-1]
DR RefSeq; XP_016872639.1; XM_017017150.1. [Q9UPZ3-1]
DR RefSeq; XP_016872643.1; XM_017017154.1. [Q9UPZ3-2]
DR AlphaFoldDB; Q9UPZ3; -.
DR SMR; Q9UPZ3; -.
DR BioGRID; 116399; 48.
DR ComplexPortal; CPX-5044; BLOC-2 complex.
DR CORUM; Q9UPZ3; -.
DR IntAct; Q9UPZ3; 30.
DR MINT; Q9UPZ3; -.
DR STRING; 9606.ENSP00000265967; -.
DR GlyGen; Q9UPZ3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UPZ3; -.
DR PhosphoSitePlus; Q9UPZ3; -.
DR BioMuta; HPS5; -.
DR DMDM; 29429222; -.
DR EPD; Q9UPZ3; -.
DR jPOST; Q9UPZ3; -.
DR MassIVE; Q9UPZ3; -.
DR MaxQB; Q9UPZ3; -.
DR PaxDb; Q9UPZ3; -.
DR PeptideAtlas; Q9UPZ3; -.
DR PRIDE; Q9UPZ3; -.
DR ProteomicsDB; 85477; -. [Q9UPZ3-1]
DR ProteomicsDB; 85478; -. [Q9UPZ3-2]
DR Antibodypedia; 25002; 120 antibodies from 23 providers.
DR DNASU; 11234; -.
DR Ensembl; ENST00000349215.8; ENSP00000265967.5; ENSG00000110756.18. [Q9UPZ3-1]
DR Ensembl; ENST00000396253.7; ENSP00000379552.3; ENSG00000110756.18. [Q9UPZ3-2]
DR Ensembl; ENST00000438420.6; ENSP00000399590.2; ENSG00000110756.18. [Q9UPZ3-2]
DR Ensembl; ENST00000671838.2; ENSP00000500370.1; ENSG00000288445.2. [Q9UPZ3-1]
DR Ensembl; ENST00000672334.1; ENSP00000500042.1; ENSG00000288445.2. [Q9UPZ3-2]
DR Ensembl; ENST00000672413.1; ENSP00000499956.1; ENSG00000288445.2. [Q9UPZ3-2]
DR GeneID; 11234; -.
DR KEGG; hsa:11234; -.
DR MANE-Select; ENST00000349215.8; ENSP00000265967.5; NM_181507.2; NP_852608.1.
DR UCSC; uc001mod.2; human. [Q9UPZ3-1]
DR CTD; 11234; -.
DR DisGeNET; 11234; -.
DR GeneCards; HPS5; -.
DR GeneReviews; HPS5; -.
DR HGNC; HGNC:17022; HPS5.
DR HPA; ENSG00000110756; Tissue enhanced (liver).
DR MalaCards; HPS5; -.
DR MIM; 607521; gene.
DR MIM; 614074; phenotype.
DR neXtProt; NX_Q9UPZ3; -.
DR OpenTargets; ENSG00000110756; -.
DR Orphanet; 231512; Hermansky-Pudlak syndrome due to BLOC-2 deficiency.
DR PharmGKB; PA38432; -.
DR VEuPathDB; HostDB:ENSG00000110756; -.
DR eggNOG; KOG3621; Eukaryota.
DR GeneTree; ENSGT00940000155818; -.
DR HOGENOM; CLU_008734_0_0_1; -.
DR InParanoid; Q9UPZ3; -.
DR OMA; MCLLCYQ; -.
DR OrthoDB; 881551at2759; -.
DR PhylomeDB; Q9UPZ3; -.
DR TreeFam; TF323607; -.
DR PathwayCommons; Q9UPZ3; -.
DR SignaLink; Q9UPZ3; -.
DR SIGNOR; Q9UPZ3; -.
DR BioGRID-ORCS; 11234; 16 hits in 1083 CRISPR screens.
DR ChiTaRS; HPS5; human.
DR GeneWiki; HPS5; -.
DR GenomeRNAi; 11234; -.
DR Pharos; Q9UPZ3; Tbio.
DR PRO; PR:Q9UPZ3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9UPZ3; protein.
DR Bgee; ENSG00000110756; Expressed in sural nerve and 105 other tissues.
DR ExpressionAtlas; Q9UPZ3; baseline and differential.
DR Genevisible; Q9UPZ3; HS.
DR GO; GO:0031084; C:BLOC-2 complex; IPI:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IC:ComplexPortal.
DR GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
DR GO; GO:0048066; P:developmental pigmentation; IBA:GO_Central.
DR GO; GO:0046907; P:intracellular transport; IC:ComplexPortal.
DR GO; GO:1903232; P:melanosome assembly; IC:ComplexPortal.
DR GO; GO:0060155; P:platelet dense granule organization; IC:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR035431; HPS5.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PIRSF; PIRSF037475; BLOC-2_complex_Hps5; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Albinism; Alternative splicing; Cytoplasm; Disease variant;
KW Hermansky-Pudlak syndrome; Phosphoprotein; Reference proteome.
FT CHAIN 1..1129
FT /note="BLOC-2 complex member HPS5"
FT /id="PRO_0000084054"
FT REGION 483..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..114
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032,
FT ECO:0000303|PubMed:12548288, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007035"
FT VARIANT 417
FT /note="L -> M (in dbSNP:rs7128017)"
FT /evidence="ECO:0000269|PubMed:10231032,
FT ECO:0000269|PubMed:12548288"
FT /id="VAR_015513"
FT VARIANT 624
FT /note="L -> R (in HPS5; dbSNP:rs281865102)"
FT /evidence="ECO:0000269|PubMed:15296495"
FT /id="VAR_062285"
FT VARIANT 1098
FT /note="T -> I (in HPS5; dbSNP:rs61884288)"
FT /evidence="ECO:0000269|PubMed:15296495"
FT /id="VAR_062286"
FT CONFLICT 70
FT /note="L -> P (in Ref. 4; BAF84352)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="C -> R (in Ref. 4; BAF85125)"
FT /evidence="ECO:0000305"
FT CONFLICT 1016
FT /note="E -> K (in Ref. 4; AAH33640)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1129 AA; 127449 MW; C4FBF4EC90D1B8ED CRC64;
MAFVPVIPES YSHVLAEFES LDPLLSALRL DSSRLKCTSI AVSRKWLALG SSGGGLHLIQ
KEGWKHRLFL SHREGAISQV ACCLHDDDYV AVATSQGLVV VWELNQERRG KPEQMYVSSE
HKGRRVTALC WDTAILRVFV GDHAGKVSAI KLNTSKQAKA AAAFVMFPVQ TITTVDSCVV
QLDYLDGRLL ISSLTRSFLC DTEREKFWKI GNKERDGEYG ACFFPGRCSG GQQPLIYCAR
PGSRMWEVNF DGEVISTHQF KKLLSLPPLP VITLRSEPQY DHTAGSSQSL SFPKLLHLSE
HCVLTWTERG IYIFIPQNVQ VLLWSEVKDI QDVAVCRNEL FCLHLNGKVS HLSLISVERC
VERLLRRGLW NLAARTCCLF QNSVIASRAR KTLTADKLEH LKSQLDHGTY NDLISQLEEL
ILKFEPLDSA CSSRRSSISS HESFSILDSG IYRIISSRRG SQSDEDSCSL HSQTLSEDER
FKEFTSQQEE DLPDQCCGSH GNEDNVSHAP VMFETDKNET FLPFGIPLPF RSPSPLVSLQ
AVKESVSSFV RKTTEKIGTL HTSPDLKVRP ELRGDEQSCE EDVSSDTCPK EEDTEEEKEV
TSPPPEEDRF QELKVATAEA MTKLQDPLVL FESESLRMVL QEWLSHLEKT FAMKDFSGVS
DTDNSSMKLN QDVLLVNESK KGILDEDNEK EKRDSLGNEE SVDKTACECV RSPRESLDDL
FQICSPCAIA SGLRNDLAEL TTLCLELNVL NSKIKSTSGH VDHTLQQYSP EILACQFLKK
YFFLLNLKRA KESIKLSYSN SPSVWDTFIE GLKEMASSNP VYMEMEKGDL PTRLKLLDDE
VPFDSPLLVV YATRLYEKFG ESALRSLIKF FPSILPSDII QLCHHHPAEF LAYLDSLVKS
RPEDQRSSFL ESLLQPESLR LDWLLLAVSL DAPPSTSTMD DEGYPRPHSH LLSWGYSQLI
LHLIKLPADF ITKEKMTDIC RSCGFWPGYL ILCLELERRR EAFTNIVYLN DMSLMEGDNG
WIPETVEEWK LLLHLIQSKS TRPAPQESLN GSLSDGPSPI NVENVALLLA KAMGPDRAWS
LLQECGLALE LSEKFTRTCD ILRIAEKRQR ALIQSMLEKC DRFLWSQQA
