VP33B_HUMAN
ID VP33B_HUMAN Reviewed; 617 AA.
AC Q9H267; B3KQF6; Q96K14; Q9NRP6; Q9NSF3;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Vacuolar protein sorting-associated protein 33B;
DE Short=hVPS33B;
GN Name=VPS33B;
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 VARIANT SER-514.
RX PubMed=10894945; DOI=10.1159/000015571;
RA Carim-Todd L., Sumoy L., Andreu N., Estivill X., Escarceller M.;
RT "Cloning, mapping and expression analysis of VPS33B, the human orthologue
RT of rat Vps33b.";
RL Cytogenet. Cell Genet. 89:92-95(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11250079; DOI=10.1016/s0378-1119(01)00333-x;
RA Huizing M., Didier A., Walenta J., Anikster Y., Gahl W.A., Kraemer H.;
RT "Molecular cloning and characterization of human VPS18, VPS11, VPS16, and
RT VPS33.";
RL Gene 264:241-247(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-514.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 1), AND VARIANT SER-514.
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 [7]
RP FUNCTION, DEPHOSPHORYLATION, PHOSPHORYLATION, INTERACTION WITH
RP MYCOBACTERIUM TUBERCULOSIS PTPA (MICROBIAL INFECTION), MUTAGENESIS OF
RP TYR-133; TYR-382; TYR-511 AND TYR-517, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18474358; DOI=10.1016/j.chom.2008.03.008;
RA Bach H., Papavinasasundaram K.G., Wong D., Hmama Z., Av-Gay Y.;
RT "Mycobacterium tuberculosis virulence is mediated by PtpA dephosphorylation
RT of human vacuolar protein sorting 33B.";
RL Cell Host Microbe 3:316-322(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=19109425; DOI=10.1091/mbc.e08-07-0728;
RA Zhu G.D., Salazar G., Zlatic S.A., Fiza B., Doucette M.M., Heilman C.J.,
RA Levey A.I., Faundez V., L'hernault S.W.;
RT "SPE-39 family proteins interact with the HOPS complex and function in
RT lysosomal delivery.";
RL Mol. Biol. Cell 20:1223-1240(2009).
RN [10]
RP FUNCTION, INTERACTION WITH RAB11A AND VIPAS39, CHARACTERIZATION OF VARIANT
RP ARCS1 PRO-30, AND SUBCELLULAR LOCATION.
RX PubMed=20190753; DOI=10.1038/ng.538;
RA Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y.,
RA Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B.,
RA Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H., Matthews R.P.,
RA Thomas S.G., Rappoport J.Z., Arias I.M., Wolburg H., Knisely A.S.,
RA Kelly D.A., Muller F., Maher E.R., Gissen P.;
RT "Mutations in VIPAR cause an arthrogryposis, renal dysfunction and
RT cholestasis syndrome phenotype with defects in epithelial polarization.";
RL Nat. Genet. 42:303-312(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=21411634; DOI=10.1091/mbc.e10-10-0799;
RA Zlatic S.A., Tornieri K., L'Hernault S.W., Faundez V.;
RT "Clathrin-dependent mechanisms modulate the subcellular distribution of
RT class C Vps/HOPS tether subunits in polarized and nonpolarized cells.";
RL Mol. Biol. Cell 22:1699-1715(2011).
RN [13]
RP SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT ARCS1 PRO-30.
RX PubMed=22753090; DOI=10.1002/humu.22155;
RA Smith H., Galmes R., Gogolina E., Straatman-Iwanowska A., Reay K.,
RA Banushi B., Bruce C.K., Cullinane A.R., Romero R., Chang R., Ackermann O.,
RA Baumann C., Cangul H., Cakmak Celik F., Aygun C., Coward R.,
RA Dionisi-Vici C., Sibbles B., Inward C., Kim C.A., Klumperman J.,
RA Knisely A.S., Watson S.P., Gissen P.;
RT "Associations among genotype, clinical phenotype, and intracellular
RT localization of trafficking proteins in ARC syndrome.";
RL Hum. Mutat. 33:1656-1664(2012).
RN [14]
RP FUNCTION, CHARACTERIZATION OF VARIANTS ARCS1 PRO-30 AND PHE-243,
RP MUTAGENESIS OF 232-ASP--ASP-234; ASP-234; 235-VAL--PHE-237; GLY-249;
RP 251-VAL--ASP-253 AND ASP-252, AND INTERACTION WITH VIPAS39; STX7; VPS18 AND
RP VPS41.
RX PubMed=23918659; DOI=10.1093/hmg/ddt378;
RA Tornieri K., Zlatic S.A., Mullin A.P., Werner E., Harrison R.,
RA L'hernault S.W., Faundez V.;
RT "Vps33b pathogenic mutations preferentially affect VIPAS39/SPE-39-positive
RT endosomes.";
RL Hum. Mol. Genet. 22:5215-5228(2013).
RN [15]
RP INTERACTION WITH VIPAS39.
RX PubMed=23901104; DOI=10.1073/pnas.1307074110;
RA Graham S.C., Wartosch L., Gray S.R., Scourfield E.J., Deane J.E.,
RA Luzio J.P., Owen D.J.;
RT "Structural basis of Vps33A recruitment to the human HOPS complex by
RT Vps16.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:13345-13350(2013).
RN [16]
RP VARIANT ARCS1 PRO-30, AND SUBCELLULAR LOCATION.
RX PubMed=15052268; DOI=10.1038/ng1325;
RA Gissen P., Johnson C.A., Morgan N.V., Stapelbroek J.M., Forshew T.,
RA Cooper W.N., McKiernan P.J., Klomp L.W.J., Morris A.A.M., Wraith J.E.,
RA McClean P., Lynch S.A., Thompson R.J., Lo B., Quarrell O.W., Di Rocco M.,
RA Trembath R.C., Mandel H., Wali S., Karet F.E., Knisely A.S., Houwen R.H.J.,
RA Kelly D.A., Maher E.R.;
RT "Mutations in VPS33B, encoding a regulator of SNARE-dependent membrane
RT fusion, cause arthrogryposis-renal dysfunction-cholestasis (ARC)
RT syndrome.";
RL Nat. Genet. 36:400-404(2004).
RN [17]
RP VARIANT ARCS1 PHE-243.
RX PubMed=18853461; DOI=10.1002/humu.20900;
RA Cullinane A.R., Straatman-Iwanowska A., Seo J.K., Ko J.S., Song K.S.,
RA Gizewska M., Gruszfeld D., Gliwicz D., Tuysuz B., Erdemir G., Sougrat R.,
RA Wakabayashi Y., Hinds R., Barnicoat A., Mandel H., Chitayat D.,
RA Fischler B., Garcia-Cazorla A., Knisely A.S., Kelly D.A., Maher E.R.,
RA Gissen P.;
RT "Molecular investigations to improve diagnostic accuracy in patients with
RT ARC syndrome.";
RL Hum. Mutat. 30:E330-E337(2009).
CC -!- FUNCTION: May play a role in vesicle-mediated protein trafficking to
CC lysosomal compartments and in membrane docking/fusion reactions of late
CC endosomes/lysosomes. Mediates phagolysosomal fusion in macrophages
CC (PubMed:18474358). Proposed to be involved in endosomal maturation
CC implicating VIPAS39. In epithelial cells, the VPS33B:VIPAS39 complex
CC may play a role in the apical recycling pathway and in the maintenance
CC of the apical-basolateral polarity (PubMed:20190753). Seems to be
CC involved in the sorting of specific cargos from the trans-Golgi network
CC to alpha-granule-destined multivesicular bodies (MVBs) promoting MVBs
CC maturation in megakaryocytes (By similarity).
CC {ECO:0000250|UniProtKB:P59016, ECO:0000269|PubMed:18474358,
CC ECO:0000305|PubMed:20190753, ECO:0000305|PubMed:23918659}.
CC -!- SUBUNIT: Interacts with RAB11A and VIPAS39. Associates with adaptor
CC protein complex 3 (AP-3), clathrin:AP-3 and clathrin:HGS complexes
CC (PubMed:21411634). {ECO:0000269|PubMed:20190753,
CC ECO:0000269|PubMed:21411634, ECO:0000269|PubMed:23901104}.
CC -!- SUBUNIT: (Microbial infection) Interacts with M.tuberculosis PtpA.
CC {ECO:0000269|PubMed:18474358}.
CC -!- INTERACTION:
CC Q9H267; Q6IA61: C14orf133; NbExp=3; IntAct=EBI-749072, EBI-10305835;
CC Q9H267; Q15025: TNIP1; NbExp=9; IntAct=EBI-749072, EBI-357849;
CC Q9H267; Q9H9C1: VIPAS39; NbExp=39; IntAct=EBI-749072, EBI-749080;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:15052268}; Peripheral membrane protein; Cytoplasmic
CC side. Lysosome membrane {ECO:0000269|PubMed:15052268}; Peripheral
CC membrane protein; Cytoplasmic side. Early endosome
CC {ECO:0000269|PubMed:21411634}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:21411634}. Recycling endosome
CC {ECO:0000269|PubMed:22753090}. Note=Colocalizes in clusters with
CC VIPAS39 at cytoplasmic organelles (PubMed:19109425). Colocalizes with
CC RAB11A and VIPAS39 on recycling endosomes (PubMed:22753090).
CC Colocalizes with AP-3, clathrin, Rab5 and Rab7b (PubMed:21411634).
CC Colocalizes with M.tuberculosis PtpA in the cytosol of tuberculosis-
CC infected macrophages and associates with phagosomes (PubMed:18474358).
CC {ECO:0000269|PubMed:18474358, ECO:0000269|PubMed:19109425,
CC ECO:0000269|PubMed:21411634, ECO:0000269|PubMed:22753090}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H267-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H267-2; Sequence=VSP_056567;
CC -!- TISSUE SPECIFICITY: Ubiquitous; highly expressed in testis and low
CC expression in the lung.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:18474358}.
CC -!- PTM: (Microbial infection) Dephosphorylated by M.tuberculosis PtpA,
CC which induces the reduction of host phagolysosome fusion in
CC M.tuberculosis-infected macrophages. {ECO:0000269|PubMed:18474358}.
CC -!- DISEASE: Arthrogryposis, renal dysfunction and cholestasis syndrome 1
CC (ARCS1) [MIM:208085]: A multisystem disorder, characterized by
CC neurogenic arthrogryposis multiplex congenita, renal tubular
CC dysfunction and neonatal cholestasis with bile duct hypoplasia and low
CC gamma glutamyl transpeptidase activity. Platelet dysfunction is common.
CC {ECO:0000269|PubMed:15052268, ECO:0000269|PubMed:18853461,
CC ECO:0000269|PubMed:20190753, ECO:0000269|PubMed:22753090,
CC ECO:0000269|PubMed:23918659}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
CC -!- CAUTION: According to PubMed:18474358, it is autophosphorylated.
CC However, it is not related with protein kinases, suggesting it is
CC phosphorylated by another protein. {ECO:0000305}.
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DR EMBL; AF201694; AAF91174.1; -; mRNA.
DR EMBL; AL357472; CAB93109.1; -; mRNA.
DR EMBL; AF308803; AAG34680.1; -; mRNA.
DR EMBL; AK027754; BAB55345.1; -; mRNA.
DR EMBL; AK074863; BAG52018.1; -; mRNA.
DR EMBL; AC068831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471101; EAX02140.1; -; Genomic_DNA.
DR EMBL; BC016445; AAH16445.1; -; mRNA.
DR CCDS; CCDS10369.1; -. [Q9H267-1]
DR RefSeq; NP_001276077.1; NM_001289148.1.
DR RefSeq; NP_001276078.1; NM_001289149.1. [Q9H267-2]
DR RefSeq; NP_061138.3; NM_018668.4. [Q9H267-1]
DR RefSeq; XP_005254944.1; XM_005254887.1. [Q9H267-2]
DR RefSeq; XP_011519750.1; XM_011521448.1. [Q9H267-2]
DR AlphaFoldDB; Q9H267; -.
DR SMR; Q9H267; -.
DR BioGRID; 117659; 187.
DR ComplexPortal; CPX-6241; CHEVI tethering complex.
DR CORUM; Q9H267; -.
DR IntAct; Q9H267; 26.
DR MINT; Q9H267; -.
DR STRING; 9606.ENSP00000327650; -.
DR iPTMnet; Q9H267; -.
DR MetOSite; Q9H267; -.
DR PhosphoSitePlus; Q9H267; -.
DR BioMuta; VPS33B; -.
DR DMDM; 313104046; -.
DR EPD; Q9H267; -.
DR jPOST; Q9H267; -.
DR MassIVE; Q9H267; -.
DR MaxQB; Q9H267; -.
DR PaxDb; Q9H267; -.
DR PeptideAtlas; Q9H267; -.
DR PRIDE; Q9H267; -.
DR ProteomicsDB; 3557; -.
DR ProteomicsDB; 80506; -. [Q9H267-1]
DR Antibodypedia; 28996; 113 antibodies from 22 providers.
DR DNASU; 26276; -.
DR Ensembl; ENST00000333371.8; ENSP00000327650.4; ENSG00000184056.15. [Q9H267-1]
DR GeneID; 26276; -.
DR KEGG; hsa:26276; -.
DR MANE-Select; ENST00000333371.8; ENSP00000327650.4; NM_018668.5; NP_061138.3.
DR UCSC; uc002bqp.3; human. [Q9H267-1]
DR CTD; 26276; -.
DR DisGeNET; 26276; -.
DR GeneCards; VPS33B; -.
DR HGNC; HGNC:12712; VPS33B.
DR HPA; ENSG00000184056; Low tissue specificity.
DR MalaCards; VPS33B; -.
DR MIM; 208085; phenotype.
DR MIM; 608552; gene.
DR neXtProt; NX_Q9H267; -.
DR OpenTargets; ENSG00000184056; -.
DR Orphanet; 2697; Arthrogryposis-renal dysfunction-cholestasis syndrome.
DR PharmGKB; PA37327; -.
DR VEuPathDB; HostDB:ENSG00000184056; -.
DR eggNOG; KOG1302; Eukaryota.
DR GeneTree; ENSGT00940000156813; -.
DR HOGENOM; CLU_016678_3_1_1; -.
DR InParanoid; Q9H267; -.
DR OMA; NWIGITR; -.
DR PhylomeDB; Q9H267; -.
DR TreeFam; TF315126; -.
DR PathwayCommons; Q9H267; -.
DR Reactome; R-HSA-9636383; Prevention of phagosomal-lysosomal fusion.
DR Reactome; R-HSA-9754560; SARS-CoV-2 modulates autophagy.
DR SignaLink; Q9H267; -.
DR SIGNOR; Q9H267; -.
DR BioGRID-ORCS; 26276; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; VPS33B; human.
DR GeneWiki; VPS33B; -.
DR GenomeRNAi; 26276; -.
DR Pharos; Q9H267; Tbio.
DR PRO; PR:Q9H267; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9H267; protein.
DR Bgee; ENSG00000184056; Expressed in pancreatic ductal cell and 190 other tissues.
DR ExpressionAtlas; Q9H267; baseline and differential.
DR Genevisible; Q9H267; HS.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0033263; C:CORVET complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0030897; C:HOPS complex; IDA:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0099023; C:vesicle tethering complex; IPI:ComplexPortal.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:GO_Central.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0046907; P:intracellular transport; IC:ComplexPortal.
DR GO; GO:0032418; P:lysosome localization; IDA:UniProtKB.
DR GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR GO; GO:0032400; P:melanosome localization; IDA:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; IMP:UniProtKB.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; IMP:MGI.
DR GO; GO:0090385; P:phagosome-lysosome fusion; IC:ComplexPortal.
DR GO; GO:0070889; P:platelet alpha granule organization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IMP:UniProtKB.
DR GO; GO:0090330; P:regulation of platelet aggregation; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:MGI.
DR Gene3D; 1.25.40.850; -; 1.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.830.10; -; 1.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR InterPro; IPR027121; VPS33.
DR InterPro; IPR043155; VPS33_dom3b.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR PANTHER; PTHR11679:SF77; PTHR11679:SF77; 1.
DR Pfam; PF00995; Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasmic vesicle; Disease variant;
KW Endosome; Lysosome; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..617
FT /note="Vacuolar protein sorting-associated protein 33B"
FT /id="PRO_0000206305"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056567"
FT VARIANT 30
FT /note="L -> P (in ARCS1; effect on interaction with VIPAS39
FT is reported conflictingly but disrupts colocalization with
FT VIPAS39 at cytoplasmic organelle; impairs localization to
FT VIPAS39-containing endosomal compartment; and induces
FT fragmentation of the VIPAS39-containing endosomal
FT compartment; no effect on interaction with STX7 and
FT association with the HOPS complex; dbSNP:rs121434385)"
FT /evidence="ECO:0000269|PubMed:15052268,
FT ECO:0000269|PubMed:20190753, ECO:0000269|PubMed:22753090,
FT ECO:0000269|PubMed:23918659"
FT /id="VAR_018983"
FT VARIANT 243
FT /note="S -> F (in ARCS1; no effect on interaction with
FT VIPAS39; impairs localization to VIPAS39-containing
FT endosomal compartment; dbSNP:rs139829189)"
FT /evidence="ECO:0000269|PubMed:18853461,
FT ECO:0000269|PubMed:23918659"
FT /id="VAR_057901"
FT VARIANT 513
FT /note="F -> S (in dbSNP:rs3177428)"
FT /id="VAR_057330"
FT VARIANT 514
FT /note="G -> S (in dbSNP:rs11073964)"
FT /evidence="ECO:0000269|PubMed:10894945,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_013828"
FT MUTAGEN 133
FT /note="Y->E: Reduces phosphorylation activity, but does not
FT impair phagolysosomal fusion in M.tuberculosis-infected
FT macrophages; when associated with E-382; E-511 and E-517."
FT /evidence="ECO:0000269|PubMed:18474358"
FT MUTAGEN 232..234
FT /note="DRD->AAA: Disrupts interaction with VIPAS39."
FT /evidence="ECO:0000269|PubMed:23918659"
FT MUTAGEN 234
FT /note="D->H: No effect on interaction with VIPAS39; no
FT effect on interaction with STX7 and association with the
FT HOPS complex; impairs localization to VIPAS39-containing
FT endosomal compartment."
FT /evidence="ECO:0000269|PubMed:23918659"
FT MUTAGEN 235..237
FT /note="VDF->AAA: Disrupts interaction with VIPAS39."
FT /evidence="ECO:0000269|PubMed:23918659"
FT MUTAGEN 249
FT /note="G->V: Disrupts interaction with VIPAS39; no effect
FT on interaction with STX7; impairs localization to VIPAS39-
FT containing endosomal compartment."
FT /evidence="ECO:0000269|PubMed:23918659"
FT MUTAGEN 251..253
FT /note="VDD->AAA: Disrupts interaction with VIPAS39."
FT /evidence="ECO:0000269|PubMed:23918659"
FT MUTAGEN 252
FT /note="D->E: No effect on interaction with VIPAS39 and
FT STX7; impairs localization to VIPAS39-containing endosomal
FT compartment."
FT /evidence="ECO:0000269|PubMed:23918659"
FT MUTAGEN 382
FT /note="Y->E: Reduces phosphorylation activity, but does not
FT impair phagolysosomal fusion in M.tuberculosis-infected
FT macrophages; when associated with E-133; E-511 and E-517."
FT /evidence="ECO:0000269|PubMed:18474358"
FT MUTAGEN 511
FT /note="Y->E: Reduces phosphorylation activity, but does not
FT impair phagolysosomal fusion in M.tuberculosis-infected
FT macrophages; when associated with E-133; E-382 and E-517."
FT /evidence="ECO:0000269|PubMed:18474358"
FT MUTAGEN 517
FT /note="Y->E: Reduces phosphorylation activity, but does not
FT impair phagolysosomal fusion in M.tuberculosis-infected
FT macrophages; when associated with E-133; E-382 and E-511."
FT /evidence="ECO:0000269|PubMed:18474358"
FT CONFLICT 293
FT /note="H -> Y (in Ref. 3; BAB55345)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="K -> E (in Ref. 3; BAB55345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 70585 MW; BD7DB97E1FEB1D32 CRC64;
MAFPHRPDAP ELPDFSMLKR LARDQLIYLL EQLPGKKDLF IEADLMSPLD RIANVSILKQ
HEVDKLYKVE NKPALSSNEQ LCFLVRPRIK NMRYIASLVN ADKLAGRTRK YKVIFSPQKF
YACEMVLEEE GIYGDVSCDE WAFSLLPLDV DLLSMELPEF FRDYFLEGDQ RWINTVAQAL
HLLSTLYGPF PNCYGIGRCA KMAYELWRNL EEEEDGETKG RRPEIGHIFL LDRDVDFVTA
LCSQVVYEGL VDDTFRIKCG SVDFGPEVTS SDKSLKVLLN AEDKVFNEIR NEHFSNVFGF
LSQKARNLQA QYDRRRGMDI KQMKNFVSQE LKGLKQEHRL LSLHIGACES IMKKKTKQDF
QELIKTEHAL LEGFNIREST SYIEEHIDRQ VSPIESLRLM CLLSITENGL IPKDYRSLKT
QYLQSYGPEH LLTFSNLRRA GLLTEQAPGD TLTAVESKVS KLVTDKAAGK ITDAFSSLAK
RSNFRAISKK LNLIPRVDGE YDLKVPRDMA YVFGGAYVPL SCRIIEQVLE RRSWQGLDEV
VRLLNCSDFA FTDMTKEDKA SSESLRLILV VFLGGCTFSE ISALRFLGRE KGYRFIFLTT
AVTNSARLME AMSEVKA
