VP33B_MOUSE
ID VP33B_MOUSE Reviewed; 617 AA.
AC P59016;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Vacuolar protein sorting-associated protein 33B;
GN Name=Vps33b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Mammary gland;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, INTERACTION WITH RAB11A, AND KNOCKDOWN.
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 [4]
RP SUBUNIT.
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25947942; DOI=10.1182/blood-2014-12-614677;
RA Bem D., Smith H., Banushi B., Burden J.J., White I.J., Hanley J.,
RA Jeremiah N., Rieux-Laucat F., Bettels R., Ariceta G., Mumford A.D.,
RA Thomas S.G., Watson S.P., Gissen P.;
RT "VPS33B regulates protein sorting into and maturation of alpha-granule
RT progenitor organelles in mouse megakaryocytes.";
RL Blood 126:133-143(2015).
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 Proposed to be involved in endosomal maturation implicating in part
CC VIPAS39 (By similarity). In epithelial cells, the VPS33B:VIPAS39
CC complex may play a role in the apical RAB11A-dependentrecycling pathway
CC and in the maintenance of the apical-basolateral polarity
CC (PubMed:20190753). Seems to be involved in the sorting of specific
CC cargos from the trans-Golgi network to alpha-granule-destined
CC multivesicular bodies (MVBs) promoting MVBs maturation in
CC megakaryocytes (PubMed:25947942). {ECO:0000250|UniProtKB:Q9H267,
CC ECO:0000269|PubMed:20190753, ECO:0000269|PubMed:25947942}.
CC -!- SUBUNIT: Interacts with RAB11A and VIPAS39 (PubMed:20190753).
CC Associates with adaptor protein complex 3 (AP-3), clathrin:AP-3 and
CC clathrin:HGS complexes (PubMed:21411634). {ECO:0000269|PubMed:20190753,
CC ECO:0000269|PubMed:21411634}.
CC -!- INTERACTION:
CC P59016; P62492: Rab11a; NbExp=3; IntAct=EBI-2656383, EBI-770256;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9H267}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H267}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H267}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q9H267}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H267}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H267}. Early endosome
CC {ECO:0000250|UniProtKB:Q9H267}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:Q9H267}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q9H267}. Note=Colocalizes in clusters with
CC VIPAS39 at cytoplasmic organelles. Colocalizes with RAB11A and VIPAS39
CC on recycling endosomes. Colocalizes with AP-3, clathrin, Rab5 and
CC Rab7b. {ECO:0000250|UniProtKB:Q9H267}.
CC -!- PTM: Phosphorylated on tyrosine residues. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Increased platelet account and deficiency in
CC platelet alpha-granules associated with bleeding diathesis and
CC decreases aggregate formation; reduction of mature ype-II
CC multivesicular bodies (MVB II) in megakaryocytes.
CC {ECO:0000269|PubMed:25947942}.
CC -!- MISCELLANEOUS: Vps33b-deficient inner medullary collecting duct cells
CC display abnormal expression of membrane proteins such as Ceacam5,
CC structural and functional tight junction defects and reduced E-cadherin
CC expression.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR EMBL; BC028783; AAH28783.1; -; mRNA.
DR EMBL; BC034170; AAH34170.1; -; mRNA.
DR CCDS; CCDS39997.1; -.
DR RefSeq; NP_835171.2; NM_178070.4.
DR AlphaFoldDB; P59016; -.
DR SMR; P59016; -.
DR BioGRID; 231409; 7.
DR IntAct; P59016; 1.
DR STRING; 10090.ENSMUSP00000032749; -.
DR iPTMnet; P59016; -.
DR PhosphoSitePlus; P59016; -.
DR SwissPalm; P59016; -.
DR EPD; P59016; -.
DR MaxQB; P59016; -.
DR PaxDb; P59016; -.
DR PeptideAtlas; P59016; -.
DR PRIDE; P59016; -.
DR ProteomicsDB; 297611; -.
DR DNASU; 233405; -.
DR Ensembl; ENSMUST00000032749; ENSMUSP00000032749; ENSMUSG00000030534.
DR GeneID; 233405; -.
DR KEGG; mmu:233405; -.
DR UCSC; uc009iab.1; mouse.
DR CTD; 26276; -.
DR MGI; MGI:2446237; Vps33b.
DR VEuPathDB; HostDB:ENSMUSG00000030534; -.
DR eggNOG; KOG1302; Eukaryota.
DR GeneTree; ENSGT00940000156813; -.
DR HOGENOM; CLU_016678_3_1_1; -.
DR InParanoid; P59016; -.
DR OMA; NWIGITR; -.
DR OrthoDB; 406738at2759; -.
DR PhylomeDB; P59016; -.
DR TreeFam; TF315126; -.
DR BioGRID-ORCS; 233405; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Vps33b; mouse.
DR PRO; PR:P59016; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P59016; protein.
DR Bgee; ENSMUSG00000030534; Expressed in secondary oocyte and 202 other tissues.
DR ExpressionAtlas; P59016; baseline and differential.
DR Genevisible; P59016; MM.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0033263; C:CORVET complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030897; C:HOPS complex; IEA:Ensembl.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0099023; C:vesicle tethering complex; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR GO; GO:0007032; P:endosome organization; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR GO; GO:0032418; P:lysosome localization; ISO:MGI.
DR GO; GO:0035855; P:megakaryocyte development; IMP:UniProtKB.
DR GO; GO:0032400; P:melanosome localization; ISO:MGI.
DR GO; GO:0061025; P:membrane fusion; ISO:MGI.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; IMP:MGI.
DR GO; GO:0070889; P:platelet alpha granule organization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISO:MGI.
DR GO; GO:0090330; P:regulation of platelet aggregation; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO: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; Cytoplasmic vesicle; Endosome; Lysosome; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H267"
FT CHAIN 2..617
FT /note="Vacuolar protein sorting-associated protein 33B"
FT /id="PRO_0000206306"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H267"
FT CONFLICT 275..277
FT /note="LKV -> ARG (in Ref. 1; AAH28783)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="R -> W (in Ref. 1; AAH28783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 70526 MW; B6AA803F2EAD6397 CRC64;
MAFPHRLDAP ELPDFSMLKR LARDQLIYLL EQLPGKKDLF IEADLMSPLD RIANVSILKQ
HEVDKLYKVE NKPALSANEQ LCFLVRPRIK NMRYIASLVN ADKLAGRIRK YKVILSPQKF
YACEMVLEEE GVYGDVSCDE WAFSLLPLDV DLLSMELPEF FRDYFLEGDQ RWINTVAQAL
HLLSTLYGPF PNCYGIGRCA KMSYDLWRKL EEEEDSETKG RKPEIGHIFL LDRDVDFVTA
LCSQVVYEGL VDDTFRIKCG SVDFGPEVTS SDKSLKVLLN AEDKVFSEIR NEHFSNVFGF
LSQKARNLQA QYDRRRGMDI KQMKNFVSQE LKGLKQEHRL LSLHIGACES IMKKKTKQDF
QELIKTEHAL LEGFNIREST SYIEEHIDRQ VSPIESLRLM CLLSITENGL IPKDYRSLKT
QYLQSYGPEH LLTFSNLRRA GLLTEQAPGD TLTAVESKVS KLVTDKAAGK ITDAFSSLAK
RSNFRAISKK LNLIPRVDGE YDLKVPRDMA YVFSGAYVPL SCRIIEQVLD RRSWQGLDEV
VRLLNCSEFA FTDTAKEDKA SSESLRLILV VFLGGCTFSE ISALRFLGRE KGYRFIFLTT
AVTNSARLME AMSEVKS
