VP33B_RAT
ID VP33B_RAT Reviewed; 617 AA.
AC Q63616;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Vacuolar protein sorting-associated protein 33B;
DE Short=r-vps33b;
GN Name=Vps33b;
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=8996080; DOI=10.1016/s0378-1119(96)00367-8;
RA Pevsner J., Hsu S.-C., Hyde P.S., Scheller R.H.;
RT "Mammalian homologues of yeast vacuolar protein sorting (vps) genes
RT implicated in Golgi-to-lysosome trafficking.";
RL Gene 183:7-14(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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).
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 VIPAS39. In
CC epithelial cells, the VPS33B:VIPAS39 complex may play a role in the
CC apical recycling pathway and in the maintenance of the apical-
CC basolateral polarity. 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 (By similarity). {ECO:0000250|UniProtKB:P59016,
CC ECO:0000250|UniProtKB:Q9H267}.
CC -!- SUBUNIT: Interacts with RAB11A and VIPAS39. Associates with adaptor
CC protein complex 3 (AP-3), clathrin:AP-3 and clathrin:HGS complexes (By
CC similarity). {ECO:0000250|UniProtKB:P59016,
CC ECO:0000250|UniProtKB:Q9H267}.
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 -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated on tyrosine residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR EMBL; U35245; AAC52986.1; -; mRNA.
DR EMBL; BC081707; AAH81707.1; -; mRNA.
DR PIR; JC5721; JC5721.
DR RefSeq; NP_071622.1; NM_022286.2.
DR AlphaFoldDB; Q63616; -.
DR SMR; Q63616; -.
DR BioGRID; 248968; 1.
DR STRING; 10116.ENSRNOP00000017862; -.
DR PhosphoSitePlus; Q63616; -.
DR jPOST; Q63616; -.
DR PaxDb; Q63616; -.
DR PRIDE; Q63616; -.
DR Ensembl; ENSRNOT00000017862; ENSRNOP00000017862; ENSRNOG00000013149.
DR GeneID; 64060; -.
DR KEGG; rno:64060; -.
DR UCSC; RGD:620644; rat.
DR CTD; 26276; -.
DR RGD; 620644; Vps33b.
DR eggNOG; KOG1302; Eukaryota.
DR GeneTree; ENSGT00940000156813; -.
DR HOGENOM; CLU_016678_3_1_1; -.
DR InParanoid; Q63616; -.
DR OMA; NWIGITR; -.
DR OrthoDB; 406738at2759; -.
DR PhylomeDB; Q63616; -.
DR TreeFam; TF315126; -.
DR PRO; PR:Q63616; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000013149; Expressed in thymus and 20 other tissues.
DR Genevisible; Q63616; RN.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:RGD.
DR GO; GO:0033263; C:CORVET complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031901; C:early endosome membrane; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0030897; C:HOPS complex; ISO:RGD.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
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:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0031091; C:platelet alpha granule; ISO:RGD.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IDA:SynGO.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0099023; C:vesicle tethering complex; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0032963; P:collagen metabolic process; ISO:RGD.
DR GO; GO:0007032; P:endosome organization; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
DR GO; GO:0032418; P:lysosome localization; ISO:RGD.
DR GO; GO:0035855; P:megakaryocyte development; ISO:RGD.
DR GO; GO:0032400; P:melanosome localization; ISO:RGD.
DR GO; GO:0061025; P:membrane fusion; ISO:RGD.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; ISO:RGD.
DR GO; GO:0070889; P:platelet alpha granule organization; ISO:RGD.
DR GO; GO:0015031; P:protein transport; ISO:RGD.
DR GO; GO:0090330; P:regulation of platelet aggregation; ISO:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:RGD.
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 2: Evidence at transcript 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_0000206307"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H267"
SQ SEQUENCE 617 AA; 70693 MW; 2DCE0FC2E21B840B CRC64;
MAFPHRLDAP ELPDFSMLKR LARDQLIYLL EQLPGKKDLF IEADLMSPLD RIANVSILKQ
HEVDKLYKVE NKLTLSSNEQ LCFLVRPRIK TMRYIANLVN ADKLAGRVRK YKIILSPQKF
YACEMVLEEE GVYGDVSCDE WAFSLLPLDV DLLSMELPEF FRDYFLEGDQ RWINTVAQAL
HLLSTLYGPF PNCYGIGRCT KMSYDLWRKL EEEEDSETKG RRPEIGHIFL LDRDVDFVTA
LCSQVVYEGL VDDTFRIKCG SVDFGPEVTS SDKSLKVLLN AEDKVFSEIR NEHFSNVFGF
LSQKARNLQA QYDRRRGMDI KQMKNFVSQE LKGLKQEHRL LSLHIGACES IMKKKTKQDF
QELIKTEHAL LEGFNIREST SYIEEHIDRQ VSPIESLRLM CLLSITENGL IPKDYRSLKT
QYLQSYGPEH LLTFSNLRRA GLLTEQASGD TLTAVENKVS KLVTDKAAGK ITDAFSSLAK
RSNFRAISKK LNLIPRVDGE YDLKVPRDMA YVFSGAYVPL SCRIIEQVLD RRSWQGLDEV
VRLLNCSDFA FTDMAKEDKA SSESLRLILV VFLGGCTFSE ISALRFLGRE KGYRFIFLTT
AVTNSARLME AMSEVKS
