VP33B_BOVIN
ID VP33B_BOVIN Reviewed; 617 AA.
AC Q2HJ18; A1L527;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Vacuolar protein sorting-associated protein 33B;
GN Name=VPS33B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:Q9H267}.
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; BT029814; ABM06080.1; -; mRNA.
DR EMBL; BC113354; AAI13355.1; -; mRNA.
DR RefSeq; NP_001039749.1; NM_001046284.1.
DR AlphaFoldDB; Q2HJ18; -.
DR SMR; Q2HJ18; -.
DR STRING; 9913.ENSBTAP00000000029; -.
DR PaxDb; Q2HJ18; -.
DR PRIDE; Q2HJ18; -.
DR Ensembl; ENSBTAT00000000029; ENSBTAP00000000029; ENSBTAG00000000026.
DR GeneID; 526538; -.
DR KEGG; bta:526538; -.
DR CTD; 26276; -.
DR VEuPathDB; HostDB:ENSBTAG00000000026; -.
DR VGNC; VGNC:36817; VPS33B.
DR eggNOG; KOG1302; Eukaryota.
DR GeneTree; ENSGT00940000156813; -.
DR HOGENOM; CLU_016678_3_1_1; -.
DR InParanoid; Q2HJ18; -.
DR OMA; NWIGITR; -.
DR OrthoDB; 406738at2759; -.
DR TreeFam; TF315126; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000000026; Expressed in mesenteric lymph node and 105 other tissues.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0033263; C:CORVET complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0030897; C:HOPS complex; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISS: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; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0031091; C:platelet alpha granule; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl.
DR GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR GO; GO:0032400; P:melanosome localization; ISS:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; ISS:UniProtKB.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; IEA:Ensembl.
DR GO; GO:0070889; P:platelet alpha granule organization; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0090330; P:regulation of platelet aggregation; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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_0000244379"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H267"
SQ SEQUENCE 617 AA; 70659 MW; C19A5C5326A9DDF1 CRC64;
MAFPHRPDAP ELPDFSMLKR LARDQLIYLL EQLPGKKDLF IEADLMSPLD RIANVSILKQ
HEVDKLYKVE NKPALSSSEQ LCFLVRPRIK NMRYIASLVN ADKMAGRTRK YKVIFSPQKF
YACEMVLEEE GVYGDVSCDE WAFSLLPLDV DLLSMELPEF FRDYFLEGDQ RWINTLAQAL
HLLSTLYGPF PNCYGIGRCA KMSYELWKRL EEEEDGETKG RRPEIGHIFL LDRDVDFVTA
LCSQVVYEGL VDDTFRIKCG SVDFGPEVTS SDKSLKVLLN AEDKVFNEIR NEHFSNVFGF
LSQKARNLQA QYDRRRGMDI KQMKNFVSQE LKGLKQEHRL LSLHIGACES IMKKKTKQDF
QELIKTEHAL LEGFNIREST NYIEEHIDRQ VSPIESLRLM CLLSITENGL IPKDYRSLKT
QYLQSYGPEH LLTFFNLRRA GLLTEQAPGD TLTAVESKVS KLVTDKAAGK ITDAFSSLAK
RSNFRAISKK LNLIPRVDGE YDLKVPRDMA YVFSGAYVPL SCRIIEQVLE RRGWQGLDEV
VRLLNCSELA FTDMTKDDKA SSESLRLILV VFLGGCTFSE ISALRFLGRE KGYRFIFLTT
AVTNSARLME AMSEVKA
