VP33B_CAEEL
ID VP33B_CAEEL Reviewed; 617 AA.
AC Q18891;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Vacuolar protein sorting-associated protein 33B {ECO:0000305};
GN Name=vps-33.2 {ECO:0000312|WormBase:C56C10.1};
GN ORFNames=C56C10.1 {ECO:0000312|WormBase:C56C10.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH SPE-39.
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 [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25273556; DOI=10.1091/mbc.e13-12-0710;
RA Solinger J.A., Spang A.;
RT "Loss of the Sec1/Munc18-family proteins VPS-33.2 and VPS-33.1 bypasses a
RT block in endosome maturation in Caenorhabditis elegans.";
RL Mol. Biol. Cell 25:3909-3925(2014).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27558849; DOI=10.1111/tra.12430;
RA Gengyo-Ando K., Kage-Nakadai E., Yoshina S., Otori M., Kagawa-Nagamura Y.,
RA Nakai J., Mitani S.;
RT "Distinct roles of the two VPS33 proteins in the endolysosomal system in
RT Caenorhabditis elegans.";
RL Traffic 17:1197-1213(2016).
CC -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking to
CC lysosomal compartments and in membrane docking/fusion reactions of late
CC endosomes/lysosomes (PubMed:25273556). Believed to act as a component
CC of the putative CORVET endosomal tethering complex which is proposed to
CC be involved in the rab-5-to-rab-7 endosome conversion probably
CC implicating sand-1, and via binding SNAREs and SNARE complexes to
CC mediate tethering and docking events during SNARE-mediated membrane
CC fusion (PubMed:25273556). The CORVET complex is proposed to function as
CC a rab-5 effector to mediate early endosome fusion probably in specific
CC endosome subpopulations (PubMed:25273556). Most likely within the
CC CORVET complex, it is involved in the fusion of endocytic compartments
CC (PubMed:25273556). Required for sperm development and function
CC (PubMed:19109425, PubMed:27558849). {ECO:0000269|PubMed:19109425,
CC ECO:0000269|PubMed:25273556, ECO:0000269|PubMed:27558849}.
CC -!- SUBUNIT: Probable core component of the class C core vacuole/endosome
CC tethering (CORVET) complex. The common core is composed of the class C
CC Vps proteins vps-11, vps-16 and vps-18, and which further associates
CC with vps-8 and vps-33.2 (PubMed:25273556). Interacts with spe-39
CC (PubMed:19109425). {ECO:0000269|PubMed:19109425,
CC ECO:0000305|PubMed:25273556}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:25273556,
CC ECO:0000269|PubMed:27558849}. Late endosome membrane
CC {ECO:0000269|PubMed:27558849}; 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}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:Q9H267}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q9H267}.
CC -!- TISSUE SPECIFICITY: Broadly expressed in somatic tissues including the
CC pharynx, intestine, spermatheca, and in coelomocytes (PubMed:27558849).
CC Expressed in the lining of the gut lumen (PubMed:25273556).
CC {ECO:0000269|PubMed:25273556, ECO:0000269|PubMed:27558849}.
CC -!- DISRUPTION PHENOTYPE: Hermaphrodites exhibit sperm-specific sterility
CC and only lay unfertilized eggs (PubMed:27558849). In contrast to wild-
CC type animals, mutant males produce no or few spermatids in their
CC gonads, but instead their gonads accumulate terminally arrested
CC spermatocytes that do not bud and contain four haploid nuclei
CC (PubMed:27558849). In some instances, the spermatocytes have small buds
CC that do not form spermatids (PubMed:27558849). Oocytes and unfertilized
CC eggs contain some larger endocytic structures tethered to yolk granules
CC (PubMed:27558849). RNAi-mediated knockdown results in defective yolk
CC uptake in oocytes with the appearance of endocytic structures
CC containing yolk tethered to large membranous organelles which could be
CC lysosomes (PubMed:25273556). RNAi-mediated knockdown results in
CC defective endosome maturation with the accumulation of small vesicles
CC near the gut lumen which is possibly indicative of increased endosomal
CC fusion activity, and defective trafficking of proteins such as lmp-1 to
CC lysosomal compartments (PubMed:25273556). RNAi-mediated knockdown in a
CC sand-1 mutant background results in defective endosome fusion with the
CC formation of larger, irregularly-shaped rab-5 positive endosomes in
CC oocytes and intestinal cells, and larger yolk-containing granules than
CC in the sand-1 single mutant (PubMed:25273556). Double RNAi-mediated
CC knockdown together with vsp-33.1 results in defective protein
CC trafficking to lysosomal compartments, and an irregular distribution of
CC vesicles of various sizes throughout the gut cells (PubMed:25273556).
CC Double RNAi-mediated knockdown together with vsp-33.1 in a sand-1
CC mutant background rescues the large endosome phenotype and the
CC defective protein trafficking to lysosomal compartments in the sand-1
CC single mutant, but results in lethality (PubMed:25273556).
CC {ECO:0000269|PubMed:25273556, ECO:0000269|PubMed:27558849}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR EMBL; BX284602; CCD68172.1; -; Genomic_DNA.
DR PIR; T15853; T15853.
DR RefSeq; NP_495342.2; NM_062941.5.
DR AlphaFoldDB; Q18891; -.
DR SMR; Q18891; -.
DR ComplexPortal; CPX-1137; CORVET complex.
DR DIP; DIP-25718N; -.
DR IntAct; Q18891; 2.
DR STRING; 6239.C56C10.1; -.
DR EPD; Q18891; -.
DR PaxDb; Q18891; -.
DR PeptideAtlas; Q18891; -.
DR EnsemblMetazoa; C56C10.1.1; C56C10.1.1; WBGene00016960.
DR GeneID; 174095; -.
DR KEGG; cel:CELE_C56C10.1; -.
DR UCSC; C56C10.1; c. elegans.
DR CTD; 174095; -.
DR WormBase; C56C10.1; CE30636; WBGene00016960; vps-33.2.
DR eggNOG; KOG1302; Eukaryota.
DR GeneTree; ENSGT00940000156813; -.
DR HOGENOM; CLU_016678_3_0_1; -.
DR InParanoid; Q18891; -.
DR OMA; NWIGITR; -.
DR OrthoDB; 406738at2759; -.
DR PhylomeDB; Q18891; -.
DR PRO; PR:Q18891; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016960; Expressed in germ line (C elegans) and 4 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:0031901; C:early endosome membrane; IC:ComplexPortal.
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; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IC:ComplexPortal.
DR GO; GO:0048137; P:spermatocyte division; IMP:UniProtKB.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.25.40.850; -; 1.
DR Gene3D; 3.40.50.1910; -; 2.
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 Cytoplasmic vesicle; Differentiation; Endosome; Lysosome; Membrane;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..617
FT /note="Vacuolar protein sorting-associated protein 33B"
FT /evidence="ECO:0000305"
FT /id="PRO_0000441275"
SQ SEQUENCE 617 AA; 71592 MW; 43F189C051F363D8 CRC64;
MAPGTAELEI DETLHLLRMV MQREFIHYLE TLPGTKELFI DKCLLRPLDM IATSSDMKRH
GVKRIMHFDL QKSPQVWNIE IDQRVFFLRP NVENARKIVE YVEESSENRS ICVIWCNRQL
EECDLAFESS GVIGHITQLS LNMCLLPLES DLFSLQHVES AQPDLFSVAN MFVALQNLYG
VIPTVYGLGS ESKNLWNLVH ALCSSNELRA RPDQPISHLF LFDRQLDPVP VLLTGASYEG
LLHEFFTIDC GKLAFPVDLR KQVQTGPLDF DWIEINPEED KEAHQQNRGD TVKLDNCEDI
FASIRNKHVT AALEFLHSKA KSIQKSIEKS SMIDDVADYR NFVEKDLRAL KKDHKHCELH
INACEMMMNK VKMEDYRTMF KLEHEMLLGT VTHEEYFDFV FERVPMRSCR DVVLSMMSLA
SLKLDGVPDD TYNEFVEMYL QKYGYEHMFE LQNLRNSRVI YARRHIAHDR TISERARTWE
TLARKFRIVK GNEPMDMSNP SDMSYVFGAR ISPLLCKIVE DTIDHGWNQA EYERIIGKDK
VLVEENTYIA ADRRPDNRTR KAIMVFVNGG ITYWEVAALR LLAIQKNFRI LICTTHVIKK
REYLEVRAKD ASSVFGS
