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VP33A_CAEEL
ID   VP33A_CAEEL             Reviewed;         603 AA.
AC   P34260;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 4.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Vacuolar protein sorting-associated protein 33A;
DE   AltName: Full=Protein slp-1;
GN   Name=vps-33.1 {ECO:0000312|WormBase:B0303.9};
GN   Synonyms=slp-1 {ECO:0000303|PubMed:19109425};
GN   ORFNames=B0303.9 {ECO:0000312|WormBase:B0303.9};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=1538779; DOI=10.1038/356037a0;
RA   Sulston J., Du Z., Thomas K., Wilson R., Hillier L., Staden R.,
RA   Halloran N., Green P., Thierry-Mieg J., Qiu L., Dear S., Coulson A.,
RA   Craxton M., Durbin R., Berks M., Metzstein M., Hawkins T., Ainscough R.,
RA   Waterston R.;
RT   "The C. elegans genome sequencing project: a beginning.";
RL   Nature 356:37-41(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
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   [3]
RP   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   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24501423; DOI=10.1091/mbc.e13-09-0521;
RA   Delahaye J.L., Foster O.K., Vine A., Saxton D.S., Curtin T.P., Somhegyi H.,
RA   Salesky R., Hermann G.J.;
RT   "Caenorhabditis elegans HOPS and CCZ-1 mediate trafficking to lysosome-
RT   related organelles independently of RAB-7 and SAND-1.";
RL   Mol. Biol. Cell 25:1073-1096(2014).
RN   [5]
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   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26783301; DOI=10.1083/jcb.201506081;
RA   Liu K., Jian Y., Sun X., Yang C., Gao Z., Zhang Z., Liu X., Li Y., Xu J.,
RA   Jing Y., Mitani S., He S., Yang C.;
RT   "Negative regulation of phosphatidylinositol 3-phosphate levels in early-
RT   to-late endosome conversion.";
RL   J. Cell Biol. 212:181-198(2016).
RN   [7]
RP   ERRATUM OF PUBMED:26783301.
RX   PubMed=26975852; DOI=10.1083/jcb.20150608103012016c;
RA   Liu K., Jian Y., Sun X., Yang C., Gao Z., Zhang Z., Liu X., Li Y., Xu J.,
RA   Jing Y., Mitani S., He S., Yang C.;
RT   "Correction: Negative regulation of phosphatidylinositol 3-phosphate levels
RT   in early-to-late endosome conversion.";
RL   J. Cell Biol. 212:739-739(2016).
RN   [8]
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 including the endocytic membrane transport
CC       pathways (PubMed:25273556, PubMed:26783301, PubMed:27558849). Believed
CC       to act as a component of the putative HOPS endosomal tethering complex
CC       which is proposed to be involved in the rab-5-to-rab-7 endosome
CC       conversion probably implicating sand-1, and via binding SNAREs and
CC       SNARE complexes to mediate tethering and docking events during SNARE-
CC       mediated membrane fusion (PubMed:25273556). The HOPS complex is
CC       proposed to be recruited to rab-7 on the late endosomal membrane and to
CC       regulate late endocytic, phagocytic and autophagic traffic towards
CC       lysosomes (By similarity). Within the HOPS complex, contributes to the
CC       normal development of gut granules in embryonic and adult intestinal
CC       cells (PubMed:24501423, PubMed:25273556). Required for
CC       endosome/lysosome fusion (PubMed:26783301, PubMed:27558849). Required
CC       for early embryonic development (PubMed:27558849).
CC       {ECO:0000250|UniProtKB:Q96AX1, ECO:0000269|PubMed:24501423,
CC       ECO:0000269|PubMed:25273556, ECO:0000269|PubMed:26783301,
CC       ECO:0000269|PubMed:27558849}.
CC   -!- SUBUNIT: Probable component of the homotypic fusion and vacuole protein
CC       sorting (HOPS) complex consisting of the core class C Vps proteins vps-
CC       11, vps-16, vps-18, and which further associates with vps-33.1, vps-39
CC       and vps-41 (PubMed:24501423, PubMed:25273556). Interacts with spe-39
CC       (PubMed:19109425). {ECO:0000269|PubMed:19109425,
CC       ECO:0000305|PubMed:24501423, ECO:0000305|PubMed:25273556}.
CC   -!- INTERACTION:
CC       P34260; Q93934: adk-1; NbExp=2; IntAct=EBI-312046, EBI-312052;
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:25273556}. Early
CC       endosome {ECO:0000269|PubMed:27558849}. Late endosome
CC       {ECO:0000269|PubMed:25273556, ECO:0000269|PubMed:27558849}. Apical cell
CC       membrane {ECO:0000269|PubMed:25273556}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:25273556}. Note=Localizes to lysosome-related gut
CC       granules. {ECO:0000269|PubMed:25273556}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed at high levels in somatic
CC       tissues including the pharynx, muscles, hypodermis, neurons,
CC       coelomocytes and spermatheca (PubMed:27558849). Expressed in the
CC       intestine (PubMed:25273556, PubMed:27558849).
CC       {ECO:0000269|PubMed:25273556, ECO:0000269|PubMed:27558849}.
CC   -!- DISRUPTION PHENOTYPE: Viable, and develop into fertile adults, but
CC       their progeny arrest before embryonic morphogenesis (PubMed:27558849).
CC       Defective endosome/lysosome size and fusion, and delayed endocytic
CC       trafficking to lysosomes in coelomocytes (PubMed:26783301,
CC       PubMed:27558849). Reduced number of gut granules in the adult intestine
CC       (PubMed:24501423, PubMed:27558849). RNAi-mediated knockdown results in
CC       a reduced number of gut granules in embryonic intestinal cells
CC       (PubMed:24501423). RNAi-mediated knockdown results in the accumulation
CC       of lysosomal proteins such as lmp-1 in early endocytic compartments,
CC       and the formation of large late endosomes/lysosomes, but with
CC       simultaneous expression of rab-5- and rab-7-positive vesicles on the
CC       basal side of gut cells (PubMed:25273556). Double RNAi-mediated
CC       knockdown together with vsp-33.2 results in defective protein
CC       trafficking to lysosomal compartments, and an irregular distribution of
CC       vesicles of various sizes throughout the gut cells. RNAi-mediated
CC       knockdown in a sand-1 mutant background results in no viable offspring
CC       (PubMed:25273556). Double RNAi-mediated knockdown together with vsp-
CC       33.1 in a sand-1 mutant background rescues the large endosome phenotype
CC       and the defective protein trafficking to lysosomal compartments in the
CC       sand-1 single mutant, but still results in lethality (PubMed:25273556).
CC       Double knockout with tbc-2 or single knockout in a constitutively
CC       active rab-5 mutant background, rescues the large endosome formation
CC       defect in coelomocytes in the individual tbc-2 single and
CC       constitutively active rab-5 mutants (PubMed:27558849).
CC       {ECO:0000269|PubMed:24501423, ECO:0000269|PubMed:25273556,
CC       ECO:0000269|PubMed:26783301, ECO:0000269|PubMed:27558849}.
CC   -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR   EMBL; FO080163; CCD61712.1; -; Genomic_DNA.
DR   PIR; S27790; S27790.
DR   RefSeq; NP_498920.2; NM_066519.4.
DR   AlphaFoldDB; P34260; -.
DR   SMR; P34260; -.
DR   BioGRID; 41424; 2.
DR   ComplexPortal; CPX-1136; HOPS complex.
DR   IntAct; P34260; 2.
DR   STRING; 6239.B0303.9; -.
DR   EPD; P34260; -.
DR   PaxDb; P34260; -.
DR   PeptideAtlas; P34260; -.
DR   EnsemblMetazoa; B0303.9.1; B0303.9.1; WBGene00015130.
DR   GeneID; 176221; -.
DR   KEGG; cel:CELE_B0303.9; -.
DR   CTD; 176221; -.
DR   WormBase; B0303.9; CE00539; WBGene00015130; vps-33.1.
DR   eggNOG; KOG1302; Eukaryota.
DR   GeneTree; ENSGT00940000155165; -.
DR   HOGENOM; CLU_026398_0_0_1; -.
DR   InParanoid; P34260; -.
DR   OMA; FHIFFVP; -.
DR   OrthoDB; 406738at2759; -.
DR   PhylomeDB; P34260; -.
DR   PRO; PR:P34260; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00015130; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033263; C:CORVET complex; IBA:GO_Central.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030897; C:HOPS complex; ISS:WormBase.
DR   GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; 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; -; 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:SF1; PTHR11679:SF1; 1.
DR   Pfam; PF00995; Sec1; 1.
DR   PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR   SUPFAM; SSF56815; SSF56815; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Endosome; Lysosome; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..603
FT                   /note="Vacuolar protein sorting-associated protein 33A"
FT                   /id="PRO_0000071960"
SQ   SEQUENCE   603 AA;  68166 MW;  FF959FE7A617BD6A CRC64;
     MAANEDRDDA AAILNWEGTS EIKSANEYSR NLLFSVLDSL DGNKTIVWDR DRSVMHRVNL
     FAGASVLAAH GVVANHSIET KKSASTPHVV FFLAPTMVSL DLLCDYIDNV RNDSKILYQV
     FFIPEAWFVV RESLKTRAEG KYWERLESVK EIPLCWLPRD GECLSLSSPQ IAARLLINGD
     WTHLHKCAVA LNQLIDMCRG RSSSSNQRPM SIYAKGKWAS DVAKMMGKIR NSAEADSMTK
     NLDPIEGLLK INRIVLIDRW MDPLTPMLSQ LTFYGLLDEI YGIGMVNSVK VPEMEFKNEK
     DGDPFQEKEV YLIDEVYHRL KHSHINAVSI EASKVLAEIR DDEQFDRDKM SVAEYSVLVK
     KMPKIINRKK MIEVHMRLAE MIQSHVYCKQ SDSIKLERDL LEYSDSDKAI PLIEDLIFDA
     SPLNAVLRLI SVHSLTCGGL KPSVLQHYRR IVNQSYGSSA LNKVLKMQKM GLIREKGGGG
     KMQCEYAQMM FQQMKKNHDM LPEEFSEAKL DDMAYAYSGF SPLLCKMLEE GDRVKWVGWP
     KTVIGDKSDL IAERDGRGTC VFVIGGLTRS ELAIIRENLP NVALITTSAL ITGDKLLNNI
     TNI
 
 
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