VPS3_ARATH
ID VPS3_ARATH Reviewed; 984 AA.
AC F4I312; O23136; Q0WPB0;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Vacuolar sorting protein 3 {ECO:0000303|PubMed:29463724};
GN Name=VPS3 {ECO:0000303|PubMed:29463724};
GN OrderedLocusNames=At1g22860 {ECO:0000312|Araport:AT1G22860};
GN ORFNames=F19G10.18 {ECO:0000312|EMBL:AAB72173.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 676-984.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH VPS11; RABF2A AND RABF2B,
RP SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=29463724; DOI=10.1073/pnas.1717839115;
RA Takemoto K., Ebine K., Askani J.C., Krueger F., Gonzalez Z.A., Ito E.,
RA Goh T., Schumacher K., Nakano A., Ueda T.;
RT "Distinct sets of tethering complexes, SNARE complexes, and Rab GTPases
RT mediate membrane fusion at the vacuole in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E2457-E2466(2018).
CC -!- FUNCTION: Essential protein required during embryogenesis. Believed to
CC act as a component of the putative class C core vacuole/endosome
CC tethering (CORVET) endosomal tethering complexes. CORVET is required
CC for vacuolar transport of SYP22. Involved in root development
CC (PubMed:29463724). Plays a role in vesicle-mediated protein trafficking
CC of the endocytic membrane transport pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q8WUH2, ECO:0000269|PubMed:29463724}.
CC -!- SUBUNIT: Component of the class C core vacuole/endosome tethering
CC (CORVET) complex. Their common core is composed of the class C Vps core
CC proteins VPS11, VCL1, VPS18 and VPS33, which in CORVET further
CC associates with VPS3 (PubMed:29463724). Interacts directly with VPS11.
CC Binds to RABF2A and RABF2B (PubMed:29463724).
CC {ECO:0000269|PubMed:29463724}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q8WUH2};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q8WUH2}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q8WUH2}. Cytoplasm
CC {ECO:0000269|PubMed:29463724}. Note=Co-localizes with VAMP727, VPS18,
CC RABG3F and RABF2B at cytoplasmic punctate structures.
CC {ECO:0000269|PubMed:29463724}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality (PubMed:29463724).
CC Heterozygous mutants produce some yellowish seeds with developmentally
CC retarded or abnormally shaped embryos. Conditional dexamethasone (DEX)-
CC inducible mutants exhibit abnormal root morphology (PubMed:29463724).
CC {ECO:0000269|PubMed:29463724}.
CC -!- SIMILARITY: Belongs to the TRAP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB72173.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF01039.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF01039.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF000657; AAB72173.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30297.2; -; Genomic_DNA.
DR EMBL; AK229169; BAF01039.1; ALT_SEQ; mRNA.
DR PIR; E86362; E86362.
DR RefSeq; NP_001319063.1; NM_001332561.1.
DR AlphaFoldDB; F4I312; -.
DR STRING; 3702.AT1G22860.1; -.
DR PaxDb; F4I312; -.
DR PRIDE; F4I312; -.
DR ProteomicsDB; 242778; -.
DR EnsemblPlants; AT1G22860.1; AT1G22860.1; AT1G22860.
DR GeneID; 838891; -.
DR Gramene; AT1G22860.1; AT1G22860.1; AT1G22860.
DR KEGG; ath:AT1G22860; -.
DR Araport; AT1G22860; -.
DR TAIR; locus:2017714; AT1G22860.
DR eggNOG; KOG2063; Eukaryota.
DR HOGENOM; CLU_009467_0_0_1; -.
DR InParanoid; F4I312; -.
DR OMA; DKKLCQV; -.
DR OrthoDB; 682722at2759; -.
DR PRO; PR:F4I312; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I312; baseline and differential.
DR GO; GO:0033263; C:CORVET complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IBA:GO_Central.
DR GO; GO:0034058; P:endosomal vesicle fusion; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0010015; P:root morphogenesis; IMP:UniProtKB.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR032914; Vam6/VPS39/TRAP1.
DR InterPro; IPR019452; VPS39/TGF_beta_rcpt-assoc_1.
DR InterPro; IPR019453; VPS39/TGF_beta_rcpt-assoc_2.
DR PANTHER; PTHR12894; PTHR12894; 1.
DR Pfam; PF00637; Clathrin; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF10366; Vps39_1; 1.
DR Pfam; PF10367; Vps39_2; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS50219; CNH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endosome; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..984
FT /note="Vacuolar sorting protein 3"
FT /id="PRO_0000444309"
FT DOMAIN 21..339
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REPEAT 663..844
FT /note="CHCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01006"
SQ SEQUENCE 984 AA; 109906 MW; F0088DC86812944F CRC64;
MSKSRAVVEL TARFDLGGDD KIRALSLSPI SDSQTLVYLG TYSGSLILLS LDTLTNTVSR
LASVSLSPSP VESIFVLGEE RGRVLALCNG YLFLLDSLLS QPAKRLGGLL KGINVIAKRV
RGRDSSSTDL LPSEISTDSS SSKKFLQLLG AGNLVSDVRG NDSRHERVQQ GHYVFAVAIG
ERMLLIELQC AEKEGLSGSF VVLKEILGIG GIKTLVWLDD YVIAGTVKGY SLISCVTGLS
GVIFTLPDVS GPPLLKLLCK EWKVLLLVDN VGVVVDTNGQ PIGGSLVFRR RPDSVGELSF
YLVTVGDGKM EIHQKKSGAC VQSVSFGPQG CGPSLLAADE AGDGNLLVVT TLSKLIFYRR
VPYEEQIKDL LRKKRYRETI SLVEELDSQG EISKDMLSFL HAQIGYLLLF DLRFEEAVNQ
FLKSEKMEPS EVFPFIMRDP NRWSLVVPRN RYWGLHPPPA PFEDVVDNGL MAIQRANFLR
KAGMDTPVDE EFFSDPPSRA DLLDSAIKNI TRYLEISREK GLTLPVREGI DTLLMLLYRA
LNRVEDMENL ASSGNNCVVE ELETLLTESG HLRTLAFLYA TKGMGAKALA IWRLFTKNYS
SGLWQDSDDL VPYLHDNELI RLSGKEAAAA EAARILEEPC DPELALQHLS WIADVNPLFA
IQVLTSDKRT EELSPEQVIQ AIDPKKVEII QRYFQWLIEE RDYTDPQLHT SYALSLARSA
LECVEVQNGI QEADVPNGSE AHDSNVGSIS LFEVDVRERL QAFLQSSDLY DPEEILELVE
GSELWLEKAI LYRRIGKETL VLQILALKLE DCAAAEQYCV EIGRPDAFMQ LLDMYLDPQN
GKEPMFKAAV RLLHNHGESL DPLQVLDKLS PDMPLKLASD TILRMLRARV HHHRQGQIVH
NISRALDVDS RLARLEERSR HMQINDESLC DSCYARLGTK LFAMYPDDTI VCYKCYRRLG
ESKSVTGRDF KRDVLIKPGW LVNR