VPS36_ARATH
ID VPS36_ARATH Reviewed; 440 AA.
AC Q9FF81; Q0WQI2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Vacuolar protein sorting-associated protein 36;
DE Short=AtVPS36;
DE AltName: Full=ESCRT-II complex subunit VPS36;
GN Name=VPS36; OrderedLocusNames=At5g04920; ORFNames=MUG13.23;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-205.
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 [5]
RP IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=17090720; DOI=10.1242/dev.02654;
RA Spitzer C., Schellmann S., Sabovljevic A., Shahriari M., Keshavaiah C.,
RA Bechtold N., Herzog M., Mueller S., Hanisch F.-G., Huelskamp M.;
RT "The Arabidopsis elch mutant reveals functions of an ESCRT component in
RT cytokinesis.";
RL Development 133:4679-4689(2006).
RN [6]
RP IDENTIFICATION.
RX PubMed=16488176; DOI=10.1016/j.tplants.2006.01.008;
RA Winter V., Hauser M.-T.;
RT "Exploring the ESCRTing machinery in eukaryotes.";
RL Trends Plant Sci. 11:115-123(2006).
CC -!- FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex
CC required for transport II), which is required for multivesicular body
CC (MVB) formation and sorting of endosomal cargo proteins into MVBs. The
CC ESCRT-II complex is probably involved in the recruitment of the ESCRT-
CC III complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the endosomal sorting required for transport
CC complex II (ESCRT-II), composed of VPS22, VPS25 and VPS36.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9FF81; Q9LHG8: ELC; NbExp=3; IntAct=EBI-3865302, EBI-3865248;
CC Q9FF81; Q9SKI2: VPS2.1; NbExp=3; IntAct=EBI-3865302, EBI-3865345;
CC Q9FF81; Q8GXN6: VPS20.1; NbExp=5; IntAct=EBI-3865302, EBI-3865286;
CC Q9FF81; Q9FY89: VPS20.2; NbExp=5; IntAct=EBI-3865302, EBI-3865360;
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VPS36 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF00617.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AB005245; BAB11514.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90804.1; -; Genomic_DNA.
DR EMBL; AY072089; AAL59912.1; -; mRNA.
DR EMBL; AY096570; AAM20220.1; -; mRNA.
DR EMBL; AK228715; BAF00617.1; ALT_SEQ; mRNA.
DR RefSeq; NP_196112.1; NM_120574.5.
DR AlphaFoldDB; Q9FF81; -.
DR SMR; Q9FF81; -.
DR BioGRID; 15653; 8.
DR IntAct; Q9FF81; 6.
DR STRING; 3702.AT5G04920.1; -.
DR TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; Q9FF81; -.
DR PaxDb; Q9FF81; -.
DR PRIDE; Q9FF81; -.
DR ProteomicsDB; 242703; -.
DR EnsemblPlants; AT5G04920.1; AT5G04920.1; AT5G04920.
DR GeneID; 830374; -.
DR Gramene; AT5G04920.1; AT5G04920.1; AT5G04920.
DR KEGG; ath:AT5G04920; -.
DR Araport; AT5G04920; -.
DR TAIR; locus:2175274; AT5G04920.
DR eggNOG; KOG2760; Eukaryota.
DR HOGENOM; CLU_015433_0_1_1; -.
DR InParanoid; Q9FF81; -.
DR OMA; TLNARVW; -.
DR OrthoDB; 981902at2759; -.
DR PhylomeDB; Q9FF81; -.
DR PRO; PR:Q9FF81; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FF81; baseline and differential.
DR Genevisible; Q9FF81; AT.
DR GO; GO:0005769; C:early endosome; IDA:TAIR.
DR GO; GO:0000814; C:ESCRT II complex; ISS:TAIR.
DR GO; GO:0005770; C:late endosome; IDA:TAIR.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IDA:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IMP:TAIR.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0090351; P:seedling development; IMP:TAIR.
DR GO; GO:0007033; P:vacuole organization; IMP:TAIR.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR021648; GLUE_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR040608; Snf8/Vps36.
DR InterPro; IPR037855; Vps36.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13128; PTHR13128; 1.
DR Pfam; PF04157; EAP30; 1.
DR Pfam; PF11605; Vps36_ESCRT-II; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51495; GLUE; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endosome; Protein transport; Reference proteome; Transport.
FT CHAIN 1..440
FT /note="Vacuolar protein sorting-associated protein 36"
FT /id="PRO_0000368194"
FT DOMAIN 17..97
FT /note="GLUE N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
FT DOMAIN 115..149
FT /note="GLUE C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
FT REGION 144..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 192..212
FT /evidence="ECO:0000255"
SQ SEQUENCE 440 AA; 49034 MW; 25146E6B9F39FF75 CRC64;
MASGSSSIAI GGLFENAEVT TSGRPVLRRN EVECFLLSSI DIDSEDDPPR FTALRSGNLI
LTTHRLIWIP SQSNESVPSS IPLSAVTHIY SHKKSIKSMF HSPRIRFQAD PGSIVVTIVF
RGKGDFDGFL SKLWECWRGR AWEEEEKSES ETSKSGSGTV AQGLYGNDGT VRMVGLAGIL
RKEQEQWEST DKSLQDAFQD LNALMSKAKE MVSLAEKMRQ KLLSAPSSQN GSTDDEEMGS
KEEMQQWMLS VGIISPVTKE SAGALYHQEL SRQLADFVRI PLEKAGGMIS LTDMYYHFNR
ARGTELISPD DLWQACTLWE KFDVPVMLRK FDSGVMVIQN KSHSDEEVMS RIRMLVTKTE
TLRVGVTASD AALTLKIAPA MAKEHLLSAE TKGLLCRDMS PDGLRFYFNL FPEIDPTNLH
IVKEFGTYGE WIKATSLLSV
