VP372_ARATH
ID VP372_ARATH Reviewed; 218 AA.
AC Q3EBL9; Q8VYK5; Q9ZQA6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Vacuolar protein-sorting-associated protein 37 homolog 2;
DE Short=AtVPS37-2;
DE AltName: Full=ESCRT-I complex subunit VPS37 homolog 2;
GN Name=VPS37-2; OrderedLocusNames=At2g36680; ORFNames=F13K3.8;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 2).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP IDENTIFICATION, NOMENCLATURE, AND INTERACTION WITH ELC.
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-I complex (endosomal sorting complex
CC required for transport I), a regulator of vesicular trafficking
CC process. Required for the sorting of endocytic ubiquitinated cargos
CC into multivesicular bodies (MVBs) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the endosomal sorting required for transport
CC complex I (ESCRT-I), composed of ELC, VPS28 and VPS37. Interacts with
CC ELC. {ECO:0000269|PubMed:17090720}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3EBL9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3EBL9-2; Sequence=VSP_036800, VSP_036801;
CC Name=3;
CC IsoId=Q3EBL9-3; Sequence=VSP_036799, VSP_036802;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the VPS37 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD20144.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX821771; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC006282; AAD20144.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09282.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09283.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09284.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09285.1; -; Genomic_DNA.
DR EMBL; AY070474; AAL49940.1; -; mRNA.
DR EMBL; AY091674; AAM10273.1; -; mRNA.
DR EMBL; BX821771; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; D84783; D84783.
DR RefSeq; NP_001031495.1; NM_001036418.2. [Q3EBL9-3]
DR RefSeq; NP_001078013.1; NM_001084544.2. [Q3EBL9-3]
DR RefSeq; NP_850268.2; NM_179937.4. [Q3EBL9-1]
DR RefSeq; NP_850269.2; NM_179938.2. [Q3EBL9-2]
DR AlphaFoldDB; Q3EBL9; -.
DR SMR; Q3EBL9; -.
DR BioGRID; 3584; 3.
DR IntAct; Q3EBL9; 5.
DR STRING; 3702.AT2G36680.1; -.
DR TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; Q3EBL9; -.
DR PaxDb; Q3EBL9; -.
DR PRIDE; Q3EBL9; -.
DR ProteomicsDB; 242734; -. [Q3EBL9-1]
DR EnsemblPlants; AT2G36680.1; AT2G36680.1; AT2G36680. [Q3EBL9-1]
DR EnsemblPlants; AT2G36680.2; AT2G36680.2; AT2G36680. [Q3EBL9-2]
DR EnsemblPlants; AT2G36680.3; AT2G36680.3; AT2G36680. [Q3EBL9-3]
DR EnsemblPlants; AT2G36680.4; AT2G36680.4; AT2G36680. [Q3EBL9-3]
DR GeneID; 818240; -.
DR Gramene; AT2G36680.1; AT2G36680.1; AT2G36680. [Q3EBL9-1]
DR Gramene; AT2G36680.2; AT2G36680.2; AT2G36680. [Q3EBL9-2]
DR Gramene; AT2G36680.3; AT2G36680.3; AT2G36680. [Q3EBL9-3]
DR Gramene; AT2G36680.4; AT2G36680.4; AT2G36680. [Q3EBL9-3]
DR KEGG; ath:AT2G36680; -.
DR Araport; AT2G36680; -.
DR TAIR; locus:2040560; AT2G36680.
DR eggNOG; KOG3270; Eukaryota.
DR HOGENOM; CLU_036442_0_0_1; -.
DR InParanoid; Q3EBL9; -.
DR OMA; SLYHRRA; -.
DR PhylomeDB; Q3EBL9; -.
DR PRO; PR:Q3EBL9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q3EBL9; baseline and differential.
DR Genevisible; Q3EBL9; AT.
DR GO; GO:0000813; C:ESCRT I complex; ISS:TAIR.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR Gene3D; 1.10.287.660; -; 1.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR029012; Helix_hairpin_bin_sf.
DR InterPro; IPR009851; Mod_r.
DR Pfam; PF07200; Mod_r; 1.
DR SUPFAM; SSF140111; SSF140111; 1.
DR PROSITE; PS51314; VPS37_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endosome; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..218
FT /note="Vacuolar protein-sorting-associated protein 37
FT homolog 2"
FT /id="PRO_0000368190"
FT DOMAIN 137..218
FT /note="VPS37 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00646"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 125..168
FT /note="CRIIRTSELATAQEKLNELENQREEILKFYSPGSLLHRLQDAMN -> VNNI
FT IQSLSELIKYMKLLSICIIFLKTVQNNPYIRACDCSREAQ (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_036799"
FT VAR_SEQ 125..139
FT /note="CRIIRTSELATAQEK -> NNPYIRACDCSREAQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_036800"
FT VAR_SEQ 140..218
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_036801"
FT VAR_SEQ 169..218
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_036802"
SQ SEQUENCE 218 AA; 24987 MW; 27EADEA09A48DB19 CRC64;
MFNFWGSKEQ QQGQSRPSPE ASATPWYSPS LVTSPSSSRP QTSGQIPSHV SPGEAAGIIA
ILKDKSVDEL RKLLSDKDAY QQFLHSLDQV TIQNNIREEL RKETLHLARE NLEKEPQIVE
LRNQCRIIRT SELATAQEKL NELENQREEI LKFYSPGSLL HRLQDAMNQV DEESEELQQK
FMEKDIDTAA FVQKYKKLRS KYHRRALIHL AAKTSSIG