ID   VP371_ARATH             Reviewed;         217 AA.
AC   Q9SCP9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Vacuolar protein-sorting-associated protein 37 homolog 1;
DE            Short=AtVPS37-1;
DE   AltName: Full=ESCRT-I complex subunit VPS37 homolog 1;
GN   Name=VPS37-1; OrderedLocusNames=At3g53120; ORFNames=T4D2.50;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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].
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   [4]
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   [5]
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   -!- INTERACTION:
CC       Q9SCP9; Q9LHG8: ELC; NbExp=4; IntAct=EBI-3865264, EBI-3865248;
CC       Q9SCP9; Q9FFY6: ELCL; NbExp=4; IntAct=EBI-3865264, EBI-3865255;
CC       Q9SCP9; Q9SKI2: VPS2.1; NbExp=3; IntAct=EBI-3865264, EBI-3865345;
CC       Q9SCP9; O65421: VPS28-1; NbExp=3; IntAct=EBI-3865264, EBI-3865310;
CC       Q9SCP9; Q9S9T7: VPS28-2; NbExp=3; IntAct=EBI-3865264, EBI-3865335;
CC   -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VPS37 family. {ECO:0000305}.
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DR   EMBL; AL132958; CAB64215.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79039.1; -; Genomic_DNA.
DR   EMBL; BX822324; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; T46158; T46158.
DR   RefSeq; NP_190880.1; NM_115172.4.
DR   AlphaFoldDB; Q9SCP9; -.
DR   SMR; Q9SCP9; -.
DR   BioGRID; 9795; 7.
DR   IntAct; Q9SCP9; 5.
DR   STRING; 3702.AT3G53120.1; -.
DR   TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR   PaxDb; Q9SCP9; -.
DR   PRIDE; Q9SCP9; -.
DR   ProteomicsDB; 242626; -.
DR   EnsemblPlants; AT3G53120.1; AT3G53120.1; AT3G53120.
DR   GeneID; 824478; -.
DR   Gramene; AT3G53120.1; AT3G53120.1; AT3G53120.
DR   KEGG; ath:AT3G53120; -.
DR   Araport; AT3G53120; -.
DR   TAIR; locus:2102008; AT3G53120.
DR   eggNOG; KOG3270; Eukaryota.
DR   HOGENOM; CLU_036442_0_0_1; -.
DR   InParanoid; Q9SCP9; -.
DR   OMA; TIYHRRT; -.
DR   OrthoDB; 1406640at2759; -.
DR   PhylomeDB; Q9SCP9; -.
DR   PRO; PR:Q9SCP9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SCP9; baseline and differential.
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   Endosome; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..217
FT                   /note="Vacuolar protein-sorting-associated protein 37
FT                   homolog 1"
FT                   /id="PRO_0000368189"
FT   DOMAIN          137..217
FT                   /note="VPS37 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00646"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   217 AA;  24940 MW;  3BA1A7D5349CB892 CRC64;
     MFNFWGSKDQ QQGQSRPQEA SSQSPWYSPS LVSSPSSSRP QSSGQISAQV SPGEAAGIIV
     FLKDKSVDEL RKLLSDKDAY QQFLLSLDQV KVQNNIKDEL RRETLQLARD NLEKEPQIME
     LRNQCRIIRT TELATAQEKL NELERQKEEI LKFYSPGSLL HKLQEAMNQV DEESEALQEK
     FLEKEIDTAA FVQKYKKLRT TYHRRALIHL AAKTSNI