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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};
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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
 
 
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