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VPS2C_ARATH
ID   VPS2C_ARATH             Reviewed;         210 AA.
AC   Q941D5; Q9ZWB5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Vacuolar protein sorting-associated protein 2 homolog 3;
DE            Short=AtVPS2-3;
DE   AltName: Full=Charged multivesicular body protein 2 homolog 3;
DE   AltName: Full=ESCRT-III complex subunit VPS2 homolog 3;
GN   Name=VPS2.3; Synonyms=CHMP2-3; OrderedLocusNames=At1g03950;
GN   ORFNames=F21M11.12;
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].
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   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   [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-III complex, which is required for
CC       multivesicular bodies (MVBs) formation and sorting of endosomal cargo
CC       proteins into MVBs. The ESCRT-III complex is probably involved in the
CC       concentration of MVB cargo (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the endosomal sorting required for transport
CC       complex III (ESCRT-III), composed at least of VPS2, VPS20, VPS24 and
CC       VPS32. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD10675.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC003027; AAD10675.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE27637.1; -; Genomic_DNA.
DR   EMBL; AY052238; AAK97708.1; -; mRNA.
DR   EMBL; AY060501; AAL31114.1; -; mRNA.
DR   PIR; D86170; D86170.
DR   RefSeq; NP_563696.1; NM_100276.4.
DR   AlphaFoldDB; Q941D5; -.
DR   SMR; Q941D5; -.
DR   BioGRID; 24597; 21.
DR   IntAct; Q941D5; 21.
DR   STRING; 3702.AT1G03950.1; -.
DR   TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR   PaxDb; Q941D5; -.
DR   PRIDE; Q941D5; -.
DR   ProteomicsDB; 242321; -.
DR   EnsemblPlants; AT1G03950.1; AT1G03950.1; AT1G03950.
DR   GeneID; 839362; -.
DR   Gramene; AT1G03950.1; AT1G03950.1; AT1G03950.
DR   KEGG; ath:AT1G03950; -.
DR   Araport; AT1G03950; -.
DR   TAIR; locus:2024107; AT1G03950.
DR   eggNOG; KOG3230; Eukaryota.
DR   HOGENOM; CLU_069208_1_1_1; -.
DR   InParanoid; Q941D5; -.
DR   OMA; NMREFQM; -.
DR   OrthoDB; 1480977at2759; -.
DR   PhylomeDB; Q941D5; -.
DR   PRO; PR:Q941D5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q941D5; baseline and differential.
DR   Genevisible; Q941D5; AT.
DR   GO; GO:0000815; C:ESCRT III complex; ISS:TAIR.
DR   GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR   GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR   InterPro; IPR005024; Snf7_fam.
DR   PANTHER; PTHR10476; PTHR10476; 1.
DR   Pfam; PF03357; Snf7; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Endosome; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..210
FT                   /note="Vacuolar protein sorting-associated protein 2
FT                   homolog 3"
FT                   /id="PRO_0000368197"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          28..84
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        9..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   210 AA;  23026 MW;  B153BF12E94D54EB CRC64;
     MNIFTKKPNP REVLRESKRE MTQATRGIEK EIGSLQSEEK KLVLEIKRTA KSGNEGATKI
     LARQLIRLRQ QIANLQGSRA QMRGIATHTQ AMHAHTSVAA GMQGATKAMA AMSKNMDPAK
     QAKVMREFQK QSAQMDMTTE MMSDSIDDAL DNDEAEDETE DLTNQVLDEI GIDIASQLSS
     APKGKIGGKK AEDVGSSGID ELEKRLAALR
 
 
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