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ABIL2_ARATH
ID   ABIL2_ARATH             Reviewed;         312 AA.
AC   Q9M3A3; Q8GXQ1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Protein ABIL2;
DE   AltName: Full=Abl interactor-like protein 2;
DE            Short=AtABIL2;
GN   Name=ABIL2; OrderedLocusNames=At3g49290; ORFNames=F2K15.150;
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 [MRNA] (ISOFORM 1).
RX   PubMed=15659634; DOI=10.1105/tpc.104.027987;
RA   Basu D., Le J., El-Din El-Assal S., Huang S., Zhang C., Mallery E.L.,
RA   Koliantz G., Staiger C.J., Szymanski D.B.;
RT   "DISTORTED3/SCAR2 is a putative Arabidopsis WAVE complex subunit that
RT   activates the Arp2/3 complex and is required for epidermal morphogenesis.";
RL   Plant Cell 17:502-524(2005).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
CC   -!- FUNCTION: Involved in regulation of actin and microtubule organization.
CC       Part of a WAVE complex that activates the Arp2/3 complex (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds SCAR. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9M3A3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9M3A3-2; Sequence=VSP_031020, VSP_031021;
CC   -!- SIMILARITY: Belongs to the ABI family. {ECO:0000305}.
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DR   EMBL; AY817013; AAW49257.1; -; mRNA.
DR   EMBL; AL132956; CAB66408.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78522.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78523.1; -; Genomic_DNA.
DR   EMBL; AK118112; BAC42738.1; -; mRNA.
DR   PIR; T45834; T45834.
DR   RefSeq; NP_001030832.1; NM_001035755.2. [Q9M3A3-1]
DR   RefSeq; NP_190498.1; NM_114788.4. [Q9M3A3-1]
DR   AlphaFoldDB; Q9M3A3; -.
DR   SMR; Q9M3A3; -.
DR   BioGRID; 9408; 2.
DR   IntAct; Q9M3A3; 9.
DR   STRING; 3702.AT3G49290.1; -.
DR   iPTMnet; Q9M3A3; -.
DR   PaxDb; Q9M3A3; -.
DR   PRIDE; Q9M3A3; -.
DR   ProteomicsDB; 244606; -. [Q9M3A3-1]
DR   EnsemblPlants; AT3G49290.1; AT3G49290.1; AT3G49290. [Q9M3A3-1]
DR   EnsemblPlants; AT3G49290.2; AT3G49290.2; AT3G49290. [Q9M3A3-1]
DR   GeneID; 824090; -.
DR   Gramene; AT3G49290.1; AT3G49290.1; AT3G49290. [Q9M3A3-1]
DR   Gramene; AT3G49290.2; AT3G49290.2; AT3G49290. [Q9M3A3-1]
DR   KEGG; ath:AT3G49290; -.
DR   Araport; AT3G49290; -.
DR   TAIR; locus:2082941; AT3G49290.
DR   eggNOG; ENOG502R3IQ; Eukaryota.
DR   HOGENOM; CLU_054853_1_0_1; -.
DR   InParanoid; Q9M3A3; -.
DR   OMA; NLRMSCI; -.
DR   PhylomeDB; Q9M3A3; -.
DR   PRO; PR:Q9M3A3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M3A3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   InterPro; IPR028457; ABI.
DR   PANTHER; PTHR10460; PTHR10460; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..312
FT                   /note="Protein ABIL2"
FT                   /id="PRO_0000191795"
FT   REGION          173..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..132
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11910074"
FT                   /id="VSP_031020"
FT   VAR_SEQ         133..137
FT                   /note="RYILP -> MQSLS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11910074"
FT                   /id="VSP_031021"
SQ   SEQUENCE   312 AA;  35777 MW;  6CA00ACDD755888B CRC64;
     MPASHEASNY DEVSMQQSML FSDGLQDLKN LRAQLYSAAE YFELSYTTDD KKQIVVETLK
     DYAVKALVNT VDHLGSVTYK VNDFIDEKVD EVSETELRVS CIEQRLRMCQ EYMDHEGRSQ
     QSLVIDTPKF HKRYILPAGE IMTATNLEKL KYFGSSLEDA DDWNQFRNAV RATIRETPPP
     PVRKSTSQSS SPRQPPQRSA TFSFTSTIPK KEQDKRSVSP HRFPLLRSGS VATRKSASIS
     RPTTPSKSRS ITPIRYPSEP RRSASVRVAF EKDNQKETEQ QQPSKSKRLL KALLSRRKTK
     KDDTLYTFLD EY
 
 
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