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ARF2B_ARATH
ID   ARF2B_ARATH             Reviewed;         181 AA.
AC   P0DH91; Q9S9K6; Q9SGY6; Q9SRC3;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=ADP-ribosylation factor 2-B;
DE            Short=AtARF2;
DE   AltName: Full=ARF1-like protein U5;
GN   Name=ARF2-B; Synonyms=ARFA1-D, ARFA2-B, U5; OrderedLocusNames=At1g70490;
GN   ORFNames=F20B24.21, F24J13.6;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   ACTIVITY REGULATION.
RX   PubMed=16731582; DOI=10.1104/pp.106.077818;
RA   Song X.-F., Yang C.-Y., Liu J., Yang W.-C.;
RT   "RPA, a class II ARFGAP protein, activates ARF1 and U5 and plays a role in
RT   root hair development in Arabidopsis.";
RL   Plant Physiol. 141:966-976(2006).
CC   -!- FUNCTION: GTP-binding protein involved in protein trafficking; may
CC       modulate vesicle budding and uncoating within the Golgi apparatus.
CC   -!- ACTIVITY REGULATION: Activated by AGD10. {ECO:0000269|PubMed:16731582}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF17671.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC009398; AAF17671.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC010796; AAG52463.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35068.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35069.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35070.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60800.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60801.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60802.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60803.1; -; Genomic_DNA.
DR   EMBL; AF360164; AAK25874.1; -; mRNA.
DR   EMBL; AY056341; AAL07190.1; -; mRNA.
DR   EMBL; AY087235; AAM64791.1; -; mRNA.
DR   PIR; G96728; G96728.
DR   RefSeq; NP_001323060.1; NM_001334454.1.
DR   RefSeq; NP_001323061.1; NM_001334455.1.
DR   RefSeq; NP_001323062.1; NM_001334452.1.
DR   RefSeq; NP_001323063.1; NM_001334453.1.
DR   RefSeq; NP_177206.1; NM_105717.3.
DR   RefSeq; NP_564195.1; NM_102198.5.
DR   RefSeq; NP_850975.1; NM_180644.3.
DR   RefSeq; NP_974120.1; NM_202391.2.
DR   AlphaFoldDB; P0DH91; -.
DR   SMR; P0DH91; -.
DR   BioGRID; 24195; 5.
DR   BioGRID; 28605; 10.
DR   IntAct; P0DH91; 9.
DR   PRIDE; P0DH91; -.
DR   EnsemblPlants; AT1G23490.1; AT1G23490.1; AT1G23490.
DR   EnsemblPlants; AT1G70490.1; AT1G70490.1; AT1G70490.
DR   EnsemblPlants; AT1G70490.2; AT1G70490.2; AT1G70490.
DR   EnsemblPlants; AT1G70490.3; AT1G70490.3; AT1G70490.
DR   EnsemblPlants; AT1G70490.4; AT1G70490.4; AT1G70490.
DR   EnsemblPlants; AT1G70490.5; AT1G70490.5; AT1G70490.
DR   EnsemblPlants; AT1G70490.6; AT1G70490.6; AT1G70490.
DR   EnsemblPlants; AT1G70490.7; AT1G70490.7; AT1G70490.
DR   GeneID; 838957; -.
DR   GeneID; 843385; -.
DR   Gramene; AT1G23490.1; AT1G23490.1; AT1G23490.
DR   Gramene; AT1G70490.1; AT1G70490.1; AT1G70490.
DR   Gramene; AT1G70490.2; AT1G70490.2; AT1G70490.
DR   Gramene; AT1G70490.3; AT1G70490.3; AT1G70490.
DR   Gramene; AT1G70490.4; AT1G70490.4; AT1G70490.
DR   Gramene; AT1G70490.5; AT1G70490.5; AT1G70490.
DR   Gramene; AT1G70490.6; AT1G70490.6; AT1G70490.
DR   Gramene; AT1G70490.7; AT1G70490.7; AT1G70490.
DR   KEGG; ath:AT1G23490; -.
DR   KEGG; ath:AT1G70490; -.
DR   Araport; AT1G70490; -.
DR   TAIR; locus:2026780; AT1G70490.
DR   HOGENOM; CLU_040729_9_3_1; -.
DR   InParanoid; P0DH91; -.
DR   OMA; WEDVCRI; -.
DR   OrthoDB; 1362554at2759; -.
DR   PhylomeDB; P0DH91; -.
DR   PRO; PR:P0DH91; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P0DH91; baseline and differential.
DR   Genevisible; P0DH91; AT.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0005525; F:GTP binding; ISS:TAIR.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0016004; F:phospholipase activator activity; TAS:TAIR.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd04150; Arf1_5_like; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR045872; Arf1-5-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR024156; Small_GTPase_ARF.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   PANTHER; PTHR11711; PTHR11711; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   2: Evidence at transcript level;
KW   ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Myristate;
KW   Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..181
FT                   /note="ADP-ribosylation factor 2-B"
FT                   /id="PRO_0000415772"
FT   BINDING         24..31
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         67..71
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         126..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   181 AA;  20593 MW;  680408BADE96034A CRC64;
     MGLSFAKLFS RLFAKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
     ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRDRV VEARDELHRM LNEDELRDAV
     LLVFANKQDL PNAMNAAEIT DKLGLHSLRQ RHWYIQSTCA TSGEGLYEGL DWLSNNIAGK
     A
 
 
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