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ARF5_ARATH
ID   ARF5_ARATH              Reviewed;         185 AA.
AC   Q9ZPX1; Q547H2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=ADP-ribosylation factor-like protein 2;
DE   AltName: Full=Protein ARF-like 2;
DE   AltName: Full=Protein HALLIMASCH;
DE   AltName: Full=Protein TITAN 5;
GN   Name=ARL2; Synonyms=HAL, TTN5; OrderedLocusNames=At2g18390;
GN   ORFNames=T30D6.10;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Landsberg erecta, and cv. Wassilewskija; TISSUE=Flower;
RX   PubMed=11959844; DOI=10.1101/gad.221702;
RA   Steinborn K., Maulbetsch C., Priester B., Trautmann S., Pacher T.,
RA   Geiges B., Kuettner F., Lepiniec L., Stierhof Y.-D., Schwarz H.,
RA   Juergens G., Mayer U.;
RT   "The Arabidopsis PILZ group genes encode tubulin-folding cofactor orthologs
RT   required for cell division but not cell growth.";
RL   Genes Dev. 16:959-971(2002).
RN   [2]
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   [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].
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   [5]
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   [6]
RP   FUNCTION.
RX   PubMed=10099932; DOI=10.1016/s0171-9335(99)80011-9;
RA   Mayer U., Herzog U., Berger F., Inze D., Juergens G.;
RT   "Mutations in the pilz group genes disrupt the microtubule cytoskeleton and
RT   uncouple cell cycle progression from cell division in Arabidopsis embryo
RT   and endosperm.";
RL   Eur. J. Cell Biol. 78:100-108(1999).
RN   [7]
RP   FUNCTION, IDENTIFICATION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=10948257; DOI=10.2307/3871137;
RA   McElver J., Patton D., Rumbaugh M., Liu C., Yang L.J., Meinke D.;
RT   "The TITAN5 gene of Arabidopsis encodes a protein related to the ADP
RT   ribosylation factor family of GTP binding proteins.";
RL   Plant Cell 12:1379-1392(2000).
CC   -!- FUNCTION: Has a role in the cofactor-dependent pathway of microtubule
CC       biogenesis. Not essential for cell viability. May play a regulatory
CC       role in sequestring TFCD. {ECO:0000269|PubMed:10099932,
CC       ECO:0000269|PubMed:10948257, ECO:0000269|PubMed:11959844}.
CC   -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC       function by capturing and stabilizing tubulin in a quasi-native
CC       conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC       interaction with cofactor C then causes the release of tubulin
CC       polypeptides that are committed to the native state (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, roots and
CC       inflorescences. {ECO:0000269|PubMed:10948257}.
CC   -!- DISRUPTION PHENOTYPE: Embryo lethality. Embryo development limited to
CC       the formation of a few giant cells lacking microtubules but not actin
CC       filaments. Failure to localize KNOLLE in mitotic cells. Giant nuclei
CC       and nucleoli found in both the embryo and endosperm tissue.
CC       {ECO:0000269|PubMed:10948257, ECO:0000269|PubMed:11959844}.
CC   -!- MISCELLANEOUS: Belongs to the PILZ group of genes that disrupt, when
CC       mutated, the microtubule cytoskeleton and produce mushroom-shaped
CC       ('pilz' in German) embryos.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
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DR   EMBL; AF486852; AAM22961.1; -; mRNA.
DR   EMBL; AC006439; AAD15498.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06764.1; -; Genomic_DNA.
DR   EMBL; AY035009; AAK59514.1; -; mRNA.
DR   EMBL; AY063048; AAL34222.1; -; mRNA.
DR   EMBL; AY088331; AAM65870.1; -; mRNA.
DR   PIR; G84563; G84563.
DR   RefSeq; NP_179430.1; NM_127396.3.
DR   AlphaFoldDB; Q9ZPX1; -.
DR   SMR; Q9ZPX1; -.
DR   STRING; 3702.AT2G18390.1; -.
DR   PaxDb; Q9ZPX1; -.
DR   PRIDE; Q9ZPX1; -.
DR   ProteomicsDB; 241024; -.
DR   EnsemblPlants; AT2G18390.1; AT2G18390.1; AT2G18390.
DR   GeneID; 816354; -.
DR   Gramene; AT2G18390.1; AT2G18390.1; AT2G18390.
DR   KEGG; ath:AT2G18390; -.
DR   Araport; AT2G18390; -.
DR   TAIR; locus:2062085; AT2G18390.
DR   eggNOG; KOG0073; Eukaryota.
DR   HOGENOM; CLU_040729_12_3_1; -.
DR   InParanoid; Q9ZPX1; -.
DR   OMA; EHRGYKL; -.
DR   OrthoDB; 1271528at2759; -.
DR   PhylomeDB; Q9ZPX1; -.
DR   PRO; PR:Q9ZPX1; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZPX1; baseline and differential.
DR   Genevisible; Q9ZPX1; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; ISS:TAIR.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0009558; P:embryo sac cellularization; IMP:TAIR.
DR   GO; GO:0009960; P:endosperm development; IMP:TAIR.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0007021; P:tubulin complex assembly; ISS:TAIR.
DR   CDD; cd04154; Arl2; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR045873; Arl2.
DR   InterPro; IPR044612; ARL2/3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   PANTHER; PTHR45697; PTHR45697; 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   Cytoplasm; GTP-binding; Lipoprotein; Myristate; Nucleotide-binding;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..185
FT                   /note="ADP-ribosylation factor-like protein 2"
FT                   /id="PRO_0000207430"
FT   BINDING         23..30
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..70
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         125..128
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   185 AA;  21077 MW;  7A467C0ADA0D10F2 CRC64;
     MGLLSIIRKI KKKEKEMRIL MVGLDNSGKT TIVLKINGED TSVISPTLGF NIKTIIYQKY
     TLNIWDVGGQ KTIRSYWRNY FEQTDGLVWV VDSSDLRRLD DCKMELDNLL KEERLAGSSL
     LILANKQDIQ GALTPDEIGK VLNLESMDKS RHWKIVGCSA YTGEGLLEGF DWLVQDIASR
     IYMLD
 
 
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