AUG5_ARATH
ID AUG5_ARATH Reviewed; 796 AA.
AC Q9FMB4; Q570F2; Q7XYR0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=AUGMIN subunit 5 {ECO:0000303|PubMed:22505726};
GN Name=AUG5 {ECO:0000303|PubMed:22505726};
GN OrderedLocusNames=At5g38880 {ECO:0000312|Araport:AT5G38880};
GN ORFNames=K15E6.9 {ECO:0000312|EMBL:BAB08644.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-796.
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 FUNCTION, IDENTIFICATION IN THE AUGMIN COMPLEX BY MASS SPECTROMETRY,
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=22505726; DOI=10.1105/tpc.112.096610;
RA Hotta T., Kong Z., Ho C.M., Zeng C.J., Horio T., Fong S., Vuong T.,
RA Lee Y.R., Liu B.;
RT "Characterization of the Arabidopsis augmin complex uncovers its critical
RT function in the assembly of the acentrosomal spindle and phragmoplast
RT microtubule arrays.";
RL Plant Cell 24:1494-1509(2012).
CC -!- FUNCTION: Involved in microtubules reorganization during spindle and
CC phragmoplast development. {ECO:0000269|PubMed:22505726}.
CC -!- SUBUNIT: Part of the augmin complex composed of 8 subunits. The complex
CC acts on microtubules and interacts with gamma-tubulin in spindles and
CC the phragmoplast. {ECO:0000269|PubMed:22505726}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:22505726}. Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:22505726}. Note=Preferentially localizes to
CC microtubules minus ends. {ECO:0000269|PubMed:22505726}.
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC {ECO:0000269|PubMed:22505726}.
CC -!- SIMILARITY: Belongs to the HAUS5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93943.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB009048; BAB08644.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94368.1; -; Genomic_DNA.
DR EMBL; AK227777; BAE99759.1; -; mRNA.
DR EMBL; AK220756; BAD93943.1; ALT_INIT; mRNA.
DR EMBL; BT009661; AAP78929.1; -; mRNA.
DR RefSeq; NP_198704.2; NM_123249.3.
DR AlphaFoldDB; Q9FMB4; -.
DR SMR; Q9FMB4; -.
DR STRING; 3702.AT5G38880.1; -.
DR iPTMnet; Q9FMB4; -.
DR PaxDb; Q9FMB4; -.
DR PRIDE; Q9FMB4; -.
DR ProteomicsDB; 240915; -.
DR EnsemblPlants; AT5G38880.1; AT5G38880.1; AT5G38880.
DR GeneID; 833879; -.
DR Gramene; AT5G38880.1; AT5G38880.1; AT5G38880.
DR KEGG; ath:AT5G38880; -.
DR Araport; AT5G38880; -.
DR TAIR; locus:2152287; AT5G38880.
DR eggNOG; ENOG502QRA2; Eukaryota.
DR HOGENOM; CLU_019917_0_0_1; -.
DR InParanoid; Q9FMB4; -.
DR OMA; PHEDHFG; -.
DR OrthoDB; 277862at2759; -.
DR PhylomeDB; Q9FMB4; -.
DR PRO; PR:Q9FMB4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMB4; baseline and differential.
DR Genevisible; Q9FMB4; AT.
DR GO; GO:0070652; C:HAUS complex; IEA:InterPro.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005876; C:spindle microtubule; IDA:TAIR.
DR GO; GO:0051011; F:microtubule minus-end binding; IDA:TAIR.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051225; P:spindle assembly; IEA:InterPro.
DR InterPro; IPR044706; AUG5_plant.
DR InterPro; IPR029131; HAUS5.
DR PANTHER; PTHR34968; PTHR34968; 2.
DR Pfam; PF14817; HAUS5; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Reference proteome.
FT CHAIN 1..796
FT /note="AUGMIN subunit 5"
FT /id="PRO_0000434096"
FT REGION 79..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 115..191
FT /evidence="ECO:0000255"
FT COILED 462..501
FT /evidence="ECO:0000255"
FT COMPBIAS 79..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 89181 MW; 010A0E287DB336F4 CRC64;
MQSLSSSAPT PEAILEWLQK EMGYRQLGPY NGSSKSHVPS IDAIRKICRG NMIPIWNFLI
NRVKSEKTVE RIRRNITVHG GSSNASIGSS VNPGKEESKS KGRRKDKTVT GESSSYAEDR
EAALQERELA AKEVERLRNI VRRQRKDLKA RMLEVSREEA ERKRMLDERA NYRHKQALLE
AYDQQCDEAT RIFAEYHKRL QVYVNQANDA QRSVNSSNEV LSSLSANSER EAVYSTVKGT
KSADDVILME TTRERNIRIV CDLLASRMIE RIRNSFPAYE GNGICSLPEL ETAKLGFEYD
GEITDEMKTV IVNSLRGPPL LLQAIAAYTL RIKTLISREM EKIDVRADAE MLRYKFENNR
VTDNSSSDVS SPLSYQFNGN GKIGTDTHFQ GSNNQLLERQ KAHVQQFLAT EDALNKAAEA
RDLCHKFINR LHGSADTATH SFVGGTTQSG SNLRQFELDV WGKEREAAGL RASLNTLLSE
IQRLNKLCAE RKEAEDSLKK KWKKIEEFDA RRSELETIYT TLLKANMDAV AFWNQQPLAA
REYASATVIP ASEVVVDISN SAKDFIEKEV SAFFQSPDNS LYMLPATPQG LLESMGANGS
TGPEAVAYAE KNAALLTARA GARDPSAIPS ICRISAALQY PAGLEGSDAS LASVLESLEF
CLRVRGSEAC VLEDLAKAID LVHIRQDLVE SGHSLLDHAF RAQQKYERTT NYCLDLASEQ
ENTISDQWLP ELRTAVQNAQ ASSEHCKYVR GLLDEWWEQP ASTVVDWVTV DGQSVAAWQN
HVKQLLAFYD KESLRT
