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AUG1_ARATH
ID   AUG1_ARATH              Reviewed;         299 AA.
AC   F4IK01; Q9ZVC0;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=AUGMIN subunit 1 {ECO:0000303|PubMed:22505726};
GN   Name=AUG1 {ECO:0000303|PubMed:22505726};
GN   OrderedLocusNames=At2g41350 {ECO:0000312|Araport:AT2G41350};
GN   ORFNames=F13H10.10 {ECO:0000312|EMBL:AAC78538.2};
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 {ECO:0000312|Proteomes:UP000006548};
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   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000312|Proteomes:UP000006548};
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] (ISOFORM 2).
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] (ISOFORM 2).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-299 (ISOFORM 1).
RA   Wrobel R.L., Kimball T.L., Riters M.A., Steffen E., Thao S., Aceti D.J.,
RA   Blommel P.G., Newman C.S., Zhao Q., Fox B.G., Phillips G.N., Markley J.L.;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH AUG3.
RX   PubMed=21750235; DOI=10.1105/tpc.111.086892;
RA   Ho C.M., Hotta T., Kong Z., Zeng C.J., Sun J., Lee Y.R., Liu B.;
RT   "Augmin plays a critical role in organizing the spindle and phragmoplast
RT   microtubule arrays in Arabidopsis.";
RL   Plant Cell 23:2606-2618(2011).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [8]
RP   FUNCTION, IDENTIFICATION IN THE AUGMIN COMPLEX BY MASS SPECTROMETRY, AND
RP   DISRUPTION PHENOTYPE.
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
CC       (PubMed:22505726). The complex acts on microtubules and interacts with
CC       gamma-tubulin in spindles and the phragmoplast (PubMed:22505726).
CC       Interacts with AUG3 (PubMed:21750235). {ECO:0000269|PubMed:21750235,
CC       ECO:0000269|PubMed:22505726}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:21750235}. Cytoplasm, cytoskeleton, phragmoplast
CC       {ECO:0000269|PubMed:21750235}. Note=Preferentially localizes to
CC       microtubules minus ends. {ECO:0000269|PubMed:21750235}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=F4IK01-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F4IK01-2; Sequence=VSP_057898;
CC   -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC       {ECO:0000269|PubMed:22505726}.
CC   -!- SIMILARITY: Belongs to the HAUS1 family. {ECO:0000305}.
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DR   EMBL; AC005662; AAC78538.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09963.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09964.1; -; Genomic_DNA.
DR   EMBL; AY075602; AAL91618.1; -; mRNA.
DR   EMBL; AY143923; AAN28862.1; -; mRNA.
DR   EMBL; AY084814; AAM61380.1; -; mRNA.
DR   EMBL; BT015461; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; F84840; F84840.
DR   RefSeq; NP_001031524.1; NM_001036447.2. [F4IK01-1]
DR   RefSeq; NP_565949.1; NM_129698.3. [F4IK01-2]
DR   AlphaFoldDB; F4IK01; -.
DR   SMR; F4IK01; -.
DR   IntAct; F4IK01; 14.
DR   STRING; 3702.AT2G41350.2; -.
DR   iPTMnet; F4IK01; -.
DR   PaxDb; F4IK01; -.
DR   PRIDE; F4IK01; -.
DR   ProteomicsDB; 240926; -. [F4IK01-1]
DR   EnsemblPlants; AT2G41350.1; AT2G41350.1; AT2G41350. [F4IK01-2]
DR   EnsemblPlants; AT2G41350.2; AT2G41350.2; AT2G41350. [F4IK01-1]
DR   GeneID; 818733; -.
DR   Gramene; AT2G41350.1; AT2G41350.1; AT2G41350. [F4IK01-2]
DR   Gramene; AT2G41350.2; AT2G41350.2; AT2G41350. [F4IK01-1]
DR   KEGG; ath:AT2G41350; -.
DR   Araport; AT2G41350; -.
DR   TAIR; locus:2040247; AT2G41350.
DR   eggNOG; ENOG502QSQA; Eukaryota.
DR   HOGENOM; CLU_077821_0_0_1; -.
DR   InParanoid; F4IK01; -.
DR   OMA; YQAEGAH; -.
DR   OrthoDB; 1350537at2759; -.
DR   PhylomeDB; F4IK01; -.
DR   PRO; PR:F4IK01; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; F4IK01; baseline and differential.
DR   Genevisible; F4IK01; AT.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0070652; C:HAUS complex; IEA:InterPro.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IDA:TAIR.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR   InterPro; IPR026243; HAUS1.
DR   PANTHER; PTHR31570; PTHR31570; 1.
DR   PRINTS; PR02087; HAUSAUGMINL1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..299
FT                   /note="AUGMIN subunit 1"
FT                   /id="PRO_0000434091"
FT   COILED          76..96
FT                   /evidence="ECO:0000255"
FT   COILED          164..184
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   VAR_SEQ         217
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_057898"
SQ   SEQUENCE   299 AA;  33622 MW;  569140C498F949D6 CRC64;
     MSDVTGDLAA VSEAKGGSDA ARISEVKAWL TSQFEAVGKE VPNFEYTHRS ITHLYNLATA
     SQAKSQAATI VANDFRLKAS EYRAQAARIR EILESAGMSQ ESLPSNVVSS AQVLANVANL
     LNIRDTELSS FLVAMGDISL RKTGVEEKRA KAQKESNALL DYTRKAIQRL TYLKKILAQL
     EDDVVPCESQ MENWKTNLEV MAVKEEQYIQ QYKKYEQMLL NRVGYTPKIS HRELVEMAEH
     RKELDKMTKP VLDTLRSYQD LPPDKALAAL AIEDKKRQFT AAEKYLEEVL QSALETNDE
 
 
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