AEL2_ARATH
ID AEL2_ARATH Reviewed; 149 AA.
AC Q9SR25; F4IZX5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein AE7-like 2 {ECO:0000303|PubMed:23104832};
DE AltName: Full=MIP18 family protein At3g09380 {ECO:0000305};
GN Name=AEL2 {ECO:0000303|PubMed:23104832};
GN OrderedLocusNames=At3g09380 {ECO:0000312|Araport:AT3G09380};
GN ORFNames=F3L24.26 {ECO:0000312|EMBL:AAF14033.1};
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;
RN [1]
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 [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=16244158; DOI=10.1104/pp.105.063479;
RA Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT reveals numerous transcript variants.";
RL Plant Physiol. 139:1323-1337(2005).
RN [4]
RP FUNCTION, AND IDENTIFICATION.
RC STRAIN=cv. Columbia;
RX PubMed=23104832; DOI=10.1105/tpc.112.102608;
RA Luo D., Bernard D.G., Balk J., Hai H., Cui X.;
RT "The DUF59 family gene AE7 acts in the cytosolic iron-sulfur cluster
RT assembly pathway to maintain nuclear genome integrity in Arabidopsis.";
RL Plant Cell 24:4135-4148(2012).
CC -!- FUNCTION: May play a role in chromosome segregation through
CC establishment of sister chromatid cohesion (By similarity). Unable to
CC complement ae7 mutants, and thus probably not involved in the cytosolic
CC iron-sulfur assembly (CIA) pathway (PubMed:23104832).
CC {ECO:0000250|UniProtKB:Q9D187, ECO:0000269|PubMed:23104832}.
CC -!- SIMILARITY: Belongs to the MIP18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF14033.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC011436; AAF14033.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE74759.2; -; Genomic_DNA.
DR EMBL; EG498918; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_187549.2; NM_111772.3.
DR AlphaFoldDB; Q9SR25; -.
DR SMR; Q9SR25; -.
DR STRING; 3702.AT3G09380.1; -.
DR PaxDb; Q9SR25; -.
DR PRIDE; Q9SR25; -.
DR EnsemblPlants; AT3G09380.1; AT3G09380.1; AT3G09380.
DR GeneID; 820096; -.
DR Gramene; AT3G09380.1; AT3G09380.1; AT3G09380.
DR KEGG; ath:AT3G09380; -.
DR Araport; AT3G09380; -.
DR eggNOG; KOG3381; Eukaryota.
DR HOGENOM; CLU_075876_3_1_1; -.
DR InParanoid; Q9SR25; -.
DR OMA; XNKQIND; -.
DR OrthoDB; 1408004at2759; -.
DR PhylomeDB; Q9SR25; -.
DR PRO; PR:Q9SR25; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SR25; baseline and differential.
DR Genevisible; Q9SR25; AT.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IEA:InterPro.
DR Gene3D; 3.30.300.130; -; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR039796; MIP18.
DR InterPro; IPR002744; MIP18-like.
DR PANTHER; PTHR12377; PTHR12377; 1.
DR Pfam; PF01883; FeS_assembly_P; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
PE 2: Evidence at transcript level;
KW Chromosome partition; Reference proteome.
FT CHAIN 1..149
FT /note="Protein AE7-like 2"
FT /id="PRO_0000212697"
SQ SEQUENCE 149 AA; 16989 MW; 5ECB87D04C9D4192 CRC64;
MDSVLTNKNP IIYPKRTRRY RTDQSSTDEF SSTNRIRDIK DPEHPELSLE DLNVLTEESV
EVDDHKSYVR ITFTPTLPHC HLPTHIGLCI LVKLVQSLPA RFKVDVRVAP GSHDKETTVN
KQLGDKERVT AALENPELVA LLNKMMQVC
