AIR12_ARATH
ID AIR12_ARATH Reviewed; 252 AA.
AC Q94BT2; F4JEF2; O82442; Q9SRS7;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Auxin-induced in root cultures protein 12;
DE Flags: Precursor;
GN Name=AIR12; OrderedLocusNames=At3g07390; ORFNames=F21O3_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], INDUCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. C24; TISSUE=Cultured root;
RX PubMed=10080694; DOI=10.1023/a:1006104205959;
RA Neuteboom L.W., Ng J.M.Y., Kuyper M., Clijdesdale O.R., Hooykaas P.J.J.,
RA van der Zaal B.J.;
RT "Isolation and characterization of cDNA clones corresponding with mRNAs
RT that accumulate during auxin-induced lateral root formation.";
RL Plant Mol. Biol. 39:273-287(1999).
RN [2]
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 [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] OF 8-252.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [6]
RP INDUCTION BY AUXIN.
RX PubMed=16621846; DOI=10.1093/pcp/pcj043;
RA Laskowski M., Biller S., Stanley K., Kajstura T., Prusty R.;
RT "Expression profiling of auxin-treated Arabidopsis roots: toward a
RT molecular analysis of lateral root emergence.";
RL Plant Cell Physiol. 47:788-792(2006).
RN [7]
RP COFACTOR, FUNCTION, AND DOMAIN.
RX PubMed=19386804; DOI=10.1104/pp.109.139170;
RA Preger V., Tango N., Marchand C., Lemaire S.D., Carbonera D.,
RA Di Valentin M., Costa A., Pupillo P., Trost P.;
RT "Auxin-responsive genes AIR12 code for a new family of plasma membrane b-
RT type cytochromes specific to flowering plants.";
RL Plant Physiol. 150:606-620(2009).
CC -!- FUNCTION: One-heme-containing cytochrome.
CC {ECO:0000305|PubMed:19386804}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000305};
CC Note=Binds 1 heme group non-covalently. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- DEVELOPMENTAL STAGE: Expressed during auxin-induced lateral root
CC formation. {ECO:0000269|PubMed:10080694}.
CC -!- INDUCTION: Induced between 4 and 8 hours after treatment with auxin and
CC remains high for at least 24 hours. {ECO:0000269|PubMed:10080694,
CC ECO:0000269|PubMed:16621846}.
CC -!- DOMAIN: DOMON domain could bind one heme b.
CC {ECO:0000269|PubMed:19386804}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62613.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK64012.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AEE74537.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF055850; AAC62613.1; ALT_INIT; mRNA.
DR EMBL; AC009853; AAF02148.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74537.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY039908; AAK64012.2; ALT_INIT; mRNA.
DR EMBL; AY077679; AAL76157.1; -; mRNA.
DR PIR; T51337; T51337.
DR RefSeq; NP_566306.3; NM_111618.3.
DR AlphaFoldDB; Q94BT2; -.
DR STRING; 3702.AT3G07390.1; -.
DR iPTMnet; Q94BT2; -.
DR PaxDb; Q94BT2; -.
DR PRIDE; Q94BT2; -.
DR ProteomicsDB; 245010; -.
DR EnsemblPlants; AT3G07390.1; AT3G07390.1; AT3G07390.
DR GeneID; 819927; -.
DR Gramene; AT3G07390.1; AT3G07390.1; AT3G07390.
DR KEGG; ath:AT3G07390; -.
DR Araport; AT3G07390; -.
DR eggNOG; KOG4293; Eukaryota.
DR HOGENOM; CLU_036675_2_0_1; -.
DR InParanoid; Q94BT2; -.
DR OrthoDB; 599276at2759; -.
DR PhylomeDB; Q94BT2; -.
DR PRO; PR:Q94BT2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94BT2; baseline and differential.
DR Genevisible; Q94BT2; AT.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd09629; DOMON_CIL1_like; 1.
DR InterPro; IPR045265; AIR12_DOMON.
DR InterPro; IPR005018; DOMON_domain.
DR Pfam; PF04526; DUF568; 1.
DR PROSITE; PS50836; DOMON; 1.
PE 1: Evidence at protein level;
KW Auxin signaling pathway; Cell membrane; Electron transport; Glycoprotein;
KW GPI-anchor; Heme; Iron; Lipoprotein; Membrane; Metal-binding;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..226
FT /note="Auxin-induced in root cultures protein 12"
FT /id="PRO_0000020655"
FT PROPEP 227..252
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000020656"
FT DOMAIN 49..165
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT REGION 193..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 176
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT LIPID 226
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 147
FT /note="T -> NR (in Ref. 1; AAC62613)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="A -> R (in Ref. 1; AAC62613)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="P -> PSPGSAP (in Ref. 1; AAC62613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 252 AA; 25592 MW; DB20541FE856E603 CRC64;
MASSSSSLLI LAVACFVSLI SPAISQQACK SQNLNSAGPF DSCEDLPVLN SYLHYTYNSS
NSSLSVAFVA TPSQANGGWV AWAINPTGTK MAGSQAFLAY RSGGGAAPVV KTYNISSYSS
LVEGKLAFDF WNLRAESLSG GRIAIFTTVK VPAGADSVNQ VWQIGGNVTN GRPGVHPFGP
DNLGSHRVLS FTEDAAPGSA PSPGSAPAPG TSGSTTPGTA AGGPGNAGSL TRNVNFGVNL
GILVLLGSIF IF
