ATI1_ARATH
ID ATI1_ARATH Reviewed; 256 AA.
AC O82775; Q8LEV1; Q94K87;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=ATG8-interacting protein 1 {ECO:0000303|PubMed:22253227};
GN Name=ATI1 {ECO:0000303|PubMed:22253227};
GN OrderedLocusNames=At2g45980 {ECO:0000312|Araport:AT2G45980};
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=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;
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=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].
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 AIM MOTIF.
RX PubMed=20083108; DOI=10.1016/j.febslet.2010.01.018;
RA Noda N.N., Ohsumi Y., Inagaki F.;
RT "Atg8-family interacting motif crucial for selective autophagy.";
RL FEBS Lett. 584:1379-1385(2010).
RN [6]
RP FUNCTION, INTERACTION WITH ATG8F, AND SUBCELLULAR LOCATION.
RX PubMed=22253227; DOI=10.1105/tpc.111.093112;
RA Honig A., Avin-Wittenberg T., Ufaz S., Galili G.;
RT "A new type of compartment, defined by plant-specific Atg8-interacting
RT proteins, is induced upon exposure of Arabidopsis plants to carbon
RT starvation.";
RL Plant Cell 24:288-303(2012).
RN [7]
RP INTERACTION WITH ATG8F AND ATG8H.
RX PubMed=22580699; DOI=10.4161/psb.20030;
RA Avin-Wittenberg T., Michaeli S., Honig A., Galili G.;
RT "ATI1, a newly identified atg8-interacting protein, binds two different
RT Atg8 homologs.";
RL Plant Signal. Behav. 7:685-687(2012).
RN [8]
RP FUNCTION, INTERACTION WITH APE1 AND PSBS/NPQ4, SUBCELLULAR LOCATION, AND
RP INDUCTION BY SALT STRESS.
RX PubMed=25281689; DOI=10.1105/tpc.114.129999;
RA Michaeli S., Honig A., Levanony H., Peled-Zehavi H., Galili G.;
RT "Arabidopsis ATG8-INTERACTING PROTEIN1 is involved in autophagy-dependent
RT vesicular trafficking of plastid proteins to the vacuole.";
RL Plant Cell 26:4084-4101(2014).
CC -!- FUNCTION: Involved in a special stress-induced plastid-to-vacuole
CC protein trafficking pathway. Interacts with ATG8F in plastid bodies to
CC subsequently enable their delivery to the vacuole by an autophagic
CC pathway. Interacts with the plastid proteins APE1 and PSBS/NPQ4 and may
CC recruit them as cargo into plastid bodies that may be recognized by the
CC autophagy machinery for degradation in the vacuole. Involved in the
CC alleviation of damage caused by salt stress during plant development,
CC probably through its involvement in plastid-to-vacuole and ER-to-
CC vacuole trafficking (PubMed:25281689). Plays a role in seed germination
CC in response to exogenous abscisic acid (ABA) treatment
CC (PubMed:22253227). {ECO:0000269|PubMed:22253227,
CC ECO:0000269|PubMed:25281689}.
CC -!- SUBUNIT: Interacts with ATG8F (PubMed:22253227, PubMed:22580699).
CC Interacts with ATG8H (PubMed:22580699). Interacts with APE1 and
CC PSBS/NPQ4 (PubMed:25281689). {ECO:0000269|PubMed:22253227,
CC ECO:0000269|PubMed:22580699, ECO:0000269|PubMed:25281689}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22253227}; Single-pass membrane protein
CC {ECO:0000255}. Membrane {ECO:0000255}; Single-pass membrane protein
CC {ECO:0000255}. Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:25281689}. Note=Under favorable growth conditions,
CC partially associated with the endoplasmic reticulum (ER) membrane
CC network. Upon exposure to carbon starvation, mainly associated with
CC newly identified spherical compartments that dynamically move along the
CC ER network and reach the lytic vacuole (PubMed:22253227). Under carbon
CC starvation, salt stress and during senescence, localized to novel
CC plastid-associated bodies that are transported to vesicles. These
CC plastid bodises are morphologically distinct from the ER-associated
CC bodies (PubMed:25281689). {ECO:0000269|PubMed:22253227,
CC ECO:0000269|PubMed:25281689}.
CC -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:25281689}.
CC -!- MISCELLANEOUS: Plants over-expressing ATI1 display increased ability of
CC seed germination in presence of exogenous abscisic acid (ABA). Plants
CC silencing ATI1 and ATI2 display decreased ability of seed germination
CC in presence of exogenous ABA. {ECO:0000269|PubMed:22253227}.
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DR EMBL; AC004665; AAM14974.1; -; Genomic_DNA.
DR EMBL; AC005397; AAC62904.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10626.1; -; Genomic_DNA.
DR EMBL; AF370190; AAK44005.1; -; mRNA.
DR EMBL; AY062947; AAL33779.1; -; mRNA.
DR EMBL; AY085218; AAM62451.1; -; mRNA.
DR PIR; T02449; T02449.
DR RefSeq; NP_566059.1; NM_130161.3.
DR AlphaFoldDB; O82775; -.
DR IntAct; O82775; 6.
DR STRING; 3702.AT2G45980.1; -.
DR iPTMnet; O82775; -.
DR PaxDb; O82775; -.
DR PRIDE; O82775; -.
DR ProteomicsDB; 246559; -.
DR EnsemblPlants; AT2G45980.1; AT2G45980.1; AT2G45980.
DR GeneID; 819206; -.
DR Gramene; AT2G45980.1; AT2G45980.1; AT2G45980.
DR KEGG; ath:AT2G45980; -.
DR Araport; AT2G45980; -.
DR TAIR; locus:2062922; AT2G45980.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_054659_0_0_1; -.
DR InParanoid; O82775; -.
DR OMA; DVEMMMG; -.
DR OrthoDB; 1332505at2759; -.
DR PhylomeDB; O82775; -.
DR PRO; PR:O82775; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82775; baseline and differential.
DR Genevisible; O82775; AT.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:1904962; P:plastid to vacuole vesicle-mediated transport; IDA:TAIR.
DR GO; GO:0071211; P:protein targeting to vacuole involved in autophagy; IPI:TAIR.
DR InterPro; IPR040304; ATG8-IP-1/2.
DR PANTHER; PTHR34797; PTHR34797; 1.
PE 1: Evidence at protein level;
KW Autophagy; Chloroplast; Endoplasmic reticulum; Membrane; Plastid;
KW Protein transport; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..256
FT /note="ATG8-interacting protein 1"
FT /id="PRO_0000434630"
FT TRANSMEM 181..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 14..17
FT /note="AIM (Atg8-family-interacting motif)"
FT /evidence="ECO:0000305|PubMed:20083108"
FT MOTIF 208..211
FT /note="AIM (Atg8-family-interacting motif)"
FT /evidence="ECO:0000305|PubMed:20083108"
FT CONFLICT 57
FT /note="E -> Q (in Ref. 4; AAM62451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 256 AA; 28844 MW; 22EB8C208CE91749 CRC64;
MANNEEHPPR GNEWEVVSLT SSAYAAAPGP YNVESRDVRK YDAYYGAETS RDLYMSEHFV
FPPSEHENLP IDESLFVAEQ RKDGRDLMLE GQGLSDQFHY EAGNNQQSIY GESALGSSRH
MESFGSESAV YEHGLVDAEG NLDLHSDGEG EKDVKKSTHN LPCEAWWKRR AISMYSRTRE
ANAIWSLFFA AAVTGLVVLG QRWQQERWQV LQLKWQSSIS SEKLGRVLEP LSRLKDVIVR
SNPQASLVRS GSSSEV
