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ATG8H_ARATH
ID   ATG8H_ARATH             Reviewed;         119 AA.
AC   Q8S925; Q9SQU5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Autophagy-related protein 8h;
DE   AltName: Full=Autophagy-related ubiquitin-like modifier ATG8h;
DE            Short=AtAPG8h;
DE            Short=Protein autophagy 8h;
GN   Name=ATG8H; Synonyms=APG8H; OrderedLocusNames=At3g06420;
GN   ORFNames=F24P17.11;
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], NOMENCLATURE, AND GENE FAMILY.
RX   PubMed=12114572; DOI=10.1104/pp.011024;
RA   Hanaoka H., Noda T., Shirano Y., Kato T., Hayashi H., Shibata D.,
RA   Tabata S., Ohsumi Y.;
RT   "Leaf senescence and starvation-induced chlorosis are accelerated by the
RT   disruption of an Arabidopsis autophagy gene.";
RL   Plant Physiol. 129:1181-1193(2002).
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].
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=15494556; DOI=10.1105/tpc.104.025395;
RA   Yoshimoto K., Hanaoka H., Sato S., Kato T., Tabata S., Noda T., Ohsumi Y.;
RT   "Processing of ATG8s, ubiquitin-like proteins, and their deconjugation by
RT   ATG4s are essential for plant autophagy.";
RL   Plant Cell 16:2967-2983(2004).
RN   [8]
RP   INDUCTION.
RX   PubMed=16157655; DOI=10.1093/jxb/eri276;
RA   Slavikova S., Shy G., Yao Y., Glozman R., Levanony H., Pietrokovski S.,
RA   Elazar Z., Galili G.;
RT   "The autophagy-associated Atg8 gene family operates both under favourable
RT   growth conditions and under starvation stresses in Arabidopsis plants.";
RL   J. Exp. Bot. 56:2839-2849(2005).
RN   [9]
RP   INTERACTION WITH ATI1.
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).
CC   -!- FUNCTION: Ubiquitin-like modifier involved in autophagosomes formation.
CC       May mediate the delivery of the autophagosomes to the vacuole via the
CC       microtubule cytoskeleton. {ECO:0000250|UniProtKB:P38182}.
CC   -!- SUBUNIT: Interacts with ATG4 (By similarity). Interacts with ATI1
CC       (PubMed:22580699). {ECO:0000250|UniProtKB:Q9SL04,
CC       ECO:0000269|PubMed:22580699}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC       {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P38182}. Vacuole membrane
CC       {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P38182}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q8LEM4}.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed.
CC       {ECO:0000269|PubMed:15494556}.
CC   -!- INDUCTION: Induced by sugar starvation. {ECO:0000269|PubMed:16157655}.
CC   -!- PTM: Gly-119 forms then a thioester bond with the 'Cys-558' of ATG7
CC       (E1-like activating enzyme) before being transferred to the 'Cys-258'
CC       of ATG3 (the specific E2 conjugating enzyme), in order to be finally
CC       amidated with phosphatidylethanolamine. This lipid modification anchors
CC       ATG8 to autophagosomes. {ECO:0000250|UniProtKB:P38182}.
CC   -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF08574.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB073182; BAB88394.1; -; mRNA.
DR   EMBL; AC011623; AAF08574.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE74390.1; -; Genomic_DNA.
DR   EMBL; AK175289; BAD43052.1; -; mRNA.
DR   EMBL; AK176187; BAD43950.1; -; mRNA.
DR   EMBL; AK176657; BAD44420.1; -; mRNA.
DR   EMBL; BT024566; ABD38905.1; -; mRNA.
DR   EMBL; AY085270; AAM62502.1; -; mRNA.
DR   RefSeq; NP_566283.1; NM_111517.3.
DR   AlphaFoldDB; Q8S925; -.
DR   SMR; Q8S925; -.
DR   STRING; 3702.AT3G06420.1; -.
DR   PaxDb; Q8S925; -.
DR   PRIDE; Q8S925; -.
DR   ProteomicsDB; 246740; -.
DR   EnsemblPlants; AT3G06420.1; AT3G06420.1; AT3G06420.
DR   GeneID; 819816; -.
DR   Gramene; AT3G06420.1; AT3G06420.1; AT3G06420.
DR   KEGG; ath:AT3G06420; -.
DR   Araport; AT3G06420; -.
DR   TAIR; locus:2081051; AT3G06420.
DR   eggNOG; KOG1654; Eukaryota.
DR   HOGENOM; CLU_119276_0_1_1; -.
DR   InParanoid; Q8S925; -.
DR   OMA; FKHRRTF; -.
DR   OrthoDB; 1508198at2759; -.
DR   PhylomeDB; Q8S925; -.
DR   PRO; PR:Q8S925; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8S925; baseline and differential.
DR   Genevisible; Q8S925; AT.
DR   GO; GO:0005776; C:autophagosome; IDA:TAIR.
DR   GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004241; Atg8-like.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10969; PTHR10969; 1.
DR   Pfam; PF02991; ATG8; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Lipoprotein;
KW   Membrane; Microtubule; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation pathway; Vacuole.
FT   CHAIN           1..119
FT                   /note="Autophagy-related protein 8h"
FT                   /id="PRO_0000286919"
FT   LIPID           119
FT                   /note="Phosphatidylethanolamine amidated glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
SQ   SEQUENCE   119 AA;  13884 MW;  25F4AF1E247E02F3 CRC64;
     MGIVVKSFKD QFSSDERLKE SNNIIAKYPD RIPVIIEKYS NADLPDMEKN KYLVPRDMTV
     GHFIHMLSKR MQLDPSKALF VFVHNTLPQT ASRMDSLYNT FKEEDGFLYM CYSTEKTFG
 
 
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