ATG1B_ARATH
ID ATG1B_ARATH Reviewed; 711 AA.
AC F4JBP3; Q8GWX7; Q9M334;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Serine/threonine-protein kinase ATG1b {ECO:0000305};
DE EC=2.7.11.-;
DE AltName: Full=Autophagy-related protein 1b {ECO:0000303|PubMed:12114572};
DE Short=AtAPG1b {ECO:0000303|PubMed:12114572};
GN Name=ATG1B {ECO:0000303|PubMed:17204848};
GN OrderedLocusNames=At3g53930 {ECO:0000312|Araport:AT3G53930};
GN ORFNames=F5K20_230 {ECO:0000312|EMBL:CAB88355.1};
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=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] OF 53-711.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
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 [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17204848; DOI=10.4161/auto.3595;
RA Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT "ATG genes involved in non-selective autophagy are conserved from yeast to
RT man, but the selective Cvt and pexophagy pathways also require organism-
RT specific genes.";
RL Autophagy 3:106-116(2007).
CC -!- FUNCTION: Serine/threonine protein kinase involved in autophagy. The
CC ATG1-ATG13 protein kinase complex regulates downstream events required
CC for autophagosome enclosure and/or vacuolar delivery.
CC {ECO:0000250|UniProtKB:Q94C95}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC {ECO:0000250|UniProtKB:Q94C95}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=F4JBP3-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO64880.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB88355.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL132960; CAB88355.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79160.1; -; Genomic_DNA.
DR EMBL; BT005945; AAO64880.1; ALT_INIT; mRNA.
DR EMBL; AK118572; BAC43172.1; -; mRNA.
DR PIR; T45933; T45933.
DR RefSeq; NP_190961.2; NM_115253.3. [F4JBP3-1]
DR AlphaFoldDB; F4JBP3; -.
DR SMR; F4JBP3; -.
DR IntAct; F4JBP3; 1.
DR STRING; 3702.AT3G53930.2; -.
DR iPTMnet; F4JBP3; -.
DR PaxDb; F4JBP3; -.
DR PRIDE; F4JBP3; -.
DR EnsemblPlants; AT3G53930.1; AT3G53930.1; AT3G53930. [F4JBP3-1]
DR GeneID; 824560; -.
DR Gramene; AT3G53930.1; AT3G53930.1; AT3G53930. [F4JBP3-1]
DR KEGG; ath:AT3G53930; -.
DR Araport; AT3G53930; -.
DR eggNOG; KOG0595; Eukaryota.
DR OMA; SPHCIDL; -.
DR PRO; PR:F4JBP3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4JBP3; baseline and differential.
DR Genevisible; F4JBP3; AT.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:1905037; P:autophagosome organization; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR045269; Atg1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24348; PTHR24348; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Autophagy; Cytoplasmic vesicle; Kinase;
KW Nucleotide-binding; Protein transport; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transport.
FT CHAIN 1..711
FT /note="Serine/threonine-protein kinase ATG1b"
FT /id="PRO_0000434620"
FT DOMAIN 20..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 318..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 421..424
FT /note="AIM (Atg8-family-interacting motif)"
FT /evidence="ECO:0000250|UniProtKB:Q94C95"
FT COMPBIAS 328..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 711 AA; 78798 MW; F5309F7A21C5077C CRC64;
MAQSSLVAAA GRSGRVIGDY AVGRQIGSGS FSVVWEGRHL VHGTVVAIKE IAMARLNKKL
QESLMSEIII LRKINHPNII RFIDMIEAPG KINLVLEYCK GGDLSMYIHK HGSVPEATAK
HFMLQLAAGL QVLRDNNIIH RDLKPQNLLL STDDNDAALK IADFGFARSL QPRGLAETLC
GSPLYMAPEI MQLQKYDAKA DLWSVGAILF QLVTGRTPFT GNSQIQLLQN IIRSTELHFP
ADCRDLSTDC KDLCQKLLRR NPVERLTFEE FFHHPFLSDK QSYDFTRSRL DSRTMNDFHS
SGSSPSRNIE EISQEDGLPF FLDDDSSGPE GSPSSFKHTS PMKSSYGFSV ERREAALSPL
KNMDLSSRYS RVSHRAETNN FKFEGHRLSD RSQFKPSSLP DSRSFSTQGR GDSPDSMDQD
YVLISGPPVD IPSSSSGSPK PFNYPFKSHS PPVEFIKRNV TNLTAPMPIA SATGNNLSRF
GSLESQNCIP GTSHGSLDLV DAFEQPSTNS LTRIRSLQKC AAAIAELVHE RGENGKHLEA
FSIQLVILAI WNQALHICHT QAVSGIEGSL LQDINRVGRN ISHGGSEKLL PQIQKEFVQE
VERAEELAKF VESDNAKMPD AMEMILQAAL ALGISGGVDE VMGDAENAGN LYSKAVRLLV
FLAVEAQTLI LNPPLTLTNS VRYRLRTYID SLITRLKHLQ SHRRTSYPQK Q
