ATG1C_ARATH
ID ATG1C_ARATH Reviewed; 733 AA.
AC F4IRW0; Q5E914; Q8RWS7;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Serine/threonine-protein kinase ATG1c {ECO:0000305};
DE EC=2.7.11.-;
DE AltName: Full=Autophagy-related protein 1c {ECO:0000303|PubMed:12114572};
DE Short=AtAPG1c {ECO:0000303|PubMed:12114572};
GN Name=ATG1C {ECO:0000303|PubMed:17204848};
GN OrderedLocusNames=At2g37840 {ECO:0000312|Araport:AT2G37840};
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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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=2;
CC Name=1;
CC IsoId=F4IRW0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4IRW0-2; Sequence=VSP_057967;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; CP002685; AEC09455.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09456.1; -; Genomic_DNA.
DR EMBL; AY091138; AAM14087.1; -; mRNA.
DR EMBL; BT021106; AAX12876.1; -; mRNA.
DR RefSeq; NP_850285.1; NM_179954.3. [F4IRW0-1]
DR RefSeq; NP_850286.1; NM_179955.2. [F4IRW0-2]
DR AlphaFoldDB; F4IRW0; -.
DR SMR; F4IRW0; -.
DR STRING; 3702.AT2G37840.1; -.
DR TCDB; 9.A.15.3.1; the autophagy-related phagophore-formation transporter (apt) family.
DR iPTMnet; F4IRW0; -.
DR PaxDb; F4IRW0; -.
DR PRIDE; F4IRW0; -.
DR ProteomicsDB; 246733; -. [F4IRW0-1]
DR EnsemblPlants; AT2G37840.1; AT2G37840.1; AT2G37840. [F4IRW0-1]
DR EnsemblPlants; AT2G37840.2; AT2G37840.2; AT2G37840. [F4IRW0-2]
DR GeneID; 818361; -.
DR Gramene; AT2G37840.1; AT2G37840.1; AT2G37840. [F4IRW0-1]
DR Gramene; AT2G37840.2; AT2G37840.2; AT2G37840. [F4IRW0-2]
DR KEGG; ath:AT2G37840; -.
DR Araport; AT2G37840; -.
DR TAIR; locus:2065680; AT2G37840.
DR eggNOG; KOG0595; Eukaryota.
DR HOGENOM; CLU_031241_0_0_1; -.
DR InParanoid; F4IRW0; -.
DR OMA; VWHARHK; -.
DR OrthoDB; 312774at2759; -.
DR PRO; PR:F4IRW0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IRW0; baseline and differential.
DR Genevisible; F4IRW0; 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..733
FT /note="Serine/threonine-protein kinase ATG1c"
FT /id="PRO_0000434621"
FT DOMAIN 12..269
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 292..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 419..422
FT /note="AIM (Atg8-family-interacting motif)"
FT /evidence="ECO:0000250|UniProtKB:Q94C95"
FT COMPBIAS 324..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..159
FT /note="MAQFTGRVVGDYLVGRQIGSGSFSVVWEARHRVDGTEVAIKEIAMDRLNKKL
FT QESLMSEIFILRRINHPNIIRLIDMIKSPGKVHLVLEYCKGGDLSVYVQRHGIVPEATA
FT KHFMQQLAAGLQVLRDNNIIHRDLKPQNLLLSTNENDADLKIADFGFA -> MNELEKV
FT SNGLKLLLNVYCRIS (in isoform 2)"
FT /id="VSP_057967"
FT CONFLICT 227
FT /note="T -> I (in Ref. 3; AAM14087)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="S -> N (in Ref. 3; AAM14087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 733 AA; 81815 MW; CB9530ABD05D746E CRC64;
MAQFTGRVVG DYLVGRQIGS GSFSVVWEAR HRVDGTEVAI KEIAMDRLNK KLQESLMSEI
FILRRINHPN IIRLIDMIKS PGKVHLVLEY CKGGDLSVYV QRHGIVPEAT AKHFMQQLAA
GLQVLRDNNI IHRDLKPQNL LLSTNENDAD LKIADFGFAR SLQPRGLAET LCGSPLYMAP
EIMQLQKYDA KADLWSVGAI LFQLVTGRTP FTGNSQIQLL QNIIRSTELH FPGDCRDLSL
DCIDLCQKLL RRNPVERLTF EEFFNHPFLS DRQSYDFSRS RLGLRTMDGF LSSGSSPSRN
MEESSQEDCL PFLLDDDSSG PEGSPSYLKK TSSMKSSSGI KVDTRIERKE VESSPLKHTE
LTSGYSSFNQ KVENDRFRFE TQINSDRRNR REPTGLTDSR SLIAPGRVDD SQDSMDQDFV
LVSGPPVDMP SSSSSSSKPY NFPFKSQSPP VELFNRSISS TAPMPIIGAT SNSIGQFGSL
DSQYSAPSTS HGSLDLGDAF EQPSTHSLTR IRSLRKYAAT IAELVYERIE SDKHLEAFSI
QLAILAIWKQ ALHICHTQAI SGLEGSPSQD INKLRSSSLK HDTHSSNKVT DLSHDGSEEI
SSQIQRQFIQ EIELAEELAK SIEPGNTKMP DAMETIFEAA LDLGKLGGVK EVMGDTENAG
NQYSKAVRLL VFLLVEAPML ILNPPLSLTN SVRYRLRTYI DFLSRRLKHL QSHRRSSAGQ
MQGSSLAMMN RQS
