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ULK3_XENLA
ID   ULK3_XENLA              Reviewed;         468 AA.
AC   Q4V7Q6;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Serine/threonine-protein kinase ULK3;
DE            EC=2.7.11.1;
DE   AltName: Full=Unc-51-like kinase 3;
GN   Name=ulk3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine/threonine protein kinase that acts as a regulator of
CC       Sonic hedgehog (SHH) signaling and autophagy. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. APG1/unc-51/ULK1 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
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DR   EMBL; BC097772; AAH97772.1; -; mRNA.
DR   RefSeq; NP_001089515.1; NM_001096046.1.
DR   AlphaFoldDB; Q4V7Q6; -.
DR   SMR; Q4V7Q6; -.
DR   MaxQB; Q4V7Q6; -.
DR   DNASU; 734568; -.
DR   GeneID; 734568; -.
DR   KEGG; xla:734568; -.
DR   CTD; 734568; -.
DR   Xenbase; XB-GENE-5958954; ulk3.L.
DR   OrthoDB; 1084750at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 734568; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0000407; C:phagophore assembly site; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   InterPro; IPR045269; Atg1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR007330; MIT_dom.
DR   InterPro; IPR036181; MIT_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; PF04212; MIT; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00745; MIT; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF116846; SSF116846; 2.
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   ATP-binding; Autophagy; Cytoplasm; Kinase; Nucleotide-binding;
KW   Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..468
FT                   /note="Serine/threonine-protein kinase ULK3"
FT                   /id="PRO_0000250153"
FT   DOMAIN          13..269
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          279..347
FT                   /note="MIT 1"
FT   DOMAIN          374..442
FT                   /note="MIT 2"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         19..27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   468 AA;  53127 MW;  527E38EE938002FE CRC64;
     MAAGWAPPRL EDFILTEKLG SGSYATVYKA YRKRNAREVV AIKCVSKKSL NKAAVENLLT
     EIEILKTVHH PHILELKDFQ WDQDYIFLIT EYCAGGDLSR FIRTRRILPE RIVQVFLQQL
     ASALKFLHEK NISHLDLKPQ NILLSRLDRP HLKLADFGFA QHMSSEDAPQ ALRGSPLYMA
     PEMVCSKHYD ARVDLWSVGV ILYEALFGKA PFASKSFSEL EEKILSHKTI ELPTRPRLSP
     ECRDLLQQLL QRDPDKRISF IEFFAHLFVD LEHMPSAETL EKATRLVVEA VEKDSAGEHS
     AALTLYCKAL EYFIPALHYE SDAKRKEAMR SKVCQYISRA EELKVLVSSS NKTLLMQGIS
     GRELLKEMAQ DKPRLFSALE VASAAVAKDE EGCACDALDL YQQSLGELLL MLSAESPGRR
     RELLHAEIQT LMGRAEFLKE QMKTSQWKSE SLGQEVLSES VRNSCSLQ
 
 
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