ID   ULK3_CHICK              Reviewed;         468 AA.
AC   Q5ZJH6;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
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; ORFNames=RCJMB04_18b17;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720458; CAG32117.1; -; mRNA.
DR   AlphaFoldDB; Q5ZJH6; -.
DR   SMR; Q5ZJH6; -.
DR   STRING; 9031.ENSGALP00000039246; -.
DR   VEuPathDB; HostDB:geneid_769780; -.
DR   eggNOG; KOG0595; Eukaryota.
DR   InParanoid; Q5ZJH6; -.
DR   OrthoDB; 1084750at2759; -.
DR   PhylomeDB; Q5ZJH6; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005776; C:autophagosome; IBA:GO_Central.
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:1905037; P:autophagosome organization; IBA:GO_Central.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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_0000250152"
FT   DOMAIN          14..270
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          280..348
FT                   /note="MIT 1"
FT   DOMAIN          375..444
FT                   /note="MIT 2"
FT   ACT_SITE        137
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         20..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   468 AA;  53065 MW;  F9C47E447D339268 CRC64;
     MAGGGCAPPR LDGFVLTERL GTGTYATVYK AYGKRDTREV VAVKCVSKRS LNRASVENLL
     TEIEILKTIR HPHIVELKDF QWDSDHIYLI MEFCAGGDLS RFIRMRRILP EKVARIFLQQ
     LACALKFLHD HNISHLDLKP QNILLSTPEN PQLKLADFGF AQYMSPWDEK HVLRGSPLYM
     APEMVCRQQY DARVDLWSVG VILYEALFGR PPFASRSFAE LEEKIRSDRA IELPSRPPLS
     PDCRDLLQRL LERDPLKRIS FEEFFAHPFV DMEHMPGPES FCKATNLVVE AVKKDQEGDA
     SAALSLYCKA LEYFVPALHY ESDARRKEAI RTKVGQYISR AEELKALVAS KSKNLLQQGN
     PAREILKEMA KDKPRLCAAL EMASVAVARE EEGKDDGDTL ELYQQSLGEL LLLLAAEPAG
     RRRELLHAEI QTLMARAEYL KDQIKMREAQ SMGKEALADS VRSSCTLQ