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Database: UniProt
Entry: W8C0S9_CERCA
LinkDB: W8C0S9_CERCA
Original site: W8C0S9_CERCA 
ID   W8C0S9_CERCA            Unreviewed;       496 AA.
AC   W8C0S9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Serine/threonine-protein kinase ULK3 {ECO:0000256|ARBA:ARBA00021644};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   AltName: Full=Unc-51-like kinase 3 {ECO:0000256|ARBA:ARBA00032242};
GN   Name=ULK3 {ECO:0000313|EMBL:JAC02704.1};
OS   Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Ceratitis; Ceratitis.
OX   NCBI_TaxID=7213 {ECO:0000313|EMBL:JAC02704.1};
RN   [1] {ECO:0000313|EMBL:JAC02704.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Geib S.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAC02704.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA   Calla B., Hall B., Hou S., Geib S.M.;
RT   "A genomic perspective to assessing quality of mass-reared SIT flies used
RT   in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT   California.";
RL   BMC Genomics 15:98-98(2014).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; GAMC01003852; JAC02704.1; -; mRNA.
DR   AlphaFoldDB; W8C0S9; -.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24348:SF65; SERINE/THREONINE-PROTEIN KINASE ULK3; 1.
DR   PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 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; MIT domain; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Kinase {ECO:0000313|EMBL:JAC02704.1};
KW   Lipid droplet {ECO:0000256|ARBA:ARBA00022677};
KW   Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW   Transferase {ECO:0000313|EMBL:JAC02704.1}.
FT   DOMAIN          9..264
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          360..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  57050 MW;  3868164035724F71 CRC64;
     MTLPRITDYE LMEKLGVGSY STVYKARHKK DRSFHAIKIV EMSTLSDSSR ENLITEIRLL
     RSLNHKYIVT LQDFFWDDKK IYIVLEFCNA GNLSAFIRSK KSLPEATCRF FLRQLAAAVQ
     YMRANDICHF DLKPQNLLLT RNSNVVLKVA DFGFAQHLKL GEINQQLKGS PLYMAPEIVR
     KHQYDAKADL WSIGVILYEC LFGKAPYTSK SIEELLQRIR NAEKIKIPAN ASISNECHDL
     LCRLLEHDPA KRISFDSFFA HPFIDLKTLP TEHTLQKASD LVTKAVEYDE KQNYKEAYYL
     YCSALQYFVP LITEEADASK RLALRNRALT YLKRAEEIKN VLIDAEYKAA AVKELPKHLQ
     QCTQQQEQQP SSSSKPNSAQ QTQPDIIEVL EPDMRYKQLF ALSNSSPQLK SALEIGRQGE
     LYLYERKFKA ALEAYTSALG MLVPFANNEP KGERRNLLLQ QLEIWMKEAE SIKSILSAKE
     MVDEQKLTSV RHCSIQ
//
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