ID   ULK4_PONAB              Reviewed;        1275 AA.
AC   Q5R4M2;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Serine/threonine-protein kinase ULK4;
DE            EC=2.7.11.1;
DE   AltName: Full=Unc-51-like kinase 4;
GN   Name=ULK4;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the remodeling of cytoskeletal components,
CC       such as alpha-tubulin, and in this way regulates neurite branching and
CC       elongation, as well as cell motility. {ECO:0000250|UniProtKB:Q96C45}.
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   -!- 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; CR861224; CAH93294.1; -; mRNA.
DR   RefSeq; NP_001126939.1; NM_001133467.1.
DR   AlphaFoldDB; Q5R4M2; -.
DR   SMR; Q5R4M2; -.
DR   STRING; 9601.ENSPPYP00000015642; -.
DR   PRIDE; Q5R4M2; -.
DR   GeneID; 100173957; -.
DR   KEGG; pon:100173957; -.
DR   CTD; 54986; -.
DR   eggNOG; KOG0597; Eukaryota.
DR   InParanoid; Q5R4M2; -.
DR   OrthoDB; 219167at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR045906; ULK4.
DR   PANTHER; PTHR46240; PTHR46240; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..1275
FT                   /note="Serine/threonine-protein kinase ULK4"
FT                   /id="PRO_0000250155"
FT   DOMAIN          4..280
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REPEAT          727..765
FT                   /note="HEAT 1"
FT   REPEAT          842..880
FT                   /note="HEAT 2"
FT   REPEAT          926..964
FT                   /note="HEAT 3"
FT   REPEAT          1025..1063
FT                   /note="HEAT 4"
FT   REPEAT          1151..1189
FT                   /note="HEAT 5"
FT   REPEAT          1213..1253
FT                   /note="HEAT 6"
FT   REGION          299..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        121
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   1275 AA;  142929 MW;  D66C0420534A13B1 CRC64;
     MENFILYEEI GRGSKSVVYK GRRKGTINFV AILCTDKCKR PEITNWVRLT HEIKHKNIVT
     FHEWYETSNH LWLVVELCTG GSLKTVIAQD ENLPEDVVRE FGIDLISGLH HLHKLGILFC
     DISPRKILLE GPGTLKFSNF CLAKVEGENL EEFFALVAAE EGGGDSGENV LKKSMKSRVK
     GSPVYTAPEV VRGAEFSISS DLWSVGCLLY EMFSGKPPFF SESISELTEK ILCEDPLPPI
     PKDSSCPKAS SDFTNLLDGL LQRDPQKRLT WTRLLQHSFW KKAFAGADQE SSVEDLSLSR
     NTMECSGPQD SKELLQNSQS RQAKGHKSGQ RLGHYFRLEN PTEFRPKSTL EGQLNESMFL
     LSSRPTPRTS TAVEVSPGED RTHCSPQKTS PLTKITSGRL SQQDLESQMR ELIYTDSDLV
     VTPIIDNPKI MKQPPVKFDP KILHLPAYSV DKLLFLKDQD WNDFLQQVCS QIDSTEKSMG
     ASRAKLNLLC YLCMVAGHQE VATRLLHSPL FKLLIQHLRI APNWDIRAKV ARVIGLLASH
     TTELQENTPV VEAIVLLTEL IRENFRNSKL KQCLLPTLGE LIYLVATQEE KKKNPRECWA
     FPLAAYTVLM RCLREGEERV VNHMAAKIIE NVCTTFSAQA QGFITGEIGP ILWYLFRHST
     ADSLRITAVS ALCRITRHSP TAFQNVIEKV GLNSVINSLA SAICKVQQYM LTLFTAMLSC
     GVHLQRLIQE KDFVSTIIRL LESPSTYIRA KAFLVLLYIL IYNREMLLLS CQARLVMYIE
     RDSRKITPGK EQQSGNEYLS KCLDLLIRHI VQELPRILGD ILNSLANVSG RKHPSTVQVK
     QLKMCLPLMP IVLHLVTSQV FRPQVVTEEF LFSYGTILSH IKSVDSGETN IDGAIGLTAS
     EEFIKITLSA FEAIIQYPIL LKDYRSTVVD YILPPLVSLV QSQNVEWRLF SLRLLSETTS
     LLVNQEFGDG KEKASVDSDS NLLALIRDVL LPQYEHILVE PDPVPAYALK LLVAMTEHNP
     TFTRLVEESK LIPLIFEVTL EHQESILGNT MQSVIALLNN LVACKDSNMK LLYEQGLVSH
     ICNLLTETAT LCLDVDNKNN NEMAAALLFS LLDILHSMLT YTSGIVRLAL QTQKSGSGED
     IQAAEDLLLL NRPLTDLISL LIPLLPNEDP EIFDVSSKCL SILVQLYGGE NPDSLSPENV
     EIFAHLLTSK EDPKEQKLLL RILRRMITSN EKHLESLKNA GSLLRALERL APGSGSFADS
     VVAPLALEIL QAVGR