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Serine/threonine-protein kinase unc-51 (EC 2.7.11.1) (Uncoordinated protein 51)

 UNC51_CAEEL             Reviewed;         856 AA.
Q23023;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 152.
RecName: Full=Serine/threonine-protein kinase unc-51;
EC=2.7.11.1 {ECO:0000269|PubMed:15539493};
AltName: Full=Uncoordinated protein 51;
Name=unc-51 {ECO:0000312|WormBase:Y60A3A.1};
ORFNames=Y60A3A.1 {ECO:0000312|WormBase:Y60A3A.1};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, MUTAGENESIS
OF LYS-39 AND ARG-841, AND DISRUPTION PHENOTYPE.
STRAIN=Bristol N2;
PubMed=7958904; DOI=10.1101/gad.8.20.2389;
Ogura K., Wicky C., Magnenat L., Tobler H., Mori I., Mueller F.,
Ohshima Y.;
"Caenorhabditis elegans unc-51 gene required for axonal elongation
encodes a novel serine/threonine kinase.";
Genes Dev. 8:2389-2400(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12958363; DOI=10.1126/science.1087782;
Melendez A., Talloczy Z., Seaman M., Eskelinen E.L., Hall D.H.,
Levine B.;
"Autophagy genes are essential for dauer development and life-span
extension in C. elegans.";
Science 301:1387-1391(2003).
[4]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH UNC-14 AND
VAB-8, AND MUTAGENESIS OF LYS-39 AND 37-ALA--ILE-41.
PubMed=15539493; DOI=10.1242/dev.01457;
Lai T., Garriga G.;
"The conserved kinase UNC-51 acts with VAB-8 and UNC-14 to regulate
axon outgrowth in C. elegans.";
Development 131:5991-6000(2004).
[5]
FUNCTION.
PubMed=17890369; DOI=10.1534/genetics.107.075762;
Aladzsity I., Toth M.L., Sigmond T., Szabo E., Bicsak B., Barna J.,
Regos A., Orosz L., Kovacs A.L., Vellai T.;
"Autophagy genes unc-51 and bec-1 are required for normal cell size in
Caenorhabditis elegans.";
Genetics 177:655-660(2007).
[6]
FUNCTION, AND INTERACTION WITH ATG-13.
PubMed=19377305; DOI=10.4161/auto.5.5.8624;
Tian E., Wang F., Han J., Zhang H.;
"epg-1 functions in autophagy-regulated processes and may encode a
highly divergent Atg13 homolog in C. elegans.";
Autophagy 5:608-615(2009).
-!- FUNCTION: Protein kinase important for axonal elongation and
axonal guidance (PubMed:7958904, PubMed:15539493). Functions in
the CAN axons to direct both anterior and posterior migrations
(PubMed:15539493). Phosphorylates both unc-14 and vab-8
(PubMed:15539493). Plays a role in autophagy (PubMed:12958363,
PubMed:17890369). Interaction with autophagy related proteins such
as atg-13 links it to the autophagy machinery to in turn promote
P-granule degradation in somatic cells (PubMed:19377305).
Regulates cell size (PubMed:17890369). Plays a role in male tail
ray pattern formation (PubMed:17890369). May be required for
normal dauer morphogenesis (PubMed:12958363).
{ECO:0000269|PubMed:12958363, ECO:0000269|PubMed:15539493,
ECO:0000269|PubMed:17890369, ECO:0000269|PubMed:19377305,
ECO:0000269|PubMed:7958904}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:15539493}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15539493};
-!- SUBUNIT: Interacts with unc-14 and vab-8 (PubMed:15539493).
Interacts (via C-terminus) with atg-13 (PubMed:19377305).
{ECO:0000269|PubMed:15539493, ECO:0000269|PubMed:19377305}.
-!- INTERACTION:
G5ECQ1:unc-14; NbExp=4; IntAct=EBI-329049, EBI-2419199;
Q21441:vab-8; NbExp=4; IntAct=EBI-329049, EBI-2412191;
-!- DEVELOPMENTAL STAGE: During embryonic development unc-51 is
expressed extensively, particularly in the head region of late
embryos. In the larval stages, expression appears to be restricted
to neurons. {ECO:0000269|PubMed:7958904}.
-!- DISRUPTION PHENOTYPE: Worms exhibit various abnormalities in
axonal elongation and axonal structures (PubMed:7958904). RNAi-
mediated knockdown causes abnormalities in constitutive dauer
formation in daf-2 e1370 mutant including a lack of autophagosome
formation (PubMed:12958363). {ECO:0000269|PubMed:12958363,
ECO:0000269|PubMed:7958904}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. APG1/unc-51/ULK1 subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; Z38016; CAA86114.1; -; mRNA.
EMBL; AL117207; CAB60406.1; -; Genomic_DNA.
PIR; T43631; T43631.
RefSeq; NP_507869.1; NM_075468.4.
UniGene; Cel.5550; -.
PDB; 5AZG; X-ray; 1.81 A; C/D=353-361.
PDBsum; 5AZG; -.
ProteinModelPortal; Q23023; -.
SMR; Q23023; -.
BioGrid; 45271; 2.
DIP; DIP-26124N; -.
IntAct; Q23023; 3.
STRING; 6239.Y60A3A.1.2; -.
iPTMnet; Q23023; -.
EPD; Q23023; -.
PaxDb; Q23023; -.
PeptideAtlas; Q23023; -.
EnsemblMetazoa; Y60A3A.1; Y60A3A.1; WBGene00006786.
GeneID; 180311; -.
KEGG; cel:CELE_Y60A3A.1; -.
UCSC; Y60A3A.1.1; c. elegans.
CTD; 180311; -.
WormBase; Y60A3A.1; CE24516; WBGene00006786; unc-51.
eggNOG; KOG0595; Eukaryota.
eggNOG; ENOG410XR01; LUCA.
GeneTree; ENSGT00910000144033; -.
InParanoid; Q23023; -.
KO; K08269; -.
OMA; GTIPEQF; -.
OrthoDB; EOG091G0P85; -.
PhylomeDB; Q23023; -.
BRENDA; 2.7.11.1; 1045.
Reactome; R-CEL-1632852; Macroautophagy.
Reactome; R-CEL-8854214; TBC/RABGAPs.
Reactome; R-CEL-8934903; Receptor Mediated Mitophagy.
SignaLink; Q23023; -.
PRO; PR:Q23023; -.
Proteomes; UP000001940; Chromosome V.
Bgee; WBGene00006786; -.
GO; GO:0030424; C:axon; IDA:WormBase.
GO; GO:0043005; C:neuron projection; IDA:WormBase.
GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:WormBase.
GO; GO:0043277; P:apoptotic cell clearance; IMP:WormBase.
GO; GO:0006914; P:autophagy; IGI:WormBase.
GO; GO:0007411; P:axon guidance; IMP:WormBase.
GO; GO:0007409; P:axonogenesis; IMP:WormBase.
GO; GO:0016477; P:cell migration; IMP:WormBase.
GO; GO:0040024; P:dauer larval development; IGI:WormBase.
GO; GO:0008340; P:determination of adult lifespan; IGI:WormBase.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
GO; GO:0012501; P:programmed cell death; IGI:WormBase.
GO; GO:0046777; P:protein autophosphorylation; IDA:WormBase.
GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
GO; GO:0030516; P:regulation of axon extension; IMP:WormBase.
GO; GO:0008361; P:regulation of cell size; IMP:WormBase.
GO; GO:0040014; P:regulation of multicellular organism growth; IGI:WormBase.
GO; GO:0032880; P:regulation of protein localization; IMP:WormBase.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR022708; Ser/Thr_kinase_C.
InterPro; IPR017184; Ser/Thr_kinase_Unc51.
Pfam; PF12063; DUF3543; 1.
Pfam; PF00069; Pkinase; 1.
PIRSF; PIRSF037369; Ser/Thr_PK_unc51; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Developmental protein;
Differentiation; Kinase; Magnesium; Metal-binding; Neurogenesis;
Nucleotide-binding; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 856 Serine/threonine-protein kinase unc-51.
/FTId=PRO_0000086785.
DOMAIN 9 275 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 15 23 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 750 856 Interaction with unc-14 and vab-8.
COMPBIAS 415 418 Poly-Ser.
COMPBIAS 429 436 Poly-Gln.
COMPBIAS 521 526 Poly-Thr.
COMPBIAS 602 605 Poly-Glu.
ACT_SITE 134 134 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 39 39 ATP. {ECO:0000305}.
MUTAGEN 37 41 Missing: Abrogates kinase activity.
{ECO:0000269|PubMed:15539493}.
MUTAGEN 39 39 K->M: In KSEX9; variable effects.
{ECO:0000269|PubMed:15539493,
ECO:0000269|PubMed:7958904}.
MUTAGEN 39 39 K->R: Impairs kinase activity.
{ECO:0000269|PubMed:15539493,
ECO:0000269|PubMed:7958904}.
MUTAGEN 841 841 R->H: In E1120; paralyzed, egg laying
defective and dumpy.
{ECO:0000269|PubMed:7958904}.
SEQUENCE 856 AA; 94893 MW; 721F6F6FB0399F6E CRC64;
MEQFDGFEYS KRDLLGHGAF AIVYRGRYVD RTDVPVAIKA IAKKNISKSK NLLTKEIKIL
KELSSLKHEN LVGLLKCTET PTHVYLVMEF CNGGDLADYL QQKTTLNEDT IQHFVVQIAH
ALEAINKKGI VHRDLKPQNI LLCNNSRTQN PHFTDIVIKL ADFGFARFLN DGVMAATLCG
SPMYMAPEVI MSMQYDAKAD LWSIGTILFQ CLTGKAPFVA QTPPQLKAYY EKTRELRPNI
PEWCSPNLRD LLLRLLKRNA KDRISFEDFF NHPFLTSPLL PSPSKRILES ARSPLLANRR
IITPQSSLPV PKRAGSTKLD SPTPVRRIGE SPRVQRRVIT PGMPSPVPGA PMQESTDFTF
LPPRQESSPV KQVQVHTNVS PSLTTCKPVP VPSQRLTYQK MEERLAAARK TAVPSSSSPT
GSAVSAQHQH QHQQQQEPAS SPVVQRIERP DQLPRRTTLQ DPNAHDIERM TMPNPTFVVC
GSSTKPSPNN ANRVRRSTIT SPADTQDMVA ADQMLSNLDP TTTTTTIPKS ATTANIQGIP
RGARDRSVTS PPQPTIHENE PLDNAKYQQT DVNNSPTAPT EPFIIKNQTT CSTSSTSSSV
VEEEEAMSLP FASGSHLAAG FKKTPAEVPM DHGALPPALD QEIVLGEEHK QILAKLRFVA
ELVDTLIHVA EQKDNPLASA MASRRQLLTT GTSTTNTSSP YRRAEQLVVY VRALHMLSSA
LLLAQTNVAN RVLHPSVAVQ QVLNQLNDKY HQCLVRSQEL ASLGLPGQDP AMAVISAERI
MYRHAIELCQ AAALDELFGN PQLCSQRYQT AYMMLHTLAE QVNCDQDKTV LTRYKVAVEK
RLRILERQGF VAAVNT


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