SAX1_CAEBR
ID SAX1_CAEBR Reviewed; 472 AA.
AC A8XJL7;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Serine/threonine-protein kinase sax-1 {ECO:0000250|UniProtKB:Q2L6W9};
DE EC=2.7.11.1;
DE AltName: Full=NDR protein kinase {ECO:0000250|UniProtKB:Q2L6W9, ECO:0000250|UniProtKB:Q9Y2H1};
DE AltName: Full=Sensory axon guidance protein 1 {ECO:0000250|UniProtKB:Q2L6W9};
GN Name=sax-1 {ECO:0000312|EMBL:CAP32843.2}; ORFNames=CBG14249;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP32843.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP32843.2};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Acts with sax-2 to restrict the growth of both primary and
CC secondary neurites. Regulates mechanosensory tiling by controlling the
CC termination point of sensory dendrites (By similarity).
CC {ECO:0000250|UniProtKB:Q2L6W9}.
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 Evidence={ECO:0000250|UniProtKB:Q9Y2H1};
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; Evidence={ECO:0000250|UniProtKB:Q9Y2H1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2H1};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250|UniProtKB:Q2L6W9}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000255}.
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DR EMBL; HE600983; CAP32843.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XJL7; -.
DR SMR; A8XJL7; -.
DR STRING; 6238.CBG14249; -.
DR EnsemblMetazoa; CBG14249a.1; CBG14249a.1; WBGene00034813.
DR WormBase; CBG14249a; CBP35530; WBGene00034813; Cbr-sax-1.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_000288_67_2_1; -.
DR InParanoid; A8XJL7; -.
DR OMA; PERYSEN; -.
DR OrthoDB; 759391at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Developmental protein; Kinase; Magnesium;
KW Metal-binding; Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..472
FT /note="Serine/threonine-protein kinase sax-1"
FT /id="PRO_0000389612"
FT DOMAIN 87..381
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 382..452
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 93..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 472 AA; 55090 MW; 51B61230F7E7EEBE CRC64;
MGDVAPEVEI SQYTKDKASC TRISIESYYS KRVTQCAERE NRLKKLEEDM SARGLSDDEK
DEKRKIHHSK ETDYLRLKRT RLTVNDFESL KVIGRGAFGE VRLVQKHDTG HIYAMKILRK
SEMVEKEQTA HVRAERDILS EADCDWVVKM YYSFQDYSNL YLVMEFLPGG DMMTLLIKKD
TLTEEATQFY VAEAALAIQF IHNLGFIHRD IKPDNLLLDA RGHVKLSDFG LCTGLKKFHR
TDHYRNWPVT LPPDFISKPF ESKRKAETWK RNRRAYAYST VGTPDYIAPE VFQPNGYTKS
CDWWSLGVIM YEMLIGYPPF CSELPQETYR KVINWQQTLV FPSDVPISIE AKATIKRFCC
EAERRLGNHG GLDEIKQCPF FRRIDWNHIR ERPPPIRVTV KSIDDTSNFD DFPDEDLSWP
TSTLIRPEEQ PGRRGEFVDF TYKRFDGLTQ KMRYSDLKKQ AKKNKKGQGS SD
