SAX1_CAEEL
ID SAX1_CAEEL Reviewed; 476 AA.
AC Q2L6W9; Q21613; Q21946; Q2L6X0; Q9NB00;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Serine/threonine-protein kinase sax-1 {ECO:0000303|PubMed:10982409};
DE EC=2.7.11.1;
DE AltName: Full=NDR protein kinase {ECO:0000250|UniProtKB:Q9Y2H1, ECO:0000303|PubMed:10982409};
DE AltName: Full=Sensory axon guidance protein 1;
GN Name=sax-1 {ECO:0000312|WormBase:R11G1.4a}; ORFNames=R11G1.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF91417.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-476 (ISOFORM A), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAF91417.1};
RX PubMed=10982409; DOI=10.1091/mbc.11.9.3177;
RA Zallen J.A., Peckol E.L., Tobin D.M., Bargmann C.I.;
RT "Neuronal cell shape and neurite initiation are regulated by the Ndr kinase
RT SAX-1, a member of the Orb6/COT-1/warts serine/threonine kinase family.";
RL Mol. Biol. Cell 11:3177-3190(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAA84441.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-464 (ISOFORM B).
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA84441.1};
RX PubMed=7761441; DOI=10.1073/pnas.92.11.5022;
RA Millward T.A., Cron P., Hemmings B.A.;
RT "Molecular cloning and characterization of a conserved nuclear
RT serine/threonine protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5022-5026(1995).
RN [4] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=10409513; DOI=10.1242/dev.126.16.3679;
RA Zallen J.A., Kirch S.A., Bargmann C.I.;
RT "Genes required for axon pathfinding and extension in the C. elegans nerve
RT ring.";
RL Development 126:3679-3692(1999).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15473964; DOI=10.1016/j.neuron.2004.09.021;
RA Gallegos M.E., Bargmann C.I.;
RT "Mechanosensory neurite termination and tiling depend on SAX-2 and the SAX-
RT 1 kinase.";
RL Neuron 44:239-249(2004).
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. {ECO:0000269|PubMed:10982409,
CC ECO:0000269|PubMed:15473964}.
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:0000269|PubMed:10982409}. Nucleus
CC {ECO:0000269|PubMed:10982409}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:10982409, ECO:0000269|PubMed:9851916};
CC IsoId=Q2L6W9-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:7761441, ECO:0000269|PubMed:9851916};
CC IsoId=Q2L6W9-2; Sequence=VSP_053167;
CC -!- TISSUE SPECIFICITY: Widely expressed in embryonic and larval neurons
CC that contribute axons to the nerve ring and in hypodermal cells,
CC including lateral seam cells. Also displays a punctate localization in
CC muscle. {ECO:0000269|PubMed:10982409}.
CC -!- DISRUPTION PHENOTYPE: Expanded cell bodies and ectopic neurites in many
CC classes of neurons. Overlap of anterior lateral microtubule (ALM) and
CC posterior lateral microtubule (PLM) neurites along the anteroposterior
CC axis. {ECO:0000269|PubMed:10409513, ECO:0000269|PubMed:10982409,
CC ECO:0000269|PubMed:15473964}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000255}.
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DR EMBL; FO080291; CCD62663.1; -; Genomic_DNA.
DR EMBL; FO080291; CCD62664.1; -; Genomic_DNA.
DR EMBL; AF275634; AAF91417.1; -; mRNA.
DR EMBL; Z34989; CAA84441.1; -; mRNA.
DR RefSeq; NP_001024858.2; NM_001029687.3. [Q2L6W9-2]
DR RefSeq; NP_508627.5; NM_076226.5. [Q2L6W9-1]
DR AlphaFoldDB; Q2L6W9; -.
DR SMR; Q2L6W9; -.
DR STRING; 6239.R11G1.4a; -.
DR EPD; Q2L6W9; -.
DR PaxDb; Q2L6W9; -.
DR PeptideAtlas; Q2L6W9; -.
DR EnsemblMetazoa; R11G1.4a.1; R11G1.4a.1; WBGene00004727. [Q2L6W9-1]
DR EnsemblMetazoa; R11G1.4b.1; R11G1.4b.1; WBGene00004727. [Q2L6W9-2]
DR GeneID; 180655; -.
DR KEGG; cel:CELE_R11G1.4; -.
DR UCSC; R11G1.4a.1; c. elegans.
DR CTD; 180655; -.
DR WormBase; R11G1.4a; CE39615; WBGene00004727; sax-1. [Q2L6W9-1]
DR WormBase; R11G1.4b; CE39616; WBGene00004727; sax-1. [Q2L6W9-2]
DR eggNOG; KOG0605; Eukaryota.
DR GeneTree; ENSGT00940000153544; -.
DR InParanoid; Q2L6W9; -.
DR OMA; PERYSEN; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; Q2L6W9; -.
DR PRO; PR:Q2L6W9; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004727; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; ISS:WormBase.
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; ISS:WormBase.
DR GO; GO:0030031; P:cell projection assembly; IMP:WormBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:WormBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:WormBase.
DR GO; GO:0031175; P:neuron projection development; IMP:WormBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:WormBase.
DR GO; GO:0008360; P:regulation of cell shape; IMP:WormBase.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasm; Developmental protein;
KW Kinase; Magnesium; Metal-binding; Neurogenesis; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..476
FT /note="Serine/threonine-protein kinase sax-1"
FT /id="PRO_0000389613"
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"
FT VAR_SEQ 460..461
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:7761441,
FT ECO:0000303|PubMed:9851916"
FT /id="VSP_053167"
FT CONFLICT 59
FT /note="E -> R (in Ref. 3; CAA84441)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="T -> M (in Ref. 3; CAA84441)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="A -> R (in Ref. 3; CAA84441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 55547 MW; 0FF0FDB260A5EF8F CRC64;
MGEIAPEMEI SQYTKDKASC TRISIESYYS KRVTQCAERE NRLKKLEEDI SARGLSDEEK
EEKRKIHHSK ETDYLRLKRT RLTVNDFESL KVIGRGAFGE VRLVQKHDTG HIYAMKILRK
SEMVEKEQTA HVRAERDILS EADCDWVVKM YYSFQDYSNL YLVMEFLPGG DMMTLLIKKD
TLTEEATQFY IAEAALAIQF IHSLGFIHRD IKPDNLLLDA RGHVKLSDFG LCTGLKKFHR
TDHYRNWPST LPPDFISKPF ESKRKAETWK RNRRAYAYST VGTPDYIAPE VFQPNGYTKS
CDWWSLGVIM YEMLIGYPPF CSELPQETYR KVINWQQTLV FPSDVPISIE AKATIKRFCC
EAERRLGNHG GLDEIKQCPF VKRIDWNHIR ERPPPIRVTV KSIDDTSNFD DFPDEDLTWP
TSTLIRPEEQ PGRRGEFVDF TYKRFDGLTQ KMRYSDLKKF QQAKKNKKGG QQGTSD
