STRD1_CAEEL
ID STRD1_CAEEL Reviewed; 388 AA.
AC G5ECN5;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=STE20-related kinase adapter protein strd-1 {ECO:0000305|PubMed:20023164};
DE AltName: Full=STRAD STE20-related adapter homolog {ECO:0000312|WormBase:Y52D3.1a};
GN Name=strd-1 {ECO:0000312|WormBase:Y52D3.1a};
GN ORFNames=Y52D3.1 {ECO:0000312|WormBase:Y52D3.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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}
RP FUNCTION, INTERACTION WITH SAD-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-175.
RX PubMed=20023164; DOI=10.1242/dev.041459;
RA Kim J.S., Hung W., Narbonne P., Roy R., Zhen M.;
RT "C. elegans STRADalpha and SAD cooperatively regulate neuronal polarity and
RT synaptic organization.";
RL Development 137:93-102(2010).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PAR-4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-243.
RX PubMed=20110331; DOI=10.1242/dev.042044;
RA Narbonne P., Hyenne V., Li S., Labbe J.C., Roy R.;
RT "Differential requirements for STRAD in LKB1-dependent functions in C.
RT elegans.";
RL Development 137:661-670(2010).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22801495; DOI=10.1038/nature11240;
RA Denning D.P., Hatch V., Horvitz H.R.;
RT "Programmed elimination of cells by caspase-independent cell extrusion in
RT C. elegans.";
RL Nature 488:226-230(2012).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23267054; DOI=10.1534/genetics.112.148106;
RA Chien S.C., Brinkmann E.M., Teuliere J., Garriga G.;
RT "Caenorhabditis elegans PIG-1/MELK acts in a conserved PAR-4/LKB1 polarity
RT pathway to promote asymmetric neuroblast divisions.";
RL Genetics 193:897-909(2013).
CC -!- FUNCTION: Pseudokinase which may act as an adapter for kinases sad-1
CC and par-4 and thereby is involved in several developmental processes.
CC Regulates cell-autonomously both neuronal polarity and synaptic
CC organization when bound to sad-1. Required for sad-1 localization to
CC synapses (PubMed:20023164). Required to establish germline stem cell
CC (GSC) quiescence during dauer development, to promote cell shedding
CC during embryogenesis and to control asymmetric cell division of the Q.p
CC neuroblast lineage, probably when bound to par-4 (PubMed:20110331,
CC PubMed:22801495, PubMed:23267054). May be involved in maintaining the
CC integrity of the early embryonic cortex when bound to par-4
CC (PubMed:20110331). {ECO:0000269|PubMed:20023164,
CC ECO:0000269|PubMed:20110331, ECO:0000269|PubMed:22801495,
CC ECO:0000269|PubMed:23267054}.
CC -!- SUBUNIT: Interacts with sad-1 (PubMed:20023164). Interacts with par-4
CC (PubMed:20110331). {ECO:0000269|PubMed:20023164,
CC ECO:0000269|PubMed:20110331}.
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:20023164}. Nucleus
CC {ECO:0000269|PubMed:20023164}. Cell projection, dendrite
CC {ECO:0000269|PubMed:20023164}. Cell projection, axon
CC {ECO:0000269|PubMed:20023164}. Synapse {ECO:0000269|PubMed:20023164}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:20110331}. Cytoplasm
CC {ECO:0000269|PubMed:20110331}. Note=Localizes in punctate structures
CC along the neurites of GABAergic motoneurons. Co-localizes with sad-1 at
CC synapses (PubMed:20023164). Co-localizes with par-4 at the cell cortex
CC of the early embryo. Cell cortex localization is regulated by par-4
CC (PubMed:20110331). {ECO:0000269|PubMed:20023164,
CC ECO:0000269|PubMed:20110331}.
CC -!- TISSUE SPECIFICITY: Expressed in nervous system, pharynx and excretory
CC canal (PubMed:20023164). Expressed in germline (PubMed:20110331).
CC {ECO:0000269|PubMed:20023164, ECO:0000269|PubMed:20110331}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo.
CC {ECO:0000269|PubMed:20110331}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000303|PubMed:20023164}.
CC -!- DISRUPTION PHENOTYPE: Ectopic expression of pre-synaptic reporter snb-
CC 1-GFP in ASI sensory neurons. Along the dorsal nerve cord of DD
CC motoneurons, pre-synaptic puncta appear diffuse or smaller and synapse
CC localization of sad-1 is disrupted. Germline hyperplasia and loss of
CC aak-2 phosphorylation during dauer development (PubMed:20110331).
CC During neuroblast division, daughter cell size asymmetry in the Q.p
CC division is defective (PubMed:23267054). Animals are slightly stiff but
CC with active locomotion (PubMed:20023164). In par-4 (it33) mutants,
CC causes embryonic lethality (PubMed:20023164). In ced-3 (n3692) mutants,
CC impaired cell shedding during embryogenesis which results in the
CC generation of an ectopic excretory cell (PubMed:22801495). In addition,
CC these double mutants produce additional AVM or PVM mechanosensory
CC neurons (PubMed:23267054). {ECO:0000269|PubMed:20023164,
CC ECO:0000269|PubMed:20110331, ECO:0000269|PubMed:22801495,
CC ECO:0000269|PubMed:23267054}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; BX284603; CAB16482.1; -; Genomic_DNA.
DR PIR; T26977; T26977.
DR RefSeq; NP_001022902.1; NM_001027731.3.
DR AlphaFoldDB; G5ECN5; -.
DR SMR; G5ECN5; -.
DR IntAct; G5ECN5; 1.
DR STRING; 6239.Y52D3.1a.1; -.
DR EPD; G5ECN5; -.
DR PaxDb; G5ECN5; -.
DR PeptideAtlas; G5ECN5; -.
DR EnsemblMetazoa; Y52D3.1a.1; Y52D3.1a.1; WBGene00013132.
DR GeneID; 176526; -.
DR KEGG; cel:CELE_Y52D3.1; -.
DR CTD; 176526; -.
DR WormBase; Y52D3.1a; CE19223; WBGene00013132; strd-1.
DR eggNOG; KOG0582; Eukaryota.
DR GeneTree; ENSGT00940000168867; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; G5ECN5; -.
DR OMA; QRDPENR; -.
DR OrthoDB; 995563at2759; -.
DR PhylomeDB; G5ECN5; -.
DR PRO; PR:G5ECN5; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00013132; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0044297; C:cell body; IDA:WormBase.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IPI:WormBase.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IMP:WormBase.
DR GO; GO:0055059; P:asymmetric neuroblast division; IMP:WormBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:WormBase.
DR GO; GO:0043055; P:maintenance of dauer; IGI:WormBase.
DR GO; GO:1904746; P:negative regulation of apoptotic process involved in development; IGI:UniProtKB.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:WormBase.
DR GO; GO:0035418; P:protein localization to synapse; IMP:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0050808; P:synapse organization; IMP:WormBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cytoplasm; Neurogenesis; Nucleotide-binding;
KW Nucleus; Reference proteome; Synapse.
FT CHAIN 1..388
FT /note="STE20-related kinase adapter protein strd-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433877"
FT DOMAIN 52..335
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 58..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 175
FT /note="D->A: No defect in neuronal polarity and synaptic
FT organization."
FT /evidence="ECO:0000269|PubMed:20023164"
FT MUTAGEN 243
FT /note="G->S: In rr92; germline hyperplasia during dauer
FT development."
FT /evidence="ECO:0000269|PubMed:20110331"
SQ SEQUENCE 388 AA; 44275 MW; 39B13C597A397C19 CRC64;
MADTTILDTT CSSTLAANVE FSHATDSAIG ISLKNATITE AEGVPNLKET GYDCVRYMGT
CNGGQIYLGR ERKKLKDYVA IKKFAIDDVD DYAAIAKESS NLRLMHHPNI IELCECFVYE
RSIYQITPAM NLGSLFDIVF EYMKWGINEK SAAAITRQLL DALSYLHQRR YIHRDLKPKH
ILIDSSGNVK LSGFRFMIEL NHHLDCVFEF DAHLQNQLYY LAPEVLAQNI HGYTSKSDIY
MLGISICEAI NGVMPFGELE PLEMLHRKLN GQVPRPVDMI SLKDDQKMGL DISHRPQEHL
TRRFSKEMHE FIANCLDYDP QQRGSASDLK SSAWLGSKIH KNLGPVDVRQ ELNLDYAHFD
LSLWEQEPLI PMEPDQKYEI VFDYSPIS
