MES1_CAEEL
ID MES1_CAEEL Reviewed; 966 AA.
AC G5EBL2;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Protein mes-1 {ECO:0000305};
DE AltName: Full=Maternal-effect sterile protein 1 {ECO:0000312|WormBase:F54F7.5};
DE Flags: Precursor;
GN Name=mes-1 {ECO:0000312|WormBase:F54F7.5};
GN ORFNames=F54F7.5 {ECO:0000312|WormBase:F54F7.5};
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:0000312|EMBL:AAF13716.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=11003841; DOI=10.1242/dev.127.20.4419;
RA Berkowitz L.A., Strome S.;
RT "MES-1, a protein required for unequal divisions of the germline in early
RT C. elegans embryos, resembles receptor tyrosine kinases and is localized to
RT the boundary between the germline and gut cells.";
RL Development 127:4419-4431(2000).
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-89 AND SER-441.
RX PubMed=7555722; DOI=10.1242/dev.121.9.2961;
RA Strome S., Martin P., Schierenberg E., Paulsen J.;
RT "Transformation of the germ line into muscle in mes-1 mutant embryos of C.
RT elegans.";
RL Development 121:2961-2972(1995).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12110172; DOI=10.1016/s1534-5807(02)00185-5;
RA Bei Y., Hogan J., Berkowitz L.A., Soto M., Rocheleau C.E., Pang K.M.,
RA Collins J., Mello C.C.;
RT "SRC-1 and Wnt signaling act together to specify endoderm and to control
RT cleavage orientation in early C. elegans embryos.";
RL Dev. Cell 3:113-125(2002).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=14534135; DOI=10.1242/dev.00790;
RA Tsou M.-F.B., Hayashi A., Rose L.S.;
RT "LET-99 opposes Galpha/GPR signaling to generate asymmetry for spindle
RT positioning in response to PAR and MES-1/SRC-1 signaling.";
RL Development 130:5717-5730(2003).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12730122; DOI=10.1101/gad.1081203;
RA Srinivasan D.G., Fisk R.M., Xu H., van den Heuvel S.;
RT "A complex of LIN-5 and GPR proteins regulates G protein signaling and
RT spindle function in C elegans.";
RL Genes Dev. 17:1225-1239(2003).
CC -!- FUNCTION: During early embryogenesis, controls asymmetric cell division
CC and the asymmetric localization of P granules of germline precursor P2
CC and its descendant P3 (PubMed:7555722). Probably upstream of tyrosine
CC kinase src-1, plays a role in endoderm development by controlling
CC spindle orientation during EMS blastomere cell division
CC (PubMed:12110172). Controls EMS spindle orientation probably by
CC promoting lin-5 and gpr-1/2 enrichment at, and let-99 exclusion from
CC the junction between P2 and EMS cells (PubMed:14534135,
CC PubMed:12730122). {ECO:0000269|PubMed:12110172,
CC ECO:0000269|PubMed:12730122, ECO:0000269|PubMed:14534135,
CC ECO:0000269|PubMed:7555722}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11003841,
CC ECO:0000269|PubMed:12110172}; Single-pass type I membrane protein
CC {ECO:0000305}. Note=Localizes at the site of contact between EMS and P2
CC cells in the 4-cell stage embryo, between P3 and E cells in the 12-cell
CC stage embryo and between P4 and Ep cells in the 26-cell stage embryo.
CC {ECO:0000269|PubMed:11003841, ECO:0000269|PubMed:12110172}.
CC -!- DEVELOPMENTAL STAGE: Expressed at least in P2 germline cell at 4-cell
CC stage and up to 26-cell stage embryos (PubMed:11003841,
CC PubMed:12110172). Expressed only at L4 stage during larval development
CC and then accumulates in adults (PubMed:11003841).
CC {ECO:0000269|PubMed:11003841, ECO:0000269|PubMed:12110172}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: 71 percent of embryos of mutant mothers develop
CC into sterile adults with extra body muscle cells at the restrictive
CC temperature (25 degrees Celsius) (PubMed:7555722). Low embryonic
CC lethality (7-8 percent) (PubMed:7555722). Loss of lin-5 and grp-1/2
CC enrichment at the EMS/P2 cell boundaries at the 4-cell embryonic stage
CC (PubMed:12730122). Decrease in phosphotyrosine levels at the site of
CC contact between P2 and EMS cells (PubMed:12110172).
CC {ECO:0000269|PubMed:12110172, ECO:0000269|PubMed:12730122,
CC ECO:0000269|PubMed:7555722}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; AF200199; AAF13716.1; -; mRNA.
DR EMBL; BX284606; CAA91758.2; -; Genomic_DNA.
DR PIR; T22681; T22681.
DR RefSeq; NP_741906.1; NM_171780.4.
DR AlphaFoldDB; G5EBL2; -.
DR SMR; G5EBL2; -.
DR IntAct; G5EBL2; 1.
DR STRING; 6239.F54F7.5; -.
DR EPD; G5EBL2; -.
DR PaxDb; G5EBL2; -.
DR EnsemblMetazoa; F54F7.5.1; F54F7.5.1; WBGene00003219.
DR GeneID; 181362; -.
DR KEGG; cel:CELE_F54F7.5; -.
DR CTD; 181362; -.
DR WormBase; F54F7.5; CE28237; WBGene00003219; mes-1.
DR eggNOG; ENOG502TGP9; Eukaryota.
DR GeneTree; ENSGT00940000176578; -.
DR HOGENOM; CLU_296878_0_0_1; -.
DR OrthoDB; 219129at2759; -.
DR SignaLink; G5EBL2; -.
DR PRO; PR:G5EBL2; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003219; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:WormBase.
DR GO; GO:0008356; P:asymmetric cell division; IMP:WormBase.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:WormBase.
DR GO; GO:0001708; P:cell fate specification; IMP:WormBase.
DR GO; GO:0003006; P:developmental process involved in reproduction; IMP:UniProtKB.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:UniProtKB.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:WormBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:WormBase.
DR GO; GO:0007276; P:gamete generation; IMP:WormBase.
DR GO; GO:0070986; P:left/right axis specification; IGI:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cell membrane; Glycoprotein;
KW Membrane; Mitosis; Nucleotide-binding; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..966
FT /note="Protein mes-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5005349097"
FT TOPO_DOM 20..470
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..966
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 656..966
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 662..670
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 685
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 89
FT /note="G->E: In q367; 12 percent of mutant mothers' progeny
FT is sterile at the permissive temperature (16 degrees
FT Celsius) and 79 percent at the restrictive temperature (25
FT degrees Celsius). Low levels of embryonic lethality."
FT /evidence="ECO:0000269|PubMed:7555722"
FT MUTAGEN 441
FT /note="S->N: In q222; 6 percent of mutant mothers' progeny
FT is sterile at the permissive temperature (16 degrees
FT Celsius) and 77 percent at the restrictive temperature (25
FT degrees Celsius). Low levels of embryonic lethality."
FT /evidence="ECO:0000269|PubMed:7555722"
SQ SEQUENCE 966 AA; 108898 MW; 07B0000EBA14437F CRC64;
MKIHHFLTLL CTFLPLTTTA LTNSTPLSLL GPCYKRCVTK FGETKEQLTN AETISLEYDV
SNNTEFSLCK LGCNSHEYTD LNLAAFRYGQ LAYQKILTTV EDVPTRGTVL NDVFIVCLDT
SFMPSNNSAP SAKRLLSGTV LLVLDEDVAK ADNVFLIEVL ARNADKSAVQ VISQQWCYSS
NCNITFNAPT EVSSFDVRLR VSTFDSNGQV GGINFSKWHN INQILTKTFV DMSLKSVVWK
AEKAAANFVF NLTASDHVPA CSLQMIYRSS LSSELLHRNF YLDHTLEVFV NNLDFDKIYT
MQLAPSGTHD RSTPSLASAV IEIPPCRHLV DDYSMCAPPP VSSLSYNWNL SPTSEYELLI
KWKLLNYMDG LNVTEELSIP VAYFLLNAHP LITANNEQCE KYEKIRRVVS YGLRELVFHV
PDTDCNYEVE MTAVDTNQRI SEVKKIQVFR FNVPPYVSFL QASDIPTSVE LMAVVLATSA
IFALIALFLL YRKRKRDKKA RFQMYKDAEA GVSYDYVATT ESLGSVVQIR STNFRFEPVE
NIDGNIEAAL AQQQKFEGGT MNSMFRTYYN LDHPVKVPAH MAEASSDEDN GYENIRYSYF
GSELSDDVFE EDIYMTHKSL SIYCQDSPLT TPMAPIAPYE HFDDIPSHQY RNFQVHNFNE
RIEKQAYWLM ATVVDVVRRE LYSLKVPKDY TPETISAMRK ELEFLRTLAP HGNCRRFEGV
VIGRWDDLPR QVIGILIENT RGGTLRNYIA AVGSVFRNCS LATDHDSFAS QQDMNSTQHP
FDKLSTEADE NNSKKVKIQE ITDSLSIRFC QFAEQVSSAL EHLHSAGSVH TRVTTLNIYL
LHNYSDPFDM LPDQVVKLGN FGFAVQNSED VVLDDNLQPP EVIKGEKYEA RGDIWQFGLC
LAEMCSLGDL EQSEVGTLKS GHDTFKNLPS TQVLRDAAKR CLSARTRPSA SDLCGVFKSV
NVAATV
