SMA5_CAEEL
ID SMA5_CAEEL Reviewed; 509 AA.
AC G5EBT1; G5EBE9; G5EBM8; G5EDH5;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Mitogen-activated protein kinase sma-5 {ECO:0000305|PubMed:15944183};
DE EC=2.7.11.24 {ECO:0000250|UniProtKB:Q13164};
GN Name=sma-5 {ECO:0000312|WormBase:W06B3.2c};
GN ORFNames=W06B3.2 {ECO:0000312|WormBase:W06B3.2c};
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:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND D), FUNCTION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15944183; DOI=10.1242/dev.01895;
RA Watanabe N., Nagamatsu Y., Gengyo-Ando K., Mitani S., Ohshima Y.;
RT "Control of body size by SMA-5, a homolog of MAP kinase BMK1/ERK5, in C.
RT elegans.";
RL Development 132:3175-3184(2005).
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.
RX PubMed=17535251; DOI=10.1111/j.1365-2443.2007.01077.x;
RA Watanabe N., Ishihara T., Ohshima Y.;
RT "Mutants carrying two sma mutations are super small in the nematode C.
RT elegans.";
RL Genes Cells 12:603-609(2007).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the postembryonic
CC regulation of body size, mainly through control of cell growth. In
CC particular, controls the volume of intestine, muscles and hypodermis.
CC In addition, regulates growth, intestinal granule distribution,
CC lifespan and number of offspring. {ECO:0000269|PubMed:15944183,
CC ECO:0000269|PubMed:17535251}.
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=2.7.11.24;
CC Evidence={ECO:0000250|UniProtKB:Q13164};
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=2.7.11.24; Evidence={ECO:0000250|UniProtKB:Q13164};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q13164};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=c {ECO:0000312|WormBase:W06B3.2c};
CC IsoId=G5EBT1-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:W06B3.2a};
CC IsoId=G5EBT1-2; Sequence=VSP_057670, VSP_057671;
CC Name=b {ECO:0000312|WormBase:W06B3.2b};
CC IsoId=G5EBT1-3; Sequence=VSP_057670;
CC Name=d {ECO:0000312|WormBase:W06B3.2d};
CC IsoId=G5EBT1-4; Sequence=VSP_057669, VSP_057671;
CC -!- TISSUE SPECIFICITY: Expressed in intestine with a stronger expression
CC in the four most anterior cells, muscles, excretory cell, pharynx and,
CC to a lesser extent, in hypodermis. {ECO:0000269|PubMed:15944183}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in an
CC approximately 50 percent reduction in number of offspring.
CC {ECO:0000269|PubMed:15944183}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; BX284606; CAA18361.3; -; Genomic_DNA.
DR EMBL; BX284606; CAD44158.1; -; Genomic_DNA.
DR EMBL; BX284606; CAJ21562.1; -; Genomic_DNA.
DR EMBL; BX284606; CAJ55250.1; -; Genomic_DNA.
DR PIR; T20076; T20076.
DR RefSeq; NP_001033572.1; NM_001038483.5.
DR RefSeq; NP_001041297.1; NM_001047832.1. [G5EBT1-1]
DR RefSeq; NP_741908.1; NM_171782.3. [G5EBT1-3]
DR RefSeq; NP_741909.1; NM_171783.3.
DR AlphaFoldDB; G5EBT1; -.
DR SMR; G5EBT1; -.
DR STRING; 6239.W06B3.2c; -.
DR EPD; G5EBT1; -.
DR PaxDb; G5EBT1; -.
DR PeptideAtlas; G5EBT1; -.
DR EnsemblMetazoa; W06B3.2a.1; W06B3.2a.1; WBGene00004859. [G5EBT1-2]
DR EnsemblMetazoa; W06B3.2a.2; W06B3.2a.2; WBGene00004859. [G5EBT1-2]
DR EnsemblMetazoa; W06B3.2b.1; W06B3.2b.1; WBGene00004859. [G5EBT1-3]
DR EnsemblMetazoa; W06B3.2c.1; W06B3.2c.1; WBGene00004859. [G5EBT1-1]
DR EnsemblMetazoa; W06B3.2d.1; W06B3.2d.1; WBGene00004859. [G5EBT1-4]
DR GeneID; 181373; -.
DR KEGG; cel:CELE_W06B3.2; -.
DR CTD; 181373; -.
DR WormBase; W06B3.2a; CE31629; WBGene00004859; sma-5. [G5EBT1-2]
DR WormBase; W06B3.2b; CE31630; WBGene00004859; sma-5. [G5EBT1-3]
DR WormBase; W06B3.2c; CE39526; WBGene00004859; sma-5. [G5EBT1-1]
DR WormBase; W06B3.2d; CE38984; WBGene00004859; sma-5. [G5EBT1-4]
DR eggNOG; KOG0660; Eukaryota.
DR InParanoid; G5EBT1; -.
DR OMA; CYYMTQH; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; G5EBT1; -.
DR Reactome; R-CEL-198753; ERK/MAPK targets.
DR Reactome; R-CEL-198765; Signalling to ERK5.
DR Reactome; R-CEL-202670; ERKs are inactivated.
DR PRO; PR:G5EBT1; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004859; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
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:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0040024; P:dauer larval development; IGI:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
DR GO; GO:0051640; P:organelle localization; IMP:UniProtKB.
DR GO; GO:0007567; P:parturition; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:UniProtKB.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IGI:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..509
FT /note="Mitogen-activated protein kinase sma-5"
FT /id="PRO_0000433093"
FT DOMAIN 105..411
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 19..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 111..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_057669"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform a and isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057670"
FT VAR_SEQ 467..509
FT /note="DSTGSTSDMSTNTSGEYSPIAQHEQLLEDVATQISICEPTCDL -> GDYNT
FT WIAGVFQSERSREIIKNEYSTSSYTSPELDREYIGHVNQYQRGILSNCAA (in
FT isoform a and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_057671"
SQ SEQUENCE 509 AA; 57584 MW; 126DCE673B784DDA CRC64;
MVFADFLEKI KSLFAKTKDP ITSMSPPQEN RSPKAEYLNN FFNTNPTNGK SRGSQEAPRK
PLGQTNLNVQ GSMPAKKEGF NRVLDGLKKR QLQHDFKLER AAETYEPTQN IGSGAFGIVC
EAVETSSNQK VAIKKVAHAS ATPTLARRTL REIRVLRYIN HPNIVPLRDI FRTKGPLGID
VFLVMDLMQN NLHHIIYGNE DPLEEHYINA FLGQLLRGLE YLHAACIAHR DLKPSNLLVN
QDGTLRIADF GMAKCADNSS KKHDDEEHCY YMTQHVATLP YRAPELLFVL PEHSTAVDMW
AVGCIFGEMV IRNEILPGRS VQGQIKMLLT MLGQPPQEVI NEVRCDRTRK LIQDFGRKAD
AEWDDIMFCK ARGDDQIVRG NCDTIDFVKQ LFQYDAQKRI NIQDALLHPY IQRVIPAEAP
QKKCPFRVKK DMMQVEDLNH QELISMMKQD VRSAENPITY SELHSGDSTG STSDMSTNTS
GEYSPIAQHE QLLEDVATQI SICEPTCDL
