SEL5_CAEEL
ID SEL5_CAEEL Reviewed; 1077 AA.
AC G5ECQ3; G5EFY9;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Serine/threonine-protein kinase sel-5 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Suppressor/enhancer of lin-12 protein 5 {ECO:0000305};
GN Name=sel-5 {ECO:0000312|WormBase:F35G12.3a};
GN ORFNames=F35G12.3 {ECO:0000312|WormBase:F35G12.3a};
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|EMBL:AAF71545.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=10581273; DOI=10.1093/genetics/153.4.1641;
RA Fares H., Greenwald I.;
RT "SEL-5, a serine/threonine kinase that facilitates lin-12 activity in
RT Caenorhabditis elegans.";
RL Genetics 153:1641-1654(1999).
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).
CC -!- FUNCTION: Serine/threonine-protein kinase which may play a role in lin-
CC 12-mediated cell-fate decisions. {ECO:0000269|PubMed:10581273}.
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:0000305};
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:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Cytoplasm
CC {ECO:0000269|PubMed:10581273}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F35G12.3a};
CC IsoId=G5ECQ3-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F35G12.3b};
CC IsoId=G5ECQ3-2; Sequence=VSP_058058, VSP_058059;
CC -!- DISRUPTION PHENOTYPE: No obvious phenotype. RNAi-mediated knockdown
CC suppresses the egg laying defect of lin-12 n302 mutant. A similar
CC phenotype occurs in a lin-12 and sel-5 double mutant.
CC {ECO:0000269|PubMed:10581273}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF256466; AAF71545.1; -; mRNA.
DR EMBL; AF256467; AAF71546.1; -; mRNA.
DR EMBL; BX284603; CAA86326.1; -; Genomic_DNA.
DR EMBL; BX284603; CAA86332.1; -; Genomic_DNA.
DR PIR; T21800; T21800.
DR PIR; T21806; T21806.
DR RefSeq; NP_001022562.1; NM_001027391.6. [G5ECQ3-1]
DR RefSeq; NP_001022563.1; NM_001027392.5. [G5ECQ3-2]
DR AlphaFoldDB; G5ECQ3; -.
DR SMR; G5ECQ3; -.
DR IntAct; G5ECQ3; 2.
DR STRING; 6239.F35G12.3a; -.
DR EPD; G5ECQ3; -.
DR PaxDb; G5ECQ3; -.
DR PeptideAtlas; G5ECQ3; -.
DR EnsemblMetazoa; F35G12.3a.1; F35G12.3a.1; WBGene00004762. [G5ECQ3-1]
DR EnsemblMetazoa; F35G12.3b.1; F35G12.3b.1; WBGene00004762. [G5ECQ3-2]
DR GeneID; 175599; -.
DR KEGG; cel:CELE_F35G12.3; -.
DR CTD; 175599; -.
DR WormBase; F35G12.3a; CE00971; WBGene00004762; sel-5. [G5ECQ3-1]
DR WormBase; F35G12.3b; CE00972; WBGene00004762; sel-5. [G5ECQ3-2]
DR eggNOG; KOG1989; Eukaryota.
DR GeneTree; ENSGT00940000170379; -.
DR HOGENOM; CLU_286560_0_0_1; -.
DR InParanoid; G5ECQ3; -.
DR OMA; RYSYENI; -.
DR OrthoDB; 307406at2759; -.
DR PhylomeDB; G5ECQ3; -.
DR Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR SignaLink; G5ECQ3; -.
DR PRO; PR:G5ECQ3; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004762; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; IBA:GO_Central.
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:0045747; P:positive regulation of Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1077
FT /note="Serine/threonine-protein kinase sel-5"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435371"
FT DOMAIN 47..317
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 347..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..676
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..939
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 654..690
FT /note="ATDEDDERQLLSETDEEEKYEIDEKEEIQTKKDETIN -> GSVHLHTSIAP
FT SPLLRHVLTKAPPPVPRRTTSRGFQV (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058058"
FT VAR_SEQ 691..1077
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058059"
SQ SEQUENCE 1077 AA; 119996 MW; 3B7095A68CF807AE CRC64;
MPLGLFSSGK AQVLCDEKIP GGKKKEPKQL SENKCKGVTL KLDHTRVTIE KQIAEGGFAI
VYVASDRKNN KFALKRQFTK DNEKQLEACC REHSFLKQCI GHKNIVEFVD SYTNCLGNGI
WECMLLTEYH QKNVLQLMNE RISQNQYLTN DEILSIFTDL CEAVSFIHNR PQPIIHRDLK
VENVLISSHK PPHYVLCDFG SATTQILSVE KYGVEYVKSE VERNTTMCYR SPEMIDFYSG
LEIGLKSDIW ALGVLLYRLC FFCVPFEESP LAIQSVNYQF PSVPNIPDEI KVLIYMLLDI
DVNRRPSIYQ TSVLAFEANH RKPLSEEIQN KKCTDAVPSL KSCIQLMRDG SNPRNKRDSS
PRNPEAPPIQ SSSKMASLSQ QVPSISNISM PSGSGTVETS VAPRLRPKAT TVVPNVPSIS
PVPPVGLPHL RLPSKGSTDE TDGSQVRKVP IDFHHRQSFS GEEQLKPAAE ADSAGPLSCP
LIKPTDLGFT DLDKPALPRD RAQTDGKRRL PHESDIIFQQ QHRRNVSDTS QISRSAFKPY
SSQQTTSKTS SQVVRSVEDM SQRQNGGSGE WNPFLVAPFS NNSISRKDGQ ESAFMMDDSH
FGMVFDEIRR KEIPAELDSE TSSIDSRDPF GAAPFDQLTV STSSSAQPVS LPPATDEDDE
RQLLSETDEE EKYEIDEKEE IQTKKDETIN EEDSEIDEQR MNDRRRYSYE NIDGVGDDAS
SDSRGKTDRD DSEEEEDDDS RRGGDTSHDE DSQNTVGSED GEGGSRPLLE DDGLEDDDDH
ELISSFSSSS TNYPPLFIGT STPHTQNPIT NPFLRDELTP KMIITAPLPT AKNNLDDDWD
LGDRWTDRRD TVFERPASEH QNVFAPATLP RQATPLVCRF KPDLPTAAPV SIIPSMSNTS
FPEAVRDSDT VPCEPIIGTL ISVGAPTDPP PPPLPKKPTE ASPTQETTAT IPVALGKKEK
LLKKEKKKEK KDGKKDKLKL EEYREKGSSE PETDGSEAEI WTNDGATTFS NKKKKKSTFG
LRSSHPSIVA NDLQFSSPMP PVVKKSSKDK KSSLTGKNAS FVNTSFQPED HDDPTDL
