SPK1_CAEEL
ID SPK1_CAEEL Reviewed; 1003 AA.
AC Q03563; Q9XVX9; Q9XVY0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Serine/threonine-protein kinase spk-1;
DE EC=2.7.11.1;
GN Name=spk-1; Synonyms=rsk-1, srk-1; ORFNames=B0464.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11091073; DOI=10.1016/s0925-4773(00)00477-9;
RA Kuroyanagi H., Kimura T., Wada K., Hisamoto N., Matsumoto K., Hagiwara M.;
RT "SPK-1, a C. elegans SR protein kinase homologue, is essential for
RT embryogenesis and required for germline development.";
RL Mech. Dev. 99:51-64(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=10747030; DOI=10.1093/emboj/19.7.1625;
RA Longman D., Johnstone I.L., Caceres J.F.;
RT "Functional characterization of SR and SR-related genes in Caenorhabditis
RT elegans.";
RL EMBO J. 19:1625-1637(2000).
CC -!- FUNCTION: Required for embryogenesis and germline development in both
CC adult hermaphrodites and males. SR-protein kinase (SRPK) that binds
CC directly to and phosphorylates the RS domain of rsp-3/CeSF2 in vitro.
CC {ECO:0000269|PubMed:10747030, ECO:0000269|PubMed:11091073}.
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 -!- 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;
CC -!- SUBUNIT: Interacts with rsp-3.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=Q03563-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q03563-2; Sequence=VSP_012277, VSP_012278, VSP_012309,
CC VSP_012310, VSP_012280;
CC Name=c;
CC IsoId=Q03563-3; Sequence=VSP_012277, VSP_012278, VSP_012309,
CC VSP_012310, VSP_012279;
CC -!- TISSUE SPECIFICITY: Predominantly coexpressed with rsp-3 in adult
CC hermaphrodite germlines. {ECO:0000269|PubMed:11091073}.
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; AF241656; AAG36873.1; -; mRNA.
DR EMBL; Z19152; CAA79540.2; -; Genomic_DNA.
DR EMBL; Z19152; CAA79541.1; -; Genomic_DNA.
DR EMBL; Z19152; CAA79542.2; -; Genomic_DNA.
DR PIR; E88556; E88556.
DR PIR; F88556; F88556.
DR PIR; S28282; S28282.
DR RefSeq; NP_001021133.1; NM_001025962.2. [Q03563-2]
DR RefSeq; NP_001021134.1; NM_001025963.4. [Q03563-3]
DR RefSeq; NP_499080.3; NM_066679.4. [Q03563-1]
DR AlphaFoldDB; Q03563; -.
DR SMR; Q03563; -.
DR BioGRID; 41525; 46.
DR DIP; DIP-26907N; -.
DR IntAct; Q03563; 30.
DR STRING; 6239.B0464.5a.1; -.
DR EPD; Q03563; -.
DR PaxDb; Q03563; -.
DR PeptideAtlas; Q03563; -.
DR PRIDE; Q03563; -.
DR EnsemblMetazoa; B0464.5a.1; B0464.5a.1; WBGene00004980. [Q03563-1]
DR EnsemblMetazoa; B0464.5a.2; B0464.5a.2; WBGene00004980. [Q03563-1]
DR EnsemblMetazoa; B0464.5b.1; B0464.5b.1; WBGene00004980. [Q03563-2]
DR EnsemblMetazoa; B0464.5c.1; B0464.5c.1; WBGene00004980. [Q03563-3]
DR GeneID; 176328; -.
DR KEGG; cel:CELE_B0464.5; -.
DR UCSC; B0464.5b.1; c. elegans. [Q03563-1]
DR CTD; 176328; -.
DR WormBase; B0464.5a; CE36580; WBGene00004980; spk-1. [Q03563-1]
DR WormBase; B0464.5b; CE20457; WBGene00004980; spk-1. [Q03563-2]
DR WormBase; B0464.5c; CE36373; WBGene00004980; spk-1. [Q03563-3]
DR eggNOG; KOG1290; Eukaryota.
DR GeneTree; ENSGT00940000170102; -.
DR InParanoid; Q03563; -.
DR OMA; IEKYEWP; -.
DR OrthoDB; 290680at2759; -.
DR PhylomeDB; Q03563; -.
DR SignaLink; Q03563; -.
DR PRO; PR:Q03563; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004980; Expressed in germ line (C elegans) and 5 other tissues.
DR ExpressionAtlas; Q03563; baseline and differential.
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:0004672; F:protein kinase activity; IDA:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR GO; GO:0000245; P:spliceosomal complex assembly; IBA:GO_Central.
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; 2.
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; Developmental protein; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1003
FT /note="Serine/threonine-protein kinase spk-1"
FT /id="PRO_0000086672"
FT DOMAIN 422..904
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 92..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 555
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 428..436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..229
FT /note="Missing (in isoform b and isoform c)"
FT /evidence="ECO:0000303|PubMed:11091073"
FT /id="VSP_012277"
FT VAR_SEQ 230..287
FT /note="IESQEAEESATEDLASCHSNDDKNEKDVLVDEDTSKYDNLPVEMRSAKEGEE
FT SEGTID -> MGGPEKNSTVPLPNKKRKKKTNKKKPTAPNTPTSPQAGEKNANLKNGTV
FT TTNGSNHVE (in isoform b and isoform c)"
FT /evidence="ECO:0000303|PubMed:11091073"
FT /id="VSP_012278"
FT VAR_SEQ 288..346
FT /note="Missing (in isoform b and isoform c)"
FT /evidence="ECO:0000303|PubMed:11091073"
FT /id="VSP_012309"
FT VAR_SEQ 347
FT /note="K -> R (in isoform b and isoform c)"
FT /evidence="ECO:0000303|PubMed:11091073"
FT /id="VSP_012310"
FT VAR_SEQ 651
FT /note="P -> PQNGVRMRPPSLLFNGPIPQLLQGSSCVNTPSSPRTVPPPPPSLYPQ
FT VGCVCNQTYHLTQ (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_012279"
FT VAR_SEQ 983..999
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:11091073"
FT /id="VSP_012280"
SQ SEQUENCE 1003 AA; 112527 MW; 294E6E4DC0784FDF CRC64;
MFVVLFCRWL NGFSQHRERL YKFEDEAVQR RRRFRVHSEE SEELNDHESY SETDICTQLL
ASSADVTCHI NVDLVNQNRF YFFVKQRNKK ENSTNEEEEI SSQEINTSTQ NEETEVNLVF
ASAEDNGGVA SNFDISDALM VTSNISEVSK LPETLCEEGE TVQQKSVVNE NDHSNEDDEQ
SLQSQDGSRC SDEDMNSCVS ASDEEDVESQ DDSFHVNDAT EESIDSVSSI ESQEAEESAT
EDLASCHSND DKNEKDVLVD EDTSKYDNLP VEMRSAKEGE ESEGTIDSSV SSSTSSSSTG
DDGDDSATSY DSEDIEIQMF EYDLGTACAS ASISIPRPSI IPRNNKKTEV NANEERLDDL
SVSPGRSDSP GGGGGGHSDS FQDPMDPGEQ LGSDDEEQED PRDYKRGGYH PVNIGDVFNA
RYHVIRKLGW GHFSTVWLAW DTQDKRFVAM KIVKSAEHYT EAALDEIKLL LSVRSADPND
IGCHKVVQLL DEFTVTGING QHVAMVFEVL GCNLLKLIIR SNYRGLHLEQ VRKICRQVLE
ALGYMHEKCG IIHTDIKPEN VLITMSREEI KIMAQHAVVA RKMNMKMSGS AVSTAPDHLV
KMAQENMTKN KKKKMKKKAK KQREKLEAEL AGLEGLKMDA NGLQEAYNNA PELENFNASQ
VEDVTMEDTV NENGNRNKVE IRSPDRFDRT TLTPFSDPES KFGDLASPSA EYLSSPMSQL
PPGGILPAPP VGPNIGDPYC DIDVKIADLG NACWVNHHYT DDIQTRQYRA LEVLIGSGYG
PPADIWSTAC MAFELATGDY LFEPHQGDNY SRDEDHLAHI SELLGAIPPS IYKKGKHWRE
FFHKNGHLLH IHQLKPWSLY EVLRQKYEWS HEDAQQFESF LRPMLDFDQE KRSTAKIALK
HPFLLPFGGR APKSDCPPEL LSKMFPDGLI PEPFDGNEHQ EVYRDENDSR SASERSANSR
SAGGSDDDDE EEFNMNRPGP SGVITNNETT DISDIERFQL DLQ
