SPKA_DICDI
ID SPKA_DICDI Reviewed; 638 AA.
AC Q86AT8; Q23859; Q557I8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Stress-activated protein kinase alpha;
DE Short=SAPK-alpha;
DE EC=2.7.11.1;
GN Name=spkA-1; ORFNames=DDB_G0273445;
GN and
GN Name=spkA-2; ORFNames=DDB_G0273531;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, MUTAGENESIS OF LYS-378,
RP AUTOPHOSPHORYLATION, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP F-ACTIN.
RX PubMed=14593072; DOI=10.1091/mbc.e03-01-0039;
RA Sun B., Ma H., Firtel R.A.;
RT "Dictyostelium stress-activated protein kinase alpha, a novel stress-
RT activated mitogen-activated protein kinase kinase kinase-like kinase, is
RT important for the proper regulation of the cytoskeleton.";
RL Mol. Biol. Cell 14:4526-4540(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-411.
RC STRAIN=AX3;
RA Mueller-Taubenberger A., Gerisch G.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=17878305; DOI=10.1073/pnas.0705996104;
RA Van Driessche N., Alexander H., Min J., Kuspa A., Alexander S.,
RA Shaulsky G.;
RT "Global transcriptional responses to cisplatin in Dictyostelium discoideum
RT identify potential drug targets.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15406-15411(2007).
CC -!- FUNCTION: May be involved in cortical F-actin organization and
CC resistance to osmotic stress. Activated upon cell detachment, in vitro.
CC {ECO:0000269|PubMed:14593072}.
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 F-actin. {ECO:0000269|PubMed:14593072}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14593072}. Note=Associated with the cytoskeletal
CC cortex in response to chemoattractant stimulation. Colocalizes with F-
CC actin in F-actin-enriched structures, including membrane ruffles and
CC pseudopodia during chemotaxis.
CC -!- DEVELOPMENTAL STAGE: There are 2 transcripts. The smaller transcript is
CC high in vegetative cells and during early development and rapidly
CC decreases after 12 hours, the time of tipped aggregate formation. A
CC larger transcript occurs at 8 hours of development, remains high
CC through the 12 hours time point, and then decreases, like the smaller
CC transcript. {ECO:0000269|PubMed:14593072}.
CC -!- PTM: Autophosphorylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA80242.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY353245; AAQ57595.1; -; mRNA.
DR EMBL; AAFI02000010; EAL70677.1; -; Genomic_DNA.
DR EMBL; AAFI02000010; EAL70720.1; -; Genomic_DNA.
DR EMBL; U36938; AAA80242.1; ALT_FRAME; mRNA.
DR RefSeq; XP_644604.1; XM_639512.1.
DR RefSeq; XP_644647.1; XM_639555.1.
DR AlphaFoldDB; Q86AT8; -.
DR SMR; Q86AT8; -.
DR STRING; 44689.DDB0185206; -.
DR PaxDb; Q86AT8; -.
DR EnsemblProtists; EAL70677; EAL70677; DDB_G0273445.
DR EnsemblProtists; EAL70720; EAL70720; DDB_G0273531.
DR GeneID; 8618968; -.
DR GeneID; 8619009; -.
DR KEGG; ddi:DDB_G0273445; -.
DR KEGG; ddi:DDB_G0273531; -.
DR dictyBase; DDB_G0273445; spkA-1.
DR dictyBase; DDB_G0273531; spkA-2.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_020450_0_0_1; -.
DR InParanoid; Q86AT8; -.
DR OMA; NSITWET; -.
DR PhylomeDB; Q86AT8; -.
DR PRO; PR:Q86AT8; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:dictyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0050793; P:regulation of developmental process; IMP:dictyBase.
DR GO; GO:0006970; P:response to osmotic stress; IDA:dictyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ANK repeat; ATP-binding; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..638
FT /note="Stress-activated protein kinase alpha"
FT /id="PRO_0000354063"
FT REPEAT 43..72
FT /note="ANK 1"
FT REPEAT 80..109
FT /note="ANK 2"
FT REPEAT 113..146
FT /note="ANK 3"
FT REPEAT 150..181
FT /note="ANK 4"
FT REPEAT 185..214
FT /note="ANK 5"
FT REPEAT 219..248
FT /note="ANK 6"
FT DOMAIN 240..303
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 351..620
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 472
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 357..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 378
FT /note="K->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:14593072"
FT CONFLICT 99
FT /note="V -> G (in Ref. 4; AAA80242)"
FT /evidence="ECO:0000305"
FT CONFLICT 347..348
FT /note="ND -> KY (in Ref. 4; AAA80242)"
FT /evidence="ECO:0000305"
FT CONFLICT 409..411
FT /note="HFY -> PEF (in Ref. 4; AAA80242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 72983 MW; 4897A1A6EA62194A CRC64;
MSSTQQQQHQ LFSAVEQNDV TKVKKLSSKK KISKSNLTSF DQYGQSALTI ALKNNNEEMV
ELLLSLCVTL KADINTFDKN GFSALHQAVS SDDRILMRVL QYENINVDVQ NDDLNTPIHY
FCQKFRSPNC QEPFQLFIQK GVNVNAQNKN GETPLHKAIF NNSVRLMMVG LLLKNGANVN
LATQFQESPL HYAVRLGRED LVSVLLKAGA DVDCVGTKER KTPYQLAVEE GNKDMTARIK
KYKDLFDWLQ KHGFEQYKDA FLKEEMFLDE LGEMSEDILN KMGITSTGTR LRILKETSNL
ANEQTKKPKT PELIIEEDPT PPDTPDISGL RHSLHTLRHV GEVNIINDNE LEYTEKLGAG
SSGKVYKGLY RGKEVAIKVL KSMTESKEIE EFKKEFQIMS AIRSKHVVHF YGAVLEPKLC
MVMENCSRGS LYHVMDNNSL DIGWERTFRF AIETVRGIEC LHKWDPPIVH RDLKSLNLLV
NDKWEIKVCD FGLSRFNTGS NLETLVKMRG TFAYCAPEVY YGEQFSGKSD VYSIAVILWE
LVTRCINGRY ERPFSEYKNL QHDFQIIIQT AKKNLRPTIP NACPESLVSL IQDCWDPNLE
NRPTCTDILS RLVTIENEYR SNIQTWNNLI VPLPKNQE
