SPLA_DICDI
ID SPLA_DICDI Reviewed; 2410 AA.
AC P18160; Q54R51;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Dual specificity protein kinase splA;
DE EC=2.7.10.2;
DE AltName: Full=Non-receptor tyrosine kinase spore lysis A;
DE AltName: Full=Tyrosine-protein kinase 1;
GN Name=splA; Synonyms=DpyK1, pyK1, pykA; ORFNames=DDB_G0283385;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 827-2410, AUTOPHOSPHORYLATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=JH10;
RX PubMed=8898241; DOI=10.1242/dev.122.10.3295;
RA Nuckolls G.H., Osherov N., Loomis W.F., Spudich J.A.;
RT "The Dictyostelium dual-specificity kinase splA is essential for spore
RT differentiation.";
RL Development 122:3295-3305(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2074-2410.
RX PubMed=1972546; DOI=10.1128/mcb.10.7.3578-3583.1990;
RA Tan J.L., Spudich J.A.;
RT "Developmentally regulated protein-tyrosine kinase genes in Dictyostelium
RT discoideum.";
RL Mol. Cell. Biol. 10:3578-3583(1990).
CC -!- FUNCTION: Essential for spore differentiation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- DEVELOPMENTAL STAGE: Expressed in vegetative cells and throughout
CC development with a peak during the mound stage of morphogenesis.
CC {ECO:0000269|PubMed:8898241}.
CC -!- PTM: Tyrosine kinase domain is capable of autophosphorylation, in
CC vitro; however it is also autophosphorylated on serine and threonine
CC residues.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Tyr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000055; EAL65677.1; -; Genomic_DNA.
DR EMBL; U32174; AAB41125.1; -; Genomic_DNA.
DR EMBL; M33785; AAA33202.1; -; mRNA.
DR PIR; T18276; T18276.
DR RefSeq; XP_639040.1; XM_633948.1.
DR AlphaFoldDB; P18160; -.
DR SMR; P18160; -.
DR STRING; 44689.DDB0252636; -.
DR PaxDb; P18160; -.
DR EnsemblProtists; EAL65677; EAL65677; DDB_G0283385.
DR GeneID; 8624065; -.
DR KEGG; ddi:DDB_G0283385; -.
DR dictyBase; DDB_G0283385; splA.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_229194_0_0_1; -.
DR InParanoid; P18160; -.
DR OMA; QYRKNFR; -.
DR BRENDA; 2.7.12.1; 1939.
DR Reactome; R-DDI-5673000; RAF activation.
DR Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:P18160; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:dictyBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:dictyBase.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IMP:dictyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR CDD; cd12885; SPRY_RanBP_like; 3.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.120.920; -; 3.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_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; IPR003877; SPRY_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR044736; Vid30/RanBPM/SPLA_SPRY.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF00622; SPRY; 3.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00449; SPRY; 3.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF49899; SSF49899; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50188; B302_SPRY; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..2410
FT /note="Dual specificity protein kinase splA"
FT /id="PRO_0000088121"
FT DOMAIN 822..1004
FT /note="B30.2/SPRY 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 1020..1209
FT /note="B30.2/SPRY 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 1481..1703
FT /note="B30.2/SPRY 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 1734..1798
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 2115..2387
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1862..2105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..596
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..644
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..749
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1863..1881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1916..1930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1939..1977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1984..2005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2015..2086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2087..2104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2243
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 2121..2129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 2142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 2074
FT /note="D -> R (in Ref. 3; AAA33202)"
FT /evidence="ECO:0000305"
FT CONFLICT 2261
FT /note="V -> L (in Ref. 3; AAA33202)"
FT /evidence="ECO:0000305"
FT CONFLICT 2282
FT /note="M -> K (in Ref. 2; AAB41125 and 3; AAA33202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2410 AA; 264919 MW; 768EC59E9E05C229 CRC64;
MNSKNDLFIG FFFFFYNYYY YYNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNIYIIVIIG
LDPQQNHPSL KIPPPPSPTS PYVRRHARQH SRSNSSNSPG ELTGGVEIIQ QQNSINTQTS
PPTSTSPNTV PPPPPTNTTT SSTTITRNSN NINNSNGGII NSSSGSNINN SSSSGVINTN
INNSGGNISP TSNSLPSSNN NILYTSSGSN SGNNNNNNNT INISSGSSGI NNSSNSNINN
NNNNNSSSSS GIHASGSLTA IPTNTNSNSS IFHSSNSVNR INKSNYSADS LVLPPNRISQ
VPQSQTQPQL QISPSTSFSS QQQQQQQLQQ QLQLQQQLQQ QIQQQQQIQQ QQNLHFTYSK
TFTSGQPNTL VNLSSPPPQS KHLHVSSDHS FFNEVLTPTP VIHNSTNQNN QLLFGDSDPL
SFLEYNNFIN RYQPALKNNQ PVSSYRQQQQ IQHQIQLQQI QQQQQQQQQI QQQQLQQQQQ
IQQQQIQQQQ QQIQQQQQQQ QQQQQQQQQL QQIQPPPTIQ PPPQQTTPTL RGNRSSGNLS
GLNSFSLKQS TDSLTPPPNS QQSTVSSNST PIAATPISPL TAPTSPPPPP PPPTNFNSKF
NNNNNNNINN SSNNNTTVPP SPPPIIVLPK SPSSRSPRPA SAPVPSAPFL VNNRVINTSS
SSNISTNNTD LNLSSSSSSS PPLNISTASP SKSEDSPPTV SPSYKQQQQQ QQQQQQQQQQ
LNNSSNSSYS PKPRSPSVSS PPPSSISPNS SPIGSPNISF HHHQQHQIPP PPPVLSNTNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NTNHTNKKEG DSSWFNMSFK FFKKKLVPSN
EYRWDLRKSN SLTLNIEDKS RCSYRLPTSG SKGIAKSTQP FSSSFTYFEL FITNGNGDKI
CFGLTTNDHP IEVYPGNYQG SYGYSGDGKC YFGTNEGRVY GPSFSSGDVV GCGYDSSSKT
LYFTKNGVYL GVAAQKVNLI GLYPTVGLQN PGESVVINFF GPFSYRGAPE KPSKQSTIKD
SGGSSIIPSE DLIPKEEFEV CRWSEKKNYH GKHVVVRNRT AFLPLDSPKD TIGGVRATQP
FGEGFCYFEV IIDQLDKGQL SIGLANLEYP TFYHVGWMPR SYGYHNDDGR KFRWREEPGV
NEGESYGSSY KKGDIIGCGL SFTSREIFFT KNGMYLGTAF SNVYGVFYPS VAFNEPGISI
TGVFGPPFKF SQVTLMLKNV NSTSILVPNG NNNNNSNNNN NNNNNNIIGN GKITTTTTTS
TSPSSINNNE DISSNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNSNSSNT NNNNINNTTN
NNNSNSNNNN NNNNSNSNSN SNNNNINNNN NNNNNNNNIY LTKKPSIGST DESSTGSLGG
NNSSGNNNSS SGSIGNNSSI IKQRSPPHSI NGPLMLPPSS TNNNNNIYSS YNSTTAGSST
TILPTLNHPI FGNTTSNNNS SSTLSVGGNN NLLGRHCQSL PITASTNHTL SSSLGVSFSS
PSSSPKTSPR KIVNSSEDLG FVQTFQDQDG QPPSAWRRCG KSIKTKDDIT LTIIKKKTSV
AMADRPFSSN SSSTICYFEV YLEGHDKKGS ITVGLSHSTY PFIKHIGREP KSYGFSSEGE
KYGGSEIGEP YGPFFFFDGD SIASSCVIGC GINTSTRDIF FTKNGHYLGV AFSRVTSDPL
YPSISFRGVV GGLCVATFPG GHFRFNIEDL PGISPSVWTE ALGPDRQGSG FKNWAPNDVA
IWLESFNYGQ YRKNFRDNNI SGRHLEGITH AMLKNDLGIE PYGHREDIIN RLNRMIQIWN
DKSPDSYPKI AIDSSDKIRW PASGGSSGGI NISGGVVIGS SSGSDDGITE ISSSSKNIRP
YKSYTQKEIE DRNRRSTISG GEKKNKYYID NQMDPHQIGS MDSDGLLPDF GQGPPDEKNS
SKTLSNEQIR YLQQRKDEPP IAISSTGNGG SVSSTGGSSG FLTFPSSNSL THPPQRDKPT
QEFTHLPPIT SNYKGITNTG QPHKSFDQPL ELFPRHSAFS NNGNNGNNNN NNNNNNIKAN
QQQQQQSSYQ QSQTQQQQQH ITSTSTSTTN KWIDPFGGWE TQSSLSHPPS RPPPPPPPPP
QLPVRSEYEI DFNELEFGQT IGKGFFGEVK RGYWRETDVA IKIIYRDQFK TKSSLVMFQN
EVGILSKLRH PNVVQFLGAC TAGGEDHHCI VTEWMGGGSL RQFLTDHFNL LEQNPHIRLK
LALDIAKGMN YLHGWTPPIL HRDLSSRNIL LDHNIDPKNP VVSSRQDIKC KISDFGLSRL
KMEQASQMTQ SVGCIPYMAP EVFKGDSNSE KSDVYSYGMV LFELLTSDEP QQDMKPMKMA
HLAAYESYRP PIPLTTSSKW KEILTQCWDS NPDSRPTFKQ IIVHLKEMED QGVSSFASVP
VQTIDTGVYA
