RCKA_DICDI
ID RCKA_DICDI Reviewed; 1125 AA.
AC Q54XQ2; Q8I811;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=RGS domain-containing serine/threonine-protein kinase A;
DE EC=2.7.11.1;
DE AltName: Full=RGS domain-containing serine/threonine-protein kinase 1;
GN Name=rckA; Synonyms=rck1; ORFNames=DDB_G0278737;
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], CHARACTERIZATION, DEVELOPMENTAL STAGE, ACTIVITY
RP REGULATION, MUTAGENESIS OF GLU-512; ASN-513; CYS-553 AND LYS-869,
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=12686622; DOI=10.1091/mbc.e02-08-0550;
RA Sun B., Firtel R.A.;
RT "A regulator of G protein signaling-containing kinase is important for
RT chemotaxis and multicellular development in dictyostelium.";
RL Mol. Biol. Cell 14:1727-1743(2003).
RN [2]
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 [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16596165; DOI=10.1371/journal.pgen.0020038;
RA Goldberg J.M., Manning G., Liu A., Fey P., Pilcher K.E., Xu Y., Smith J.L.;
RT "The dictyostelium kinome -- analysis of the protein kinases from a simple
RT model organism.";
RL PLoS Genet. 2:E38-E38(2006).
CC -!- FUNCTION: Serine/threonine kinase involved in negative regulation of
CC chemotaxis.
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 -!- ACTIVITY REGULATION: Up-regulated by cAMP.
CC {ECO:0000269|PubMed:12686622}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12686622}. Cell
CC membrane {ECO:0000269|PubMed:12686622}. Note=Translocates very rapidly
CC to the plasma membrane upon stimulation by chemoattractant, but no
CC polarized localization to the leading edge in aggregating cells.
CC -!- DEVELOPMENTAL STAGE: Very low expression in vegetative cells, but
CC increases dramatically at 4 hours after starvation and then rapidly
CC falls to very low levels throughout the remainder of development.
CC {ECO:0000269|PubMed:12686622}.
CC -!- DOMAIN: The RGS domain is involved in translocation to the plasma
CC membrane.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:12686622}.
CC -!- MISCELLANEOUS: RckA kinase activity remains elevated unless the
CC stimulus is removed and the kinase function is directly involved in
CC delocalizing the protein from the plasma membrane. However, the
CC membrane localization does not require a functional kinase domain and
CC seems not to be essential for the kinase activation.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AY163574; AAN80747.1; -; mRNA.
DR EMBL; AAFI02000024; EAL67970.1; -; Genomic_DNA.
DR RefSeq; XP_641978.1; XM_636886.1.
DR AlphaFoldDB; Q54XQ2; -.
DR SMR; Q54XQ2; -.
DR STRING; 44689.DDB0214828; -.
DR PaxDb; Q54XQ2; -.
DR EnsemblProtists; EAL67970; EAL67970; DDB_G0278737.
DR GeneID; 8621710; -.
DR KEGG; ddi:DDB_G0278737; -.
DR dictyBase; DDB_G0278737; rckA.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_279833_0_0_1; -.
DR InParanoid; Q54XQ2; -.
DR OMA; YLEIERY; -.
DR PRO; PR:Q54XQ2; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0061123; P:negative regulation of positive chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.10.167.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00315; RGS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1125
FT /note="RGS domain-containing serine/threonine-protein
FT kinase A"
FT /id="PRO_0000328051"
FT DOMAIN 487..603
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 842..1097
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 963
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 848..856
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 869
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 512
FT /note="E->G: Normal kinetics of aggregation, but delayed
FT multicellular development. Normal kinetics of aggregation,
FT but delayed multicellular development; when associated with
FT A-513."
FT /evidence="ECO:0000269|PubMed:12686622"
FT MUTAGEN 513
FT /note="N->A: Normal kinetics of aggregation, but delayed
FT multicellular development; when associated with G-512."
FT /evidence="ECO:0000269|PubMed:12686622"
FT MUTAGEN 553
FT /note="C->A: Normal kinetics of aggregation, but delayed
FT multicellular development."
FT /evidence="ECO:0000269|PubMed:12686622"
FT MUTAGEN 869
FT /note="K->A: Loss of kinase activity and increased rapidity
FT of aggregation, but delayed multicellular development."
FT /evidence="ECO:0000269|PubMed:12686622"
FT CONFLICT 293..294
FT /note="Missing (in Ref. 1; AAN80747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1125 AA; 125492 MW; BBB70416EC5D9A6A CRC64;
MKTSKDSSNS NSNNNNNNNN NNNNNNNNNN GLNGTYSSKS LSPPTSPKQM SGNSIISNST
GNLSSGSGSG SSSGGNKKFI NRSFNTFIDF IKKPARRNSK AHNTPPPYPE VDTGFGYFLE
LDSKPPKPFD EKDDPIHNST GSTDSWEGDL NSSGGGGKQP QQTQQQSSGE NLNNSSDRNN
NSNENNQIVD DNSNVFNKGV VVQTVPMTEI GLFPVSLMMA QQRAEHPINV EDIESDVQTC
SIPNSKPLYS SLGCSTNSSN SGSSISAPNI TFQSFGISPV NNNNNNNNNS NNNSNSNSNS
NSNSNNNNNN NNNNNNNNNN NNNNNNNNNS TVNSNNSSLN NSPRYLNSSS SPRSMQHLSS
KITTTTTTTT TTTTTTSDDN NGNTNNNISN NNNIINNSNN NSNSNNNNNN NINNTNHKFK
TMEKYFSSKE NFPIPFPKLK DELGVIIENS SNKGYVGGNK GSEDRRKKIE QKKKQVPAPE
MKATKEKFIE TITDPTTLNS FRSFMENTQS NENLEFFLEV KRFNTIQDQV LLKHTCDDIW
RRFFDDLAVT QLCVESSLKK LINNRRENPT HSMFNEVLDL LLDDIVCDAF RNYISSPFNP
EWKSEFKKKF TNNTYSTTTQ PINNFNNTNN NNNNNCSTPP NNYSSSPIKQ SNINNNNNNA
SSSNIASSSN VNNNNNNSNG SNTSSSHHRE RLDNIKGNRE RVDSNGKERS IDNKDILSLL
ESNLSNHSNS SSNSNGKDKD KDKDKNENTT DNSNNNNNSN NNLNNLIIKN NFNNILQSPQ
IVSKINEIFK DSNNSQLSIS ITLDNDEDPT IFHLDESDME SLIEEVVKDN ISVHTEISYS
DVSIHKWIAS GSSGRVYNGQ YKGKDVAIKV LGPEVCVHFD LNEFKREVAL MSIFKHDNLA
RCLGAGQYDD KYFHLTEYCH NGSLFSYLRD QRNNISFGQR LHFALGIARG MRYLHSMSII
HRDLKSMNIL LTKRLKIKIV DFGTSRVANK YNMTTHVGTQ AWMAPEIFTS RTYTNKVDVY
SYAIILFEIF TRKSAYDENA NINIPNMVMK GERPELPKDM QTSISNIIKK CWQQKPSNRP
SFIKIVAYLE SIIYPSVSNS LGLVASTSFS SSALWSGQIL AQPKN
