ID SPNA_DICDI Reviewed; 975 AA.
AC O15743; Q552E7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=Protein spalten;
DE Includes:
DE RecName: Full=Probable guanine nucleotide-binding protein spalten;
DE Includes:
DE RecName: Full=Protein serine/threonine phosphatase spalten;
DE EC=3.1.3.16;
GN Name=spnA; Synonyms=spn; ORFNames=DDB_G0276155;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, FUNCTION, ACTIVITY
RP REGULATION, MUTAGENESIS OF ASN-373; ASP-376; ASP-920 AND ASP-924, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=AX3;
RX PubMed=9585512; DOI=10.1101/gad.12.10.1525;
RA Aubry L., Firtel R.A.;
RT "Spalten, a protein containing Galpha-protein-like and PP2C domains, is
RT essential for cell-type differentiation in Dictyostelium.";
RL Genes Dev. 12:1525-1538(1998).
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 FUNCTION.
RX PubMed=14597204; DOI=10.1016/j.ydbio.2003.07.012;
RA Aubry L., Lee S., Ravanel K., Firtel R.A.;
RT "The novel ankyrin-repeat containing kinase ARCK-1 acts as a suppressor of
RT the Spalten signaling pathway during Dictyostelium development.";
RL Dev. Biol. 263:308-322(2003).
CC -!- FUNCTION: Involved in cell-type differentiation and morphogenesis.
CC Dephosphorylates casein; in vitro. May also be involved as modulators
CC or transducers in various transmembrane signaling systems.
CC {ECO:0000269|PubMed:14597204, ECO:0000269|PubMed:9585512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by 50 mM NaF (sodium fluoride).
CC {ECO:0000269|PubMed:9585512}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9585512}.
CC Cell membrane {ECO:0000269|PubMed:9585512}.
CC -!- DEVELOPMENTAL STAGE: Moderately expressed during growth. Increases
CC during development, peaking at around 8 hours of development (mound
CC stage) and then decreases gradually during the later stages. Mainly
CC expressed in the prestalk cell population during the later
CC multicellular stages. Required for prestalk specific gene expression
CC and for prespore cell differentiation. Expressed (at protein level).
CC -!- DISRUPTION PHENOTYPE: Morphological arrest at the mound stage and a
CC defect in cell-type differentiation. Instead of going through
CC morphogenesis, after 16 hours of development, the mounds disaggregate
CC to form smaller aggregates that eventually produce abnormal looking
CC finger-like structures. {ECO:0000269|PubMed:9585512}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the G-alpha family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PP2C family.
CC {ECO:0000305}.
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DR EMBL; AF019985; AAB70844.1; -; mRNA.
DR EMBL; AAFI02000014; EAL69377.1; -; Genomic_DNA.
DR PIR; T08606; T08606.
DR RefSeq; XP_643266.1; XM_638174.1.
DR AlphaFoldDB; O15743; -.
DR SMR; O15743; -.
DR STRING; 44689.O15743; -.
DR PaxDb; 44689-DDB0185064; -.
DR EnsemblProtists; EAL69377; EAL69377; DDB_G0276155.
DR GeneID; 8620309; -.
DR KEGG; ddi:DDB_G0276155; -.
DR dictyBase; DDB_G0276155; spnA.
DR eggNOG; KOG0082; Eukaryota.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_304722_0_0_1; -.
DR InParanoid; O15743; -.
DR OMA; ISYYAVY; -.
DR PRO; PR:O15743; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IDA:dictyBase.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IMP:dictyBase.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IDA:dictyBase.
DR GO; GO:0030145; F:manganese ion binding; IDA:dictyBase.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:dictyBase.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IMP:dictyBase.
DR GO; GO:0030154; P:cell differentiation; IMP:dictyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR13832:SF876; PROTEIN PHOSPHATASE 1G; 1.
DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR Pfam; PF00503; G-alpha; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00275; G_alpha; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasm; GTP-binding; Hydrolase; Magnesium;
KW Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW Protein phosphatase; Reference proteome; Transducer.
FT CHAIN 1..975
FT /note="Protein spalten"
FT /id="PRO_0000367575"
FT DOMAIN 114..458
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT DOMAIN 704..972
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..130
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 259..267
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 282..291
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 369..376
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 427..432
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 455..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..70
FT /evidence="ECO:0000255"
FT COMPBIAS 541..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 261..267
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 286..290
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 373..376
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 749
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 750
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 920
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 963
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MUTAGEN 373
FT /note="N->D: Leads to the formation of very small-sized
FT fruiting bodies."
FT /evidence="ECO:0000269|PubMed:9585512"
FT MUTAGEN 376
FT /note="D->A: Leads to the formation of abnormal looking
FT fruiting bodies."
FT /evidence="ECO:0000269|PubMed:9585512"
FT MUTAGEN 920
FT /note="D->A: Loss of phosphatase activity; when associated
FT with A-924."
FT /evidence="ECO:0000269|PubMed:9585512"
FT MUTAGEN 924
FT /note="D->A: Loss of phosphatase activity; when associated
FT with A-920."
FT /evidence="ECO:0000269|PubMed:9585512"
SQ SEQUENCE 975 AA; 109016 MW; BBB322F5026D2A4F CRC64;
MKKMLFMNKK EKKEEQSPAH SSLAQQHQLA QQQYQLQQQQ LQLQYQQHQQ QLQLAQQQKQ
NEQNLAQLST STSSNSSVNN TTNTNTNTTN SSSISSNNNN NNNTAVPILK AHDFCGTIMI
LGHTESGKTT LQRQLEFIYG VTDPTDAKHY QRLIYGNTLA TLIRFIENSE RLNITLSPDN
LARVKRIQSQ PVELARNRLP RFPLKLGWDC KCIWEDKVIQ SVYNHSKICS EIRTPGRPKY
YMDRMFKVFD PSYTPTEMDI ISAYDQKDTI QSSAIIHKRF KVDLFGCSGK QSSPKNWVGL
HQNYKPNYIF YVVALKDYFS DHLVATQNTD PTIVEMCNNH IHRNLLLESL NSFETLTKSE
LFDKSLAIYL IFNTSDIFYE NIKQYDLKSC FSEYEGGNDP EKAVSFISNK FTKFLQNKDK
PYKSHIVNLL DKNNVREEFE GIFDSLKIDA EKRGFTTPYN QSNSSPVSSI GSNSSRNSRL
PNTSVSIPGL YSSDNDNTRL KNVNNNNNNN NNTTTYGSST FPSSVISTTG SISNSIASAM
DNDSSYSNES SPTSSMTLLP TTTTTTTTTT TTATTTDSTN NNNNNATVVI GKGKPPKEPK
PVKPPKEPKP PKEPKPPKEP KPPKEPKPIK EPKEKPVKES KPPKEPKPIK EPKESKEPKE
PKEPKPTKPP KEKKTSKVDG AAESKKNGAD SCGNGGVGSK IKLESGFGSL QGRRKNMEDT
HVILNNLMGA VTYNGPPKDI PISYYAVYDG HGGTETSTLL EPTVHNCLVN SQSFRDGDYE
QAFRDAYAEA DDIVIEKCEK SGSTGVSALL VGNKLYTANV GDSEIVLARA QPNANPKGPV
TYEPVLLSYK HLASDDQEKK RVTDLGGMII FNRLFGSLAV SRSFGDKEYK EGEKKFCVSD
PYQTTTDLTA RDHFFILACD GLWDKVEYDE AVQFVQRNIK LGKSATEISE LLAQDSYDRG
SGDNITVLVV ILNWN
//
