O15743 (SPNA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein spalten

Including the following 2 domains:

1. Probable guanine nucleotide-binding protein spalten
2. Protein serine/threonine phosphatase spalten
   EC=3.1.3.16

Gene names

Name:	spnA
Synonyms:	spn
ORF Names:	DDB_G0276155

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	975 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in cell-type differentiation and morphogenesis. Dephosphorylates casein; in vitro. May also be involved as modulators or transducers in various transmembrane signaling systems. Ref.1 Ref.4
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Enzyme regulation	Inhibited by 50 mM NaF (sodium fluoride). Ref.1
Subunit structure	G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site.
Subcellular location	Cytoplasm › cytosol. Cell membrane Ref.1.
Developmental stage	Moderately expressed during growth. Increases during development, peaking at around 8 hours of development (mound stage) and then decreases gradually during the later stages. Mainly expressed in the prestalk cell population during the later multicellular stages. Required for prestalk specific gene expression and for prespore cell differentiation. Expressed (at protein level).
Disruption phenotype	Morphological arrest at the mound stage and a defect in cell-type differentiation. Instead of going through morphogenesis, after 16 hours of development, the mounds disaggregate to form smaller aggregates that eventually produce abnormal looking finger-like structures. Ref.1
Sequence similarities	In the N-terminal section; belongs to the G-alpha family. In the C-terminal section; belongs to the PP2C family. Contains 1 PP2C-like domain.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Domain	Coiled coil
Ligand	GTP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Hydrolase Protein phosphatase Transducer
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro GTP catabolic process Inferred from electronic annotation. Source: GOC anatomical structure morphogenesis Inferred from mutant phenotype Ref.1. Source: dictyBase cell differentiation Inferred from mutant phenotype Ref.1. Source: dictyBase protein dephosphorylation Inferred from direct assay Ref.1. Source: dictyBase
Cellular_component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from direct assay Ref.1. Source: dictyBase plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell ruffle Inferred from direct assay Ref.1. Source: dictyBase
Molecular_function	GTP binding Inferred from mutant phenotype Ref.1. Source: dictyBase GTPase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from direct assay Ref.1. Source: dictyBase manganese ion binding Inferred from direct assay Ref.1. Source: dictyBase protein serine/threonine phosphatase activity Inferred from direct assay Ref.1. Source: dictyBase signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 975	975	Protein spalten		PRO_0000367575
Regions
	Domain	719 – 972	254	PP2C-like
	Nucleotide binding	122 – 129	8	GTP By similarity
	Nucleotide binding	261 – 267	7	GTP By similarity
	Nucleotide binding	286 – 290	5	GTP By similarity
	Nucleotide binding	373 – 376	4	GTP By similarity
	Coiled coil	21 – 70	50	Potential
	Compositional bias	31 – 53	23	Poly-Gln
	Compositional bias	97 – 103	7	Poly-Asn
	Compositional bias	502 – 512	11	Poly-Asn
	Compositional bias	561 – 576	16	Poly-Thr
	Compositional bias	580 – 585	6	Poly-Asn
	Compositional bias	592 – 686	95	Lys-rich
Sites
	Metal binding	749	1	Manganese 1 By similarity
	Metal binding	750	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	920	1	Manganese 2 By similarity
	Metal binding	963	1	Manganese 2 By similarity
Experimental info
	Mutagenesis	373	1	N → D: Leads to the formation of very small-sized fruiting bodies. Ref.1
	Mutagenesis	376	1	D → A: Leads to the formation of abnormal looking fruiting bodies. Ref.1
	Mutagenesis	920	1	D → A: Loss of phosphatase activity; when associated with A-924. Ref.1
	Mutagenesis	924	1	D → A: Loss of phosphatase activity; when associated with A-920. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O15743 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: BBB322F5026D2A4F	FASTA	975	109,016
	10 20 30 40 50 60 MKKMLFMNKK EKKEEQSPAH SSLAQQHQLA QQQYQLQQQQ LQLQYQQHQQ QLQLAQQQKQ 70 80 90 100 110 120 NEQNLAQLST STSSNSSVNN TTNTNTNTTN SSSISSNNNN NNNTAVPILK AHDFCGTIMI 130 140 150 160 170 180 LGHTESGKTT LQRQLEFIYG VTDPTDAKHY QRLIYGNTLA TLIRFIENSE RLNITLSPDN 190 200 210 220 230 240 LARVKRIQSQ PVELARNRLP RFPLKLGWDC KCIWEDKVIQ SVYNHSKICS EIRTPGRPKY 250 260 270 280 290 300 YMDRMFKVFD PSYTPTEMDI ISAYDQKDTI QSSAIIHKRF KVDLFGCSGK QSSPKNWVGL 310 320 330 340 350 360 HQNYKPNYIF YVVALKDYFS DHLVATQNTD PTIVEMCNNH IHRNLLLESL NSFETLTKSE 370 380 390 400 410 420 LFDKSLAIYL IFNTSDIFYE NIKQYDLKSC FSEYEGGNDP EKAVSFISNK FTKFLQNKDK 430 440 450 460 470 480 PYKSHIVNLL DKNNVREEFE GIFDSLKIDA EKRGFTTPYN QSNSSPVSSI GSNSSRNSRL 490 500 510 520 530 540 PNTSVSIPGL YSSDNDNTRL KNVNNNNNNN NNTTTYGSST FPSSVISTTG SISNSIASAM 550 560 570 580 590 600 DNDSSYSNES SPTSSMTLLP TTTTTTTTTT TTATTTDSTN NNNNNATVVI GKGKPPKEPK 610 620 630 640 650 660 PVKPPKEPKP PKEPKPPKEP KPPKEPKPIK EPKEKPVKES KPPKEPKPIK EPKESKEPKE 670 680 690 700 710 720 PKEPKPTKPP KEKKTSKVDG AAESKKNGAD SCGNGGVGSK IKLESGFGSL QGRRKNMEDT 730 740 750 760 770 780 HVILNNLMGA VTYNGPPKDI PISYYAVYDG HGGTETSTLL EPTVHNCLVN SQSFRDGDYE 790 800 810 820 830 840 QAFRDAYAEA DDIVIEKCEK SGSTGVSALL VGNKLYTANV GDSEIVLARA QPNANPKGPV 850 860 870 880 890 900 TYEPVLLSYK HLASDDQEKK RVTDLGGMII FNRLFGSLAV SRSFGDKEYK EGEKKFCVSD 910 920 930 940 950 960 PYQTTTDLTA RDHFFILACD GLWDKVEYDE AVQFVQRNIK LGKSATEISE LLAQDSYDRG 970 SGDNITVLVV ILNWN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Spalten, a protein containing Galpha-protein-like and PP2C domains, is essential for cell-type differentiation in Dictyostelium." Aubry L., Firtel R.A. Genes Dev. 12:1525-1538(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, FUNCTION, ENZYME REGULATION, MUTAGENESIS OF ASN-373; ASP-376; ASP-920 AND ASP-924, SUBCELLULAR LOCATION. Strain: AX3.
[2]	"Sequence and analysis of chromosome 2 of Dictyostelium discoideum." Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A. Nature 418:79-85(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[4]	"The novel ankyrin-repeat containing kinase ARCK-1 acts as a suppressor of the Spalten signaling pathway during Dictyostelium development." Aubry L., Lee S., Ravanel K., Firtel R.A. Dev. Biol. 263:308-322(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF019985 mRNA. Translation: AAB70844.1. AAFI02000014 Genomic DNA. Translation: EAL69377.1.
PIR	T08606.
RefSeq	XP_643266.1. XM_638174.1.
3D structure databases
HSSP	HSSP built from PDB template 1GDD based on UniProtKB P10824.
ProteinModelPortal	O15743.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0185064.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0185064; DDB0185064; DDB_G0276155.
GeneID	8620309.
KEGG	ddi:DDB_G0276155.
Organism-specific databases
dictyBase	DDB_G0276155. spnA.
Phylogenomic databases
eggNOG	COG0631.
InParanoid	O15743.
OMA	RFIENSE.
Family and domain databases
Gene3D	1.10.400.10. 1 hit. 3.60.40.10. 1 hit.
InterPro	IPR001019. Gprotein_alpha_su. IPR011025. GproteinA_insert. IPR001932. PP2C-like. IPR000222. PP2C_Mn2_Asp60_BS. IPR015655. Protein_Pase_2C. [Graphical view]
PANTHER	PTHR13832. PTHR13832. 1 hit.
Pfam	PF00503. G-alpha. 1 hit. PF00481. PP2C. 1 hit. [Graphical view]
SMART	SM00275. G_alpha. 1 hit. SM00331. PP2C_SIG. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
SUPFAM	SSF81606. PP2C-related. 1 hit. SSF47895. Transducn_insert. 1 hit.
PROSITE	PS01032. PP2C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SPNA_DICDI

Accession

Primary (citable) accession number: O15743
Secondary accession number(s): Q552E7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)