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O15743 (SPNA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length975 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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

Cytoplasmcytosol. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 975975Protein spalten
PRO_0000367575

Regions

Domain719 – 972254PP2C-like
Nucleotide binding122 – 1298GTP By similarity
Nucleotide binding261 – 2677GTP By similarity
Nucleotide binding286 – 2905GTP By similarity
Nucleotide binding373 – 3764GTP By similarity
Coiled coil21 – 7050 Potential
Compositional bias31 – 5323Poly-Gln
Compositional bias97 – 1037Poly-Asn
Compositional bias502 – 51211Poly-Asn
Compositional bias561 – 57616Poly-Thr
Compositional bias580 – 5856Poly-Asn
Compositional bias592 – 68695Lys-rich

Sites

Metal binding7491Manganese 1 By similarity
Metal binding7501Manganese 1; via carbonyl oxygen By similarity
Metal binding9201Manganese 2 By similarity
Metal binding9631Manganese 2 By similarity

Experimental info

Mutagenesis3731N → D: Leads to the formation of very small-sized fruiting bodies. Ref.1
Mutagenesis3761D → A: Leads to the formation of abnormal looking fruiting bodies. Ref.1
Mutagenesis9201D → A: Loss of phosphatase activity; when associated with A-924. Ref.1
Mutagenesis9241D → A: Loss of phosphatase activity; when associated with A-920. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O15743 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: BBB322F5026D2A4F

FASTA975109,016
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
PIRT08606.

3D structure databases

ProteinModelPortalO15743.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0185064.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0185064; DDB0185064; DDB_G0276155.
KEGGddi:DDB_G0276155.

Organism-specific databases

dictyBaseDDB_G0276155. spnA.

Phylogenomic databases

eggNOGCOG0631.
InParanoidO15743.
KOK17500.
OMAEMDIISA.

Family and domain databases

Gene3D1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
3.60.40.10. 1 hit.
InterProIPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
IPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00503. G-alpha. 1 hit.
PF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00275. G_alpha. 1 hit.
SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF81606. SSF81606. 1 hit.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPNA_DICDI
AccessionPrimary (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: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase