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SPNA_DICDI
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   03-AUG-2022, entry version 145.
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 (Slime mold).
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.DDB0185064; -.
DR   PaxDb; O15743; -.
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   GO; GO:0006470; P:protein dephosphorylation; IDA:dictyBase.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 1.10.400.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.60.40.10; -; 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_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   PANTHER; PTHR13832; PTHR13832; 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; SSF47895; SSF47895; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF81606; SSF81606; 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
 
 
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