位置:首页 > 蛋白库 > SSPA_DICDI
SSPA_DICDI
ID   SSPA_DICDI              Reviewed;         406 AA.
AC   Q55A00; Q86IM6; Q86IM7;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Probable sphingosine-1-phosphate phosphatase;
DE            Short=SPPase;
DE            EC=3.1.3.-;
GN   Name=sppA; ORFNames=DDB_G0272260;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
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   [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).
CC   -!- FUNCTION: Has enzymatic activity against both sphingosine 1 phosphate
CC       (S1P) and dihydro-S1P. Regulates intracellular and extracellular S1P
CC       levels (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000008; EAL71282.1; -; Genomic_DNA.
DR   RefSeq; XP_645184.1; XM_640092.1.
DR   AlphaFoldDB; Q55A00; -.
DR   STRING; 44689.DDB0216187; -.
DR   PaxDb; Q55A00; -.
DR   EnsemblProtists; EAL71282; EAL71282; DDB_G0272260.
DR   GeneID; 8618356; -.
DR   KEGG; ddi:DDB_G0272260; -.
DR   dictyBase; DDB_G0272260; sppA.
DR   eggNOG; KOG2822; Eukaryota.
DR   HOGENOM; CLU_678676_0_0_1; -.
DR   InParanoid; Q55A00; -.
DR   OMA; NINEYEC; -.
DR   PhylomeDB; Q55A00; -.
DR   Reactome; R-DDI-1660661; Sphingolipid de novo biosynthesis.
DR   PRO; PR:Q55A00; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:dictyBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; ISS:dictyBase.
DR   GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..406
FT                   /note="Probable sphingosine-1-phosphate phosphatase"
FT                   /id="PRO_0000365604"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          107..115
FT                   /note="Phosphatase sequence motif I"
FT                   /evidence="ECO:0000305"
FT   REGION          133..136
FT                   /note="Phosphatase sequence motif II"
FT                   /evidence="ECO:0000305"
FT   REGION          183..194
FT                   /note="Phosphatase sequence motif III"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        136
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A924"
FT   ACT_SITE        190
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P0A924"
FT   SITE            194
FT                   /note="Stabilizes the active site histidine for
FT                   nucleophilic attack"
FT                   /evidence="ECO:0000250|UniProtKB:P0A924"
SQ   SEQUENCE   406 AA;  45887 MW;  E2CEF8E700CA0049 CRC64;
     MEKIKKQNNI GSYSSDKDGE YKKFRFSKTS IRGFLLKEYE REVPIIVKIQ SYRNKFLDFY
     FKMASILGEE VFFILALPIS TWCVATQLGV ELCVVLALTI GGGNILKNTF TLPRPPPNIV
     WTNTAHQKDH GLPSTHTASA FGLTFYFLIY TYFLFPTIGE SFNISLLSMF FIVLFWSTSV
     MFSRLYNGHH TPMDVIAGLI VAITSILATT YQLRYFIEGM VLSETFLFGP MLYIAILSAI
     LFFHPQANTG PTPAYPETGL VCGASLGSLI SLWLHAQHPC PLMNQELLLL EANYDSIVST
     IHSIPLLLHG SRILIGLVLV GIAKVFSKKF FFFAYDLVIR ANTNNEQSQP ITTVSFDPNK
     KIIVTPTIEA FSKLFVYTCV SFTIVSMPYL FYYLNIQTSA DVTRYY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024