MINP1_DICDI
ID MINP1_DICDI Reviewed; 635 AA.
AC Q54ND5;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Multiple inositol polyphosphate phosphatase 1;
DE Short=Ddmipp1;
DE EC=3.1.3.62;
DE AltName: Full=2,3-bisphosphoglycerate 3-phosphatase;
DE Short=2,3-BPG phosphatase;
DE EC=3.1.3.80;
DE AltName: Full=Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase;
DE Short=Ins(1,3,4,5)P(4) 3-phosphatase;
DE Flags: Precursor;
GN Name=mipp1; ORFNames=DDB_G0285339;
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=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 [2]
RP FUNCTION AS 2,3-BISPHOSPHOGLYCERATE 3-PHOSPHATASE, AND CATALYTIC ACTIVITY.
RX PubMed=18413611; DOI=10.1073/pnas.0710980105;
RA Cho J., King J.S., Qian X., Harwood A.J., Shears S.B.;
RT "Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the
RT regulatory capacity of the Rapoport-Luebering glycolytic shunt.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5998-6003(2008).
CC -!- FUNCTION: Acts as a phosphoinositide 5- and phosphoinositide 6-
CC phosphatase and regulates cellular levels of inositol pentakisphosphate
CC (InsP5) and inositol hexakisphosphate (InsP6) (By similarity). Also
CC acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the
CC dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce
CC phospho-D-glycerate without formation of 3-phosphoglycerate.
CC {ECO:0000250, ECO:0000269|PubMed:18413611}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2,3-bisphosphoglycerate + H2O = (2R)-2-phosphoglycerate +
CC phosphate; Xref=Rhea:RHEA:27381, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58248, ChEBI:CHEBI:58289; EC=3.1.3.80;
CC Evidence={ECO:0000269|PubMed:18413611};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=myo-inositol hexakisphosphate + H2O = myo-inositol
CC pentakisphosphate (mixed isomers) + phosphate.; EC=3.1.3.62;
CC Evidence={ECO:0000269|PubMed:18413611};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. MINPP1
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000079; EAL64744.1; -; Genomic_DNA.
DR RefSeq; XP_638245.1; XM_633153.1.
DR AlphaFoldDB; Q54ND5; -.
DR SMR; Q54ND5; -.
DR STRING; 44689.DDB0266617; -.
DR PaxDb; Q54ND5; -.
DR EnsemblProtists; EAL64744; EAL64744; DDB_G0285339.
DR GeneID; 8625053; -.
DR KEGG; ddi:DDB_G0285339; -.
DR dictyBase; DDB_G0285339; mipp1.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_029165_1_1_1; -.
DR InParanoid; Q54ND5; -.
DR PhylomeDB; Q54ND5; -.
DR Reactome; R-DDI-1855231; Synthesis of IPs in the ER lumen.
DR PRO; PR:Q54ND5; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IC:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR GO; GO:0034417; F:bisphosphoglycerate 3-phosphatase activity; ISS:dictyBase.
DR GO; GO:0034416; F:bisphosphoglycerate phosphatase activity; IDA:dictyBase.
DR GO; GO:0052826; F:inositol hexakisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052745; F:inositol phosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0051717; F:inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity; IDA:dictyBase.
DR GO; GO:0006007; P:glucose catabolic process; IDA:dictyBase.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IDA:dictyBase.
DR GO; GO:0010226; P:response to lithium ion; IMP:dictyBase.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..635
FT /note="Multiple inositol polyphosphate phosphatase 1"
FT /id="PRO_0000417526"
FT TOPO_DOM 24..565
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 66..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 116
FT /evidence="ECO:0000255"
SQ SEQUENCE 635 AA; 70382 MW; 4EA5B6769999ADE6 CRC64;
MMVKIKNIII LFCIFGLLSN VSSLSSSSSS SQSSDNNGNL SPIQDYDLEF LSKHLTTKTP
YWILTKNGDS NSQGDGSSGN SNSNSNSNSN SNSNSDSSNE PPEQCKLISI DFIARHGSRM
PVLNSIEKLK EMTTSILEYK EQVNQGFNWI FNYSVPYPSD IAGNLILQGQ YEHYNISKRL
LKKYPLFFEP MKYKPQSYSI TSTAISRTGI SASAFSYGLL QGTGSLGVDG FQPVFIETAS
LDQDILLRFF ATCNQYVDQL KNGTLINKDE QTKWNQMVFP NISNEISERL GLSDIWLPTS
NVISDIFEAC AYEISINNIS DHWCSLLSKQ NILDWEYSQD LSNYWLKSYG HEINYQIATP
LLNDILSGFD IYINNNNNGS SSSSSSSSSN NGDNSGSNGS SGSGSSTSTS SNDNGSTNNN
DNKVEPTSIL RFGHAETIIP FISLLGLYKD EQKLFANSST EQIENRKFRT SVVSPYASNI
AMFLFDCGSA ADGFKILVQH NELPVLVPGC DEIYCDYQQF KSIFKQGIDN FKWNSYCNIN
DDDSGSSGGD SGNGNGNDSH SKKSSYFLAI FIPITFLVGG TIGGIFTYFS YEKIMQVKNR
KKLTQYGNDE FISSPKSKSF SFKPTKFDSR SPLIQ
