MINP1_MOUSE
ID MINP1_MOUSE Reviewed; 481 AA.
AC Q9Z2L6; Q3UA76; Q8VDR0; Q9JJD5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Multiple inositol polyphosphate phosphatase 1;
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=Minpp1; Synonyms=Mipp; ORFNames=MNCb-1572;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ACTIVE SITE, AND
RP MUTAGENESIS OF HIS-89.
RC STRAIN=129;
RX PubMed=10087200; DOI=10.1006/geno.1998.5736;
RA Chi H., Tiller G.E., Dasouki M.J., Romano P.R., Wang J., O'keefe R.J.,
RA Puzas J.E., Rosier R.N., Reynolds P.R.;
RT "Multiple inositol polyphosphate phosphatase: evolution as a distinct group
RT within the histidine phosphatase family and chromosomal localization of the
RT human and mouse genes to chromosomes 10q23 and 19.";
RL Genomics 56:324-336(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=10938126; DOI=10.1128/mcb.20.17.6496-6507.2000;
RA Chi H., Yang X., Kingsley P.D., O'Keefe R.J., Puzas J.E., Rosier R.N.,
RA Shears S.B., Reynolds P.R.;
RT "Targeted deletion of Minpp1 provides new insight into the activity of
RT multiple inositol polyphosphate phosphatase in vivo.";
RL Mol. Cell. Biol. 20:6496-6507(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=33257696; DOI=10.1038/s41467-020-19919-y;
RA Ucuncu E., Rajamani K., Wilson M.S.C., Medina-Cano D., Altin N., David P.,
RA Barcia G., Lefort N., Banal C., Vasilache-Dangles M.T., Pitelet G.,
RA Lorino E., Rabasse N., Bieth E., Zaki M.S., Topcu M., Sonmez F.M.,
RA Musaev D., Stanley V., Bole-Feysot C., Nitschke P., Munnich A.,
RA Bahi-Buisson N., Fossoud C., Giuliano F., Colleaux L., Burglen L.,
RA Gleeson J.G., Boddaert N., Saiardi A., Cantagrel V.;
RT "MINPP1 prevents intracellular accumulation of the chelator inositol
RT hexakisphosphate and is mutated in Pontocerebellar Hypoplasia.";
RL Nat. Commun. 11:6087-6087(2020).
CC -!- FUNCTION: Acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating
CC the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce
CC phospho-D-glycerate without formation of 3-phosphoglycerate (By
CC similarity). Acts as a phosphoinositide 5- and phosphoinositide 6-
CC phosphatase and regulates cellular levels of inositol pentakisphosphate
CC (InsP5) and inositol hexakisphosphate (InsP6). May play a role in bone
CC development (endochondral ossification). May play a role in the
CC transition of chondrocytes from proliferation to hypertrophy (By
CC similarity). Through the regulation of intracellular inositol
CC polyphosphates, may control intracellular cation homeostasis, including
CC that of calcium and iron, hence affecting free cation availability
CC required for neural cell signaling (PubMed:33257696).
CC {ECO:0000250|UniProtKB:F1NPQ2, ECO:0000250|UniProtKB:Q9UNW1,
CC ECO:0000269|PubMed:10938126, ECO:0000269|PubMed:33257696}.
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:10087200};
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:10087200};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:O35217}. Cell membrane
CC {ECO:0000305|PubMed:10938126}. Note=Also attached to the plasma
CC membrane in erythrocytes. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in kidney,
CC intestine, thymus and liver.
CC -!- DEVELOPMENTAL STAGE: Expressed in different stages of embryogenesis,
CC from 7.5 dpc through 14.5 dpc. The highest levels of expression is
CC found in the visceral endoderm at 7.5 dpc and 8.5 dpc and in the fetal
CC liver at 12.5 dpc and 14.5 dpc. {ECO:0000269|PubMed:10938126}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are born at Mendelian ratio and are
CC fertile. Although brain histology does not identify major differences
CC in cerebellar or cerebral cortex architecture, a mild, but significant
CC 10% decrease in the brain weight was identified associated with a
CC reduced cortical thickness in homozygous mutant mice at postnatal day
CC 21 (PubMed:33257696). At 14.5 dpc, neural progenitors show a decrease
CC of about one third in intracellular free Ca(2+) levels compared to
CC wild-type progenitors (PubMed:33257696). {ECO:0000269|PubMed:33257696}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. MINPP1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95058.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF046908; AAD02434.1; -; mRNA.
DR EMBL; AB041574; BAA95058.1; ALT_FRAME; mRNA.
DR EMBL; AK151486; BAE30439.1; -; mRNA.
DR EMBL; BC021437; AAH21437.1; -; mRNA.
DR CCDS; CCDS29751.1; -.
DR RefSeq; NP_034929.1; NM_010799.2.
DR AlphaFoldDB; Q9Z2L6; -.
DR SMR; Q9Z2L6; -.
DR STRING; 10090.ENSMUSP00000025827; -.
DR GlyConnect; 2518; 6 N-Linked glycans (1 site).
DR GlyGen; Q9Z2L6; 2 sites, 6 N-linked glycans (1 site).
DR iPTMnet; Q9Z2L6; -.
DR PhosphoSitePlus; Q9Z2L6; -.
DR CPTAC; non-CPTAC-3474; -.
DR EPD; Q9Z2L6; -.
DR MaxQB; Q9Z2L6; -.
DR PaxDb; Q9Z2L6; -.
DR PeptideAtlas; Q9Z2L6; -.
DR PRIDE; Q9Z2L6; -.
DR ProteomicsDB; 252564; -.
DR Antibodypedia; 16040; 320 antibodies from 31 providers.
DR Ensembl; ENSMUST00000025827; ENSMUSP00000025827; ENSMUSG00000024896.
DR GeneID; 17330; -.
DR KEGG; mmu:17330; -.
DR UCSC; uc008hfk.2; mouse.
DR CTD; 9562; -.
DR MGI; MGI:1336159; Minpp1.
DR VEuPathDB; HostDB:ENSMUSG00000024896; -.
DR eggNOG; KOG1382; Eukaryota.
DR GeneTree; ENSGT00390000018409; -.
DR HOGENOM; CLU_029165_3_1_1; -.
DR InParanoid; Q9Z2L6; -.
DR OMA; ETQITGR; -.
DR OrthoDB; 1046588at2759; -.
DR PhylomeDB; Q9Z2L6; -.
DR TreeFam; TF324072; -.
DR BRENDA; 3.1.3.62; 3474.
DR Reactome; R-MMU-1855231; Synthesis of IPs in the ER lumen.
DR BioGRID-ORCS; 17330; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Minpp1; mouse.
DR PRO; PR:Q9Z2L6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9Z2L6; protein.
DR Bgee; ENSMUSG00000024896; Expressed in fetal liver hematopoietic progenitor cell and 267 other tissues.
DR Genevisible; Q9Z2L6; MM.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR GO; GO:0034417; F:bisphosphoglycerate 3-phosphatase activity; ISO:MGI.
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:0030351; F:inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity; ISO:MGI.
DR GO; GO:0030352; F:inositol-1,4,5,6-tetrakisphosphate 6-phosphatase activity; ISO:MGI.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR016274; Histidine_acid_Pase_euk.
DR Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..481
FT /note="Multiple inositol polyphosphate phosphatase 1"
FT /id="PRO_0000019583"
FT MOTIF 478..481
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 89
FT /evidence="ECO:0000269|PubMed:10087200"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 89
FT /note="H->A: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10087200"
FT CONFLICT 211
FT /note="G -> D (in Ref. 4; AAH21437)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="K -> Q (in Ref. 4; AAH21437)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="M -> V (in Ref. 4; AAH21437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 54537 MW; 7CE78356B11F4606 CRC64;
MLRGARSHLP ASVAPAAVLA AALLSSFARC SLPGRGDPVA SVLSPYFGTK TRYEDANPWL
LVDPVAPRRD PELLAGTCTP VQLVALIRHG TRYPTTKQIR KLKQLQGLLQ TRESRDGGSQ
VAAALAEWPL WYGDWMDGQL VEKGRQDMRQ LALRLAALFP DLFSRENYDR LRLITSSKHR
CVDSSAAFLQ GLWQHYHPGL PPPDVSDMEC GPPRINDKLM RFFDHCEKFL TDVERNETAL
YHVEAFKTGP EMQKVLKKVA ATLQVPMNSL NADLIQVAFF TCSFDLAIKG VHSPWCDVFD
VDDARVLEYL NDLKQYWKRS YGYTINSRSS CNLFQDIFLH LDKAVEQKQR SQPVSSPVIL
QFGHAETLLP LLSLMGYFKD KEPLTAYNFE EQVNRKFRSG HIVPYASNLI FVLYHCDNAQ
SPEEQFQIQL LLNEKVLPLA HSQRPVGLYE ELKTHYRDIL QSCQTSKECS PPKANITSDE
L
