MINP1_DROME
ID MINP1_DROME Reviewed; 467 AA.
AC Q9VV72; O96421; Q8SYN4; Q8T3I2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Multiple inositol polyphosphate phosphatase 1 {ECO:0000312|FlyBase:FBgn0026061};
DE EC=3.1.3.62 {ECO:0000269|PubMed:26628373};
DE AltName: Full=2,3-bisphosphoglycerate 3-phosphatase {ECO:0000250|UniProtKB:Q9UNW1};
DE Short=2,3-BPG phosphatase {ECO:0000250|UniProtKB:Q9UNW1};
DE EC=3.1.3.80 {ECO:0000250|UniProtKB:Q9UNW1};
DE AltName: Full=Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase {ECO:0000250|UniProtKB:Q9UNW1};
DE Short=Ins(1,3,4,5)P(4) 3-phosphatase {ECO:0000250|UniProtKB:Q9UNW1};
DE Flags: Precursor;
GN Name=Mipp1 {ECO:0000312|FlyBase:FBgn0026061};
GN ORFNames=CG4123 {ECO:0000312|FlyBase:FBgn0026061};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAD02436.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
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] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAL49048.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL49048.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL49048.1}, and
RC Ovary {ECO:0000312|EMBL:AAM12275.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP INDUCTION, GLYCOSYLATION, ACTIVE SITE, GPI-ANCHOR AT GLY-441, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF HIS-67 AND 439-ARG--PRO-444.
RX PubMed=26628373; DOI=10.1016/j.celrep.2015.10.071;
RA Cheng Y.L., Andrew D.J.;
RT "Extracellular Mipp1 activity confers migratory advantage to epithelial
RT cells during collective migration.";
RL Cell Rep. 13:2174-2188(2015).
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) (PubMed:26628373). 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 (By
CC similarity). Has a role in embryonic tracheal development where it
CC localizes to the leading edge of actively migrating branches
CC (PubMed:26628373). In these leading cells, enhances formation and/or
CC maintenance of filopodia which may drive branch migration and
CC elongation by cell-cell intercalation (PubMed:26628373). The function
CC in tracheal morphogenesis is dependent on its inositol polyphosphate
CC phosphatase activity (PubMed:26628373). {ECO:0000250|UniProtKB:Q9UNW1,
CC ECO:0000269|PubMed:26628373}.
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:0000250|UniProtKB:Q9UNW1};
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:26628373};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26628373};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:26628373}. Apical cell
CC membrane {ECO:0000269|PubMed:26628373}. Basolateral cell membrane
CC {ECO:0000269|PubMed:26628373}. Cell projection, filopodium
CC {ECO:0000269|PubMed:26628373}. Cell junction
CC {ECO:0000269|PubMed:26628373}. Note=Has a dynamic localization pattern
CC during tracheal development. During early tracheal invagination
CC (embryonic stage 10), localizes mainly to the apical cell membrane.
CC During the primary tracheal branching stage (embryonic stage 11), found
CC mainly at the basolateral cell membrane. At later stages (embryonic
CC stage 13-15), also localizes to cell-cell junctions and filopodia.
CC {ECO:0000269|PubMed:26628373}.
CC -!- DEVELOPMENTAL STAGE: During embryonic stage 10-12, expressed throughout
CC the tracheal primordia. At stages 13-15, expression is lost from the
CC tracheal dorsal trunks (DTs) but is maintained in branches still
CC undergoing active elongation and migration: the dorsal branches (DBs),
CC visceral branches (VBs), lateral trunk branches (LTs) and ganglionic
CC branches (GBs). Notably, expression is enriched at regions of filopodia
CC formation such as the distal tips of the DBs, LTs and GBs.
CC {ECO:0000269|PubMed:26628373}.
CC -!- INDUCTION: Up-regulated by FGF signaling in the developing trachea.
CC {ECO:0000269|PubMed:26628373}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:26628373}.
CC -!- DISRUPTION PHENOTYPE: Tracheal morphology is grossly normal although
CC some defects are observed. Dorsal trunks (DTs) are significantly
CC elongated, and dorsal branches (DBs) frequently fail to fuse with their
CC contralateral partner. Filopodia number in DBs is reduced.
CC {ECO:0000269|PubMed:26628373}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. MINPP1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM12275.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF046913; AAD02436.1; -; mRNA.
DR EMBL; AE014296; AAF49450.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN11754.1; -; Genomic_DNA.
DR EMBL; AE014296; AHN58107.1; -; Genomic_DNA.
DR EMBL; AY071426; AAL49048.1; -; mRNA.
DR EMBL; AY095182; AAM12275.1; ALT_INIT; mRNA.
DR RefSeq; NP_001287082.1; NM_001300153.1.
DR RefSeq; NP_524109.2; NM_079385.4.
DR RefSeq; NP_730177.1; NM_168672.3.
DR AlphaFoldDB; Q9VV72; -.
DR SMR; Q9VV72; -.
DR STRING; 7227.FBpp0075156; -.
DR GlyGen; Q9VV72; 3 sites.
DR PaxDb; Q9VV72; -.
DR PRIDE; Q9VV72; -.
DR DNASU; 39841; -.
DR EnsemblMetazoa; FBtr0075398; FBpp0075156; FBgn0026061.
DR EnsemblMetazoa; FBtr0075399; FBpp0075157; FBgn0026061.
DR EnsemblMetazoa; FBtr0345813; FBpp0311799; FBgn0026061.
DR GeneID; 39841; -.
DR KEGG; dme:Dmel_CG4123; -.
DR UCSC; CG4123-RA; d. melanogaster.
DR CTD; 39841; -.
DR FlyBase; FBgn0026061; Mipp1.
DR VEuPathDB; VectorBase:FBgn0026061; -.
DR eggNOG; KOG1382; Eukaryota.
DR GeneTree; ENSGT00390000018409; -.
DR HOGENOM; CLU_029165_0_0_1; -.
DR InParanoid; Q9VV72; -.
DR OMA; QPQKMWI; -.
DR OrthoDB; 1046588at2759; -.
DR PhylomeDB; Q9VV72; -.
DR Reactome; R-DME-1855231; Synthesis of IPs in the ER lumen.
DR BioGRID-ORCS; 39841; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39841; -.
DR PRO; PR:Q9VV72; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0026061; Expressed in crop (Drosophila) and 52 other tissues.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:FlyBase.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; ISS:FlyBase.
DR GO; GO:0030175; C:filopodium; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR GO; GO:0034417; F:bisphosphoglycerate 3-phosphatase activity; ISS:FlyBase.
DR GO; GO:0052826; F:inositol hexakisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052745; F:inositol phosphate phosphatase activity; IDA:FlyBase.
DR GO; GO:0016311; P:dephosphorylation; ISS:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:FlyBase.
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.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cell projection; Developmental protein;
KW Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..441
FT /note="Multiple inositol polyphosphate phosphatase 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437746"
FT PROPEP 442..467
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437747"
FT ACT_SITE 67
FT /evidence="ECO:0000269|PubMed:26628373"
FT LIPID 441
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000305|PubMed:26628373"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 67
FT /note="H->A: Loss of InsP6 phosphatase activity. Fails to
FT rescue the filopodia formation phenotype of null mutants."
FT /evidence="ECO:0000269|PubMed:26628373"
FT MUTAGEN 439..444
FT /note="Missing: Fails to localize to the cell membrane."
FT /evidence="ECO:0000269|PubMed:26628373"
FT CONFLICT 388
FT /note="C -> L (in Ref. 1; AAD02436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 53571 MW; 80E197609E42E4C6 CRC64;
MRLLILLLLP LVAIAQDDYC FSKDTSRLQT RQFSSKTAYQ IVKGTDIDKQ YLVPGCQPQK
MWIFHRHGTR LPKKSMINKA SRVAELRDLI INNYQVARTK PETDALCQTD LIAIKLWKWN
SSITPDMEEY LTAQGYEDLR GTAKLYQRYY PTVLTANYND TYYQFRHTDT QRTTESFKAF
AEGLFGSQNA AHPVEIPKQD LLLRPYDYCS SFKNVNYKDE GSEYYKFHQS KLYNDTLADI
STRLGFLYTL EEADIKLMYD MCRYEQAWNV DRNSVWCGAF LPEQITVFEY LEDLKYYYGS
GYGFPENAHL NCRLVQDLLT HLSNPVSPHV VAHFGHSTGL LTLLTALGIQ KDDIKLRADN
YDSLTSRRWK SSLIDPFAAN FVAVKYDCPA DLDREKVVFF LNQQAVQLDW CSVGLCKWSD
VLEKYKTIAD ADCGEYYCRT GGAPSLGSGV GGLLATTLAA MLVYLMH
