MINP1_CHICK
ID MINP1_CHICK Reviewed; 448 AA.
AC F1NPQ2; Q92170;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 3.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Multiple inositol polyphosphate phosphatase 1 {ECO:0000250|UniProtKB:Q9UNW1};
DE EC=3.1.3.62 {ECO:0000269|PubMed:16759730};
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=Band 17 {ECO:0000303|PubMed:8660956};
DE AltName: Full=Histidine phosphatase of the endoplasmic reticulum 1 {ECO:0000303|PubMed:9472008};
DE Short=HiPER1 {ECO:0000303|PubMed:9472008};
DE Flags: Precursor;
GN Name=MINPP1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|Proteomes:UP000000539};
RN [1] {ECO:0000312|EMBL:AAB97100.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8660956; DOI=10.1006/excr.1996.0219;
RA Reynolds S.D., Johnston C., Leboy P.S., O'Keefe R.J., Puzas J.E.,
RA Rosier R.N., Reynolds P.R.;
RT "Identification and characterization of a unique chondrocyte gene involved
RT in transition to hypertrophy.";
RL Exp. Cell Res. 226:197-207(1996).
RN [2] {ECO:0000312|Proteomes:UP000000539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl {ECO:0000312|Proteomes:UP000000539};
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP GLYCOSYLATION.
RX PubMed=9472008; DOI=10.1242/jcs.111.6.803;
RA Romano P.R., Wang J., O'Keefe R.J., Puzas J.E., Rosier R.N., Reynolds P.R.;
RT "HiPER1, a phosphatase of the endoplasmic reticulum with a role in
RT chondrocyte maturation.";
RL J. Cell Sci. 111:803-813(1998).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION,
RP AND MUTAGENESIS OF THR-27 AND GLN-78.
RX PubMed=16759730; DOI=10.1016/j.jbiotec.2006.04.028;
RA Cho J., Choi K., Darden T., Reynolds P.R., Petitte J.N., Shears S.B.;
RT "Avian multiple inositol polyphosphate phosphatase is an active phytase
RT that can be engineered to help ameliorate the planet's 'phosphate
RT crisis'.";
RL J. Biotechnol. 126:248-259(2006).
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:9472008). 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). May play a role in bone development (endochondral
CC ossification) (By similarity). May play a role in the transition of
CC chondrocytes from proliferation to hypertrophy (PubMed:8660956,
CC PubMed:9472008). {ECO:0000250|UniProtKB:Q9UNW1,
CC ECO:0000269|PubMed:16759730, ECO:0000303|PubMed:8660956,
CC ECO:0000303|PubMed:9472008}.
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:16759730};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=140 uM for inositol hexakisphosphate
CC {ECO:0000269|PubMed:16759730};
CC Vmax=715 nmol/min/mg enzyme with inositol hexakisphosphate as
CC substrate {ECO:0000269|PubMed:16759730};
CC pH dependence:
CC Optimum pH is 4.5-7.5. {ECO:0000269|PubMed:16759730};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:9472008}.
CC -!- TISSUE SPECIFICITY: Present in growth plate chondrocytes but not
CC detectable in articular chondrocytes (at protein level)
CC (PubMed:9472008). Spatially restricted to chondrocytes in the lower
CC portion of the proliferative zone and the upper portion of the
CC hypertrophic zone in the growth plate of long bones (at protein level)
CC (PubMed:9472008). Weakly expressed in kidney, liver, lung, skin and
CC spleen, and not detected in brain, heart and muscle (PubMed:8660956).
CC {ECO:0000269|PubMed:8660956, ECO:0000269|PubMed:9472008}.
CC -!- INDUCTION: Repressed by parathyroid hormone-related protein
CC PTHLH/PTHRP. {ECO:0000269|PubMed:9472008}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16759730,
CC ECO:0000269|PubMed:9472008}.
CC -!- MISCELLANEOUS: Monogastric animals cannot hydrolyze dietary inositol
CC hexakisphosphate (InsP6) which makes up the bulk of organic phosphates
CC in soybean, grains and other plant seeds which are the primary source
CC of animal feed. The high activity of the chicken protein toward InsP6
CC offers a genetic strategy for improving InsP6 digestion in poultry and
CC reducing the pollution that results from high phosphate content in
CC manure. {ECO:0000303|PubMed:16759730}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. MINPP1
CC subfamily. {ECO:0000305}.
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DR EMBL; U59421; AAB97100.1; -; mRNA.
DR EMBL; AADN03005023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_989975.1; NM_204644.1.
DR AlphaFoldDB; F1NPQ2; -.
DR SMR; F1NPQ2; -.
DR STRING; 9031.ENSGALP00000005852; -.
DR PaxDb; F1NPQ2; -.
DR GeneID; 395356; -.
DR KEGG; gga:395356; -.
DR CTD; 9562; -.
DR VEuPathDB; HostDB:geneid_395356; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_029165_3_1_1; -.
DR OrthoDB; 1046588at2759; -.
DR SABIO-RK; F1NPQ2; -.
DR PRO; PR:F1NPQ2; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR GO; GO:0034417; F:bisphosphoglycerate 3-phosphatase activity; IEA:UniProtKB-EC.
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 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 Endoplasmic reticulum; Glycoprotein; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..448
FT /note="Multiple inositol polyphosphate phosphatase 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000437140"
FT MOTIF 445..448
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 69
FT /evidence="ECO:0000250|UniProtKB:Q9Z2L6"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 27
FT /note="T->G: Loss of 96% of activity towards InsP6."
FT /evidence="ECO:0000269|PubMed:16759730"
FT MUTAGEN 78
FT /note="Q->A: Two-fold greater substrate affinity and
FT doubling of catalytic activity."
FT /evidence="ECO:0000269|PubMed:16759730"
FT CONFLICT 4
FT /note="R -> C (in Ref. 1; AAB97100)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="S -> A (in Ref. 1; AAB97100)"
FT /evidence="ECO:0000305"
FT CONFLICT 65..67
FT /note="AVL -> RVV (in Ref. 1; AAB97100)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="D -> DG (in Ref. 1; AAB97100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 50200 MW; D62BA17068ECD5BA CRC64;
MAPRRAACLL PLLVAVASAG LGGYFGTKSR YEEVNPHLAE DPLSLGPHAA ASRLPAACAP
LQLRAVLRHG TRYPTAGQIR RLAELHGRLR RAAAPSCPAA AALAAWPMWY EESLDRLAPR
GRRDMEHLAR RLAARFPALF AARRRLALAS SSKHRCLQSG AAFRRGLGPS LSLGADETEI
EVNDALMRFF DHCDKFVAFV EDNDTAMYQV NAFKEGPEMR KVLEKVASAL CLPASELNAD
LVQVAFLTCS YELAIKNVTS PWCSLFSEED AKVLEYLNDL KQYWKRGYGY DINSRSSCIL
FQDIFQQLDK AVDESRSSKP ISSPLIVQVG HAETLQPLLA LMGYFKDAEP LQANNYIRQA
HRKFRSGRIV PYAANLVFVL YHCEQKTSKE EYQVQMLLNE KPMLFHHSNE TISTYADLKS
YYKDILQNCH FEEVCELPKV NGTVADEL
