Minpp1
entrez
17330
canonical
uniprot
Q9Z2L6
canonical
ensembl
ENSMUSG00000024896
resolver
ensp
ENSMUSP00000025827
resolver
enst
ENSMUST00000025827
resolver
genesymbol
Minpp1
resolver
genesymbol_syn
Mipp
resolver
uniprot
Q3UA76
resolver
uniprot
Q8VDR0
resolver
uniprot
Q9JJD5
resolver
uniprot_entry
MINP1_MOUSE
resolver
uniprot_sec
Q3UA76
resolver
uniprot_sec
Q8VDR0
resolver
uniprot_sec
Q9JJD5
resolver
amino_acid_sequence
MLRGARSHLPASVAPAAVLAAALLSSFARCSLPGRGDPVASVLSPYFGTKTRYEDANPWLLVDPVAPRRDPELLAGTCTPVQLVALIRHGTRYPTTKQIRKLKQLQGLLQTRESRDGGSQVAAALAEWPLWYGDWMDGQLVEKGRQDMRQLALRLAALFPDLFSRENYDRLRLITSSKHRCVDSSAAFLQGLWQHYHPGLPPPDVSDMECGPPRINDKLMRFFDHCEKFLTDVERNETALYHVEAFKTGPEMQKVLKKVAATLQVPMNSLNADLIQVAFFTCSFDLAIKGVHSPWCDVFDVDDARVLEYLNDLKQYWKRSYGYTINSRSSCNLFQDIFLHLDKAVEQKQRSQPVSSPVILQFGHAETLLPLLSLMGYFKDKEPLTAYNFEEQVNRKFRSGHIVPYASNLIFVLYHCDNAQSPEEQFQIQLLLNEKVLPLAHSQRPVGLYEELKTHYRDILQSCQTSKECSPPKANITSDEL
uniprot
proteins
ec_number
3.1.3.62
uniprot
proteins
ec_number
3.1.3.80
uniprot
proteins
function
FUNCTION: Multiple inositol polyphosphate phosphatase that hydrolyzes 1D-myo-inositol 1,3,4,5,6-pentakisphosphate (InsP5[2OH]) and 1D-myo-inositol hexakisphosphate (InsP6) to a range of less phosphorylated inositol phosphates. This regulates the availability of these various small molecule second messengers and metal chelators which control many aspects of cell physiology (PubMed:10087200, PubMed:10938126). Has a weak in vitro activity towards 1D-myo-inositol 1,4,5-trisphosphate which is unlikely to be physiologically relevant. By regulating intracellular inositol polyphosphates pools, which act as metal chelators, it may control the availability of intracellular calcium and iron, which are important for proper neuronal development and homeostasis (PubMed:33257696). May have a dual substrate specificity, and function as a 2,3-bisphosphoglycerate 3-phosphatase hydrolyzing 2,3-bisphosphoglycerate to 2-phosphoglycerate. 2,3-bisphosphoglycerate (BPG) is formed as part of the Rapoport-Luebering glycolytic bypass and is a regulator of systemic oxygen homeostasis as the major allosteric effector of hemoglobin (By similarity). {ECO:0000250|UniProtKB:Q9UNW1, ECO:0000269|PubMed:10087200, ECO:0000269|PubMed:10938126, ECO:0000269|PubMed:33257696}.
uniprot
proteins
mass_dalton
54537
uniprot
proteins
mutagenesis
MUTAGEN 89; /note="H->A: Loss of phosphatase inositol phosphate phosphatase activity."; /evidence="ECO:0000269|PubMed:10087200, ECO:0000269|PubMed:10938126
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9UNW1}.
uniprot
proteins
protein_family
Histidine acid phosphatase family
uniprot
proteins
protein_family
MINPP1 subfamily
uniprot
proteins
pubmed
10087200
uniprot
proteins
pubmed
10938126
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
33257696
uniprot
proteins
sequence_length
481
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:10938126}. Secreted {ECO:0000250|UniProtKB:Q9UNW1}. Cell membrane {ECO:0000269|PubMed:10938126}. Note=Also associated with the plasma membrane in erythrocytes. {ECO:0000269|PubMed:10938126}.
uniprot
proteins