Pitpnm1
entrez
18739
canonical
uniprot
O35954
canonical
ensembl
ENSMUSG00000024851
resolver
ensp
ENSMUSP00000054309
resolver
ensp
ENSMUSP00000097599
resolver
enst
ENSMUST00000049658
resolver
enst
ENSMUST00000100022
resolver
genesymbol
Pitpnm1
resolver
genesymbol_syn
Dres9
resolver
genesymbol_syn
Mpt1
resolver
genesymbol_syn
Nir2
resolver
genesymbol_syn
Pitpnm
resolver
uniprot_entry
PITM1_MOUSE
resolver
amino_acid_sequence
MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGNGQYTHKVYHVGSHIPGWFRALLPKAALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRIVDTIDIVRDAVAPGEYKAEEDPRLYRSAKTGRGPLADDWARTAAQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWIELSMADIRALEEETARMLAQRMAKCNTGSEGPEAQTPGKSSTEARPGTSTAGTPDGPEAPPGPDASPDASFGKQWSSSSRSSYSSQHGGGVSPQSLSEWRMQNIARDSENSSEEEFFDAHEGFSDSDEVFPKEMTKWNSNDFIDAFASPTEVEGVPDPTVMATKGIEDGARAPRDSEGLDGAGDLVVEACSVHALFLILHSGSILDSGPGDTNSKQADVQTLSTAFEAVTRVHFPEALGHVALRLVPCPPICAAAYALVSNLSPYSHDGDSLSRSQDHIPLAALPLLATSSSRYQGAVATVIARTNQAYAAFLRSSEGTGFCGQVVLIGDGVGGILGFDALCHSASAGPGSRGSSRRGSMNNEMLSPEVGPVRDPLADGVEVLGRASPEPSALPAQRTFSDMANPDPDGSQNSLQVASTATSSGEPRRASTASCPPASSEAPDGPTNAARLDFKVSGFFLFGSPLGLVLALRKTVMPALEVAQLRPACEQIYNLFHAADPCASRLEPLLAPKFQAIAPLAVPRYQKFPLGDGSSLLLADTLQTHSSLFLEELEMMVPSTPTSASGAFWKGSELGNEPASQTAAPSTTSEVVKILDRWWGNKRIDYSLYCPEALTAFPTVTLPHLFHASYWESADVVAFILRQVIEKERPQLTECEEPSIYSPAFPREKWQRKRTQVKIRNVTSNHRASDTVVCEGRPQVLNGRFMYGPLDVVTLTGEKVDVYVMTQPLSGKWIHFGTEVTNSSGRLTFPVPSERALGIGVYPVRMVVRGDHTYAECCLTVVSRGTEAVVFSIDGSFTASVSIMGSDPKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQKHRVVAWLSQHNFPHGVVSFCDGLTHDPLRQKAMFLQSLVQEVELNIVAGYGSPKDVAVYAALGLSPSQTYIVGRAVRKLQAQCQFLSDGYVAHLGQLEAGSHSHAPSGPPRAALAKSSYAVAAPVDFLRKQSQLLRSRGPSQVDREGPGTPPTTLARGKTRSISLKLDSEE
uniprot
proteins
function
FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) between membranes (By similarity). Binds PI (PubMed:10400687). Also binds phosphatidylcholine (PC) and phosphatidic acid (PA) with the binding affinity order of PI > PA > PC (By similarity). Regulates RHOA activity, and plays a role in cytoskeleton remodeling (By similarity). Necessary for normal completion of cytokinesis (By similarity). Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus (By similarity). Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus (By similarity). Required for protein export from the endoplasmic reticulum and the Golgi (By similarity). Binds calcium ions (By similarity). {ECO:0000250|UniProtKB:O00562, ECO:0000269|PubMed:10400687}.; FUNCTION: Membrane-associated phosphatidylinositol (PI) transfer protein that shuttles PI between intracellular membranes and thereby maintains plasma-membrane phosphoinositide signaling competence. Transfers phosphatidylinositol from the endoplasmic reticulum to the plasma membrane and mediates counter-transport of phosphatidic acid (PA) from the plasma membrane to the endoplasmic reticulum at endoplasmic reticulum-plasma membrane contact sites, this PI/PA exchange is required for sustained PLC-coupled receptor signaling and for replenishment of plasma membrane phosphoinositide following receptor-induced hydrolysis (PubMed:41129229). Regulates RHOA activity, and plays a role in cytoskeleton remodeling. Necessary for normal completion of cytokinesis (By similarity). Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus. Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus. Required for protein export from the endoplasmic reticulum and the Golgi (PubMed:10400687). {ECO:0000250|UniProtKB:O00562, ECO:0000269|PubMed:10400687, ECO:0000269|PubMed:41129229}.
uniprot
proteins
mass_dalton
134940
uniprot
proteins
mutagenesis
MUTAGEN 350; /note="F->S: Loss of interaction with VAPB."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 353; /note="A->S: Decreases interaction with VAPB."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 355; /note="E->A: Decreases interaction with VAPB."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 943..945; /note="LDV->DDD: Strongly decreases association with plasma membrane."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 1025; /note="S->A: Decreases phosphatic acid recognition."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 1026..1029; /note="IDGS->PDGP: Decreases association with phosphatic acid and membrane binding."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 1065; /note="T->A: Decreases association with phosphatic acid; when associated with A-1103 and A-1126."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 1103; /note="K->A: Decreases association with phosphatic acid; when associated with A-1065 and A-1126."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 1126; /note="K->A: Decreases association with phosphatic acid; when associated with A-1065 and A-1103."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 1149..1150; /note="RK->DD: Strongly decreases association with plasma membrane."; /evidence="ECO:0000269|PubMed:41129229
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on multiple sites by CDK1 at the onset of mitosis. Phosphorylation facilitates dissociation from the Golgi complex and is required for interaction with PLK1. {ECO:0000250|UniProtKB:O00562}.; PTM: Phosphorylated on threonine residues upon treatment with oleic acid. {ECO:0000250|UniProtKB:O00562}.; PTM: Phosphorylated on tyrosine residues by PTK2B. {ECO:0000250|UniProtKB:O00562}.
uniprot
proteins
protein_family
PI transfer class IIA subfamily
uniprot
proteins
protein_family
PtdIns transfer protein family
uniprot
proteins
pubmed
10400687
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
41129229
uniprot
proteins
pubmed
9245688
uniprot
proteins
pubmed
9680295
uniprot
proteins
sequence_length
1243
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00562}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00562}; Cytoplasmic side {ECO:0000250|UniProtKB:O00562}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:O00562}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00562}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00562}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00562}; Cytoplasmic side {ECO:0000250|UniProtKB:O00562}. Lipid droplet {ECO:0000250|UniProtKB:O00562}. Cleavage furrow {ECO:0000250|UniProtKB:O00562}. Midbody {ECO:0000250|UniProtKB:O00562}. Note=Upon PIP2 hydrolysis, translocates to endoplasmic reticulum-plasma membrane contact sites. Peripheral membrane protein associated with Golgi stacks in interphase cells. Associated with lipid droplets. Dissociates from the Golgi early on in mitosis and localizes to the cleavage furrow and midbody during cytokinesis. {ECO:0000250|UniProtKB:O00562}.
uniprot
proteins