PITM1_MOUSE
ID PITM1_MOUSE Reviewed; 1243 AA.
AC O35954;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Membrane-associated phosphatidylinositol transfer protein 1;
DE AltName: Full=Drosophila retinal degeneration B homolog 1;
DE Short=RdgB1;
DE AltName: Full=Mpt-1;
DE AltName: Full=Phosphatidylinositol transfer protein, membrane-associated 1;
DE Short=PITPnm 1;
DE AltName: Full=Pyk2 N-terminal domain-interacting receptor 2;
DE Short=NIR-2;
GN Name=Pitpnm1; Synonyms=Dres9, Mpt1, Nir2, Pitpnm;
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], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9245688; DOI=10.1006/bbrc.1997.7009;
RA Aikawa Y., Hara H., Watanabe T.;
RT "Molecular cloning and characterization of mammalian homologues of the
RT Drosophila retinal degeneration B gene.";
RL Biochem. Biophys. Res. Commun. 236:559-564(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=9680295; DOI=10.1046/j.1365-4624.1997.00015.x;
RA Rubboli F., Bulfone A., Bogni S., Marchitiello A., Zollo M., Borsani G.,
RA Ballabio A., Banfi S.;
RT "A mammalian homologue of the Drosophila retinal degeneration B gene:
RT implications for the evolution of phototransduction mechanisms.";
RL Genes Funct. 1:205-213(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PIK4CA.
RX PubMed=10400687; DOI=10.1074/jbc.274.29.20569;
RA Aikawa Y., Kuraoka A., Kondo H., Kawabuchi M., Watanabe T.;
RT "Involvement of PITPnm, a mammalian homologue of Drosophila rdgB, in
RT phosphoinositide synthesis on Golgi membranes.";
RL J. Biol. Chem. 274:20569-20577(1999).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-282; THR-287; SER-300;
RP SER-304; SER-319; SER-326; SER-329; SER-373 AND SER-593, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, and Spleen;
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 [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1210 AND ARG-1217, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) between
CC membranes (By similarity). Binds PI (PubMed:10400687). Also binds
CC phosphatidylcholine (PC) and phosphatidic acid (PA) with the binding
CC affinity order of PI > PA > PC (By similarity). Regulates RHOA
CC activity, and plays a role in cytoskeleton remodeling (By similarity).
CC Necessary for normal completion of cytokinesis (By similarity). Plays a
CC role in maintaining normal diacylglycerol levels in the Golgi apparatus
CC (By similarity). Necessary for maintaining the normal structure of the
CC endoplasmic reticulum and the Golgi apparatus (By similarity). Required
CC for protein export from the endoplasmic reticulum and the Golgi (By
CC similarity). Binds calcium ions (By similarity).
CC {ECO:0000250|UniProtKB:O00562, ECO:0000269|PubMed:10400687}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out);
CC Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880;
CC Evidence={ECO:0000250|UniProtKB:O00562};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000250|UniProtKB:O00562};
CC -!- SUBUNIT: Interacts with PTK2B via its C-terminus. Interacts with RHOA.
CC Has higher affinity for the inactive, GDP-bound form of RHOA. The CDK1-
CC phosphorylated form interacts with PLK1. Interacts with VAPB and PIK4CA
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O00562}. Golgi
CC apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:O00562};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:O00562}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:O00562}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:O00562}. Lipid droplet
CC {ECO:0000250|UniProtKB:O00562}. Cleavage furrow
CC {ECO:0000250|UniProtKB:O00562}. Midbody {ECO:0000250|UniProtKB:O00562}.
CC Note=Peripheral membrane protein associated with Golgi stacks in
CC interphase cells. A minor proportion is associated with the endoplasmic
CC reticulum. Associated with lipid droplets. Dissociates from the Golgi
CC early on in mitosis and localizes to the cleavage furrow and midbody
CC during cytokinesis. {ECO:0000250|UniProtKB:O00562}.
CC -!- TISSUE SPECIFICITY: Detected at high levels in brain, and at lower
CC levels in lung, kidney, spleen and liver (at protein level).
CC Ubiquitous. Highly expressed in embryonic retina and the central
CC nervous system. {ECO:0000269|PubMed:9245688,
CC ECO:0000269|PubMed:9680295}.
CC -!- DEVELOPMENTAL STAGE: Detected at low levels during fetal development up
CC to day 15. Highly expressed at day 17.
CC -!- PTM: Phosphorylated on multiple sites by CDK1 at the onset of mitosis.
CC Phosphorylation facilitates dissociation from the Golgi complex and is
CC required for interaction with PLK1 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on threonine residues upon treatment with oleic
CC acid. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues by PTK2B. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer
CC class IIA subfamily. {ECO:0000305}.
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DR EMBL; AF006467; AAB84393.1; -; mRNA.
DR EMBL; Y08922; CAA70127.1; -; mRNA.
DR EMBL; BC044893; AAH44893.1; -; mRNA.
DR EMBL; BC048150; AAH48150.1; -; mRNA.
DR CCDS; CCDS37883.1; -.
DR PIR; JC5615; JC5615.
DR RefSeq; NP_032877.1; NM_008851.4.
DR AlphaFoldDB; O35954; -.
DR SMR; O35954; -.
DR BioGRID; 202185; 4.
DR IntAct; O35954; 3.
DR MINT; O35954; -.
DR STRING; 10090.ENSMUSP00000097599; -.
DR iPTMnet; O35954; -.
DR PhosphoSitePlus; O35954; -.
DR EPD; O35954; -.
DR jPOST; O35954; -.
DR MaxQB; O35954; -.
DR PaxDb; O35954; -.
DR PeptideAtlas; O35954; -.
DR PRIDE; O35954; -.
DR ProteomicsDB; 288171; -.
DR Antibodypedia; 30438; 231 antibodies from 28 providers.
DR DNASU; 18739; -.
DR Ensembl; ENSMUST00000049658; ENSMUSP00000054309; ENSMUSG00000024851.
DR Ensembl; ENSMUST00000100022; ENSMUSP00000097599; ENSMUSG00000024851.
DR GeneID; 18739; -.
DR KEGG; mmu:18739; -.
DR UCSC; uc008fyn.3; mouse.
DR CTD; 9600; -.
DR MGI; MGI:1197524; Pitpnm1.
DR VEuPathDB; HostDB:ENSMUSG00000024851; -.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000161522; -.
DR HOGENOM; CLU_007179_0_0_1; -.
DR InParanoid; O35954; -.
DR OMA; DPLGHKA; -.
DR OrthoDB; 122895at2759; -.
DR PhylomeDB; O35954; -.
DR TreeFam; TF312967; -.
DR Reactome; R-MMU-1483226; Synthesis of PI.
DR BioGRID-ORCS; 18739; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Pitpnm1; mouse.
DR PRO; PR:O35954; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; O35954; protein.
DR Bgee; ENSMUSG00000024851; Expressed in layer of retina and 89 other tissues.
DR ExpressionAtlas; O35954; baseline and differential.
DR Genevisible; O35954; MM.
DR GO; GO:0044297; C:cell body; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0070300; F:phosphatidic acid binding; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISO:MGI.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISA:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR GO; GO:0015914; P:phospholipid transport; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.530.20; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR004177; DDHD_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR031315; LNS2/PITP.
DR InterPro; IPR001666; PI_transfer.
DR InterPro; IPR023393; START-like_dom_sf.
DR PANTHER; PTHR10658; PTHR10658; 1.
DR Pfam; PF02862; DDHD; 2.
DR Pfam; PF02121; IP_trans; 1.
DR PRINTS; PR00391; PITRANSFER.
DR SMART; SM01127; DDHD; 1.
DR SMART; SM00775; LNS2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR PROSITE; PS51043; DDHD; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Endoplasmic reticulum; Golgi apparatus; Lipid droplet;
KW Membrane; Metal-binding; Methylation; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1243
FT /note="Membrane-associated phosphatidylinositol transfer
FT protein 1"
FT /id="PRO_0000232739"
FT DOMAIN 684..878
FT /note="DDHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378"
FT REGION 259..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00562"
FT MOD_RES 282
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2N3"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2N3"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2N3"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 382
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:O00562"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00562"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00562"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00562"
FT MOD_RES 1210
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1217
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00562"
SQ SEQUENCE 1243 AA; 134940 MW; 98E247536527D83E CRC64;
MLIKEYHILL PMSLDEYQVA QLYMIQKKSR EESSGEGSGV EILANRPYTD GPGGNGQYTH
KVYHVGSHIP GWFRALLPKA ALQVEEESWN AYPYTRTRYT CPFVEKFSIE IETYYLPDGG
QQPNVFNLSG AERRQRIVDT IDIVRDAVAP GEYKAEEDPR LYRSAKTGRG PLADDWARTA
AQTGPLMCAY KLCKVEFRYW GMQAKIEQFI HDVGLRRVML RAHRQAWCWQ DEWIELSMAD
IRALEEETAR MLAQRMAKCN TGSEGPEAQT PGKSSTEARP GTSTAGTPDG PEAPPGPDAS
PDASFGKQWS SSSRSSYSSQ HGGGVSPQSL SEWRMQNIAR DSENSSEEEF FDAHEGFSDS
DEVFPKEMTK WNSNDFIDAF ASPTEVEGVP DPTVMATKGI EDGARAPRDS EGLDGAGDLV
VEACSVHALF LILHSGSILD SGPGDTNSKQ ADVQTLSTAF EAVTRVHFPE ALGHVALRLV
PCPPICAAAY ALVSNLSPYS HDGDSLSRSQ DHIPLAALPL LATSSSRYQG AVATVIARTN
QAYAAFLRSS EGTGFCGQVV LIGDGVGGIL GFDALCHSAS AGPGSRGSSR RGSMNNEMLS
PEVGPVRDPL ADGVEVLGRA SPEPSALPAQ RTFSDMANPD PDGSQNSLQV ASTATSSGEP
RRASTASCPP ASSEAPDGPT NAARLDFKVS GFFLFGSPLG LVLALRKTVM PALEVAQLRP
ACEQIYNLFH AADPCASRLE PLLAPKFQAI APLAVPRYQK FPLGDGSSLL LADTLQTHSS
LFLEELEMMV PSTPTSASGA FWKGSELGNE PASQTAAPST TSEVVKILDR WWGNKRIDYS
LYCPEALTAF PTVTLPHLFH ASYWESADVV AFILRQVIEK ERPQLTECEE PSIYSPAFPR
EKWQRKRTQV KIRNVTSNHR ASDTVVCEGR PQVLNGRFMY GPLDVVTLTG EKVDVYVMTQ
PLSGKWIHFG TEVTNSSGRL TFPVPSERAL GIGVYPVRMV VRGDHTYAEC CLTVVSRGTE
AVVFSIDGSF TASVSIMGSD PKVRAGAVDV VRHWQDSGYL IVYVTGRPDM QKHRVVAWLS
QHNFPHGVVS FCDGLTHDPL RQKAMFLQSL VQEVELNIVA GYGSPKDVAV YAALGLSPSQ
TYIVGRAVRK LQAQCQFLSD GYVAHLGQLE AGSHSHAPSG PPRAALAKSS YAVAAPVDFL
RKQSQLLRSR GPSQVDREGP GTPPTTLARG KTRSISLKLD SEE
