PITM1_RAT
ID PITM1_RAT Reviewed; 1242 AA.
AC Q5U2N3;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Membrane-associated phosphatidylinositol transfer protein 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=Nir2, Pitpnm;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287; SER-300; SER-304;
RP SER-342; SER-345; SER-346; SER-373; SER-593; SER-600 AND SER-621, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) between
CC membranes (By similarity). Binds PI, phosphatidylcholine (PC) and
CC phosphatidic acid (PA) with the binding affinity order of PI > PA > PC
CC (By similarity). Regulates RHOA activity, and plays a role in
CC cytoskeleton remodeling (By similarity). Necessary for normal
CC completion of cytokinesis (By similarity). Plays a role in maintaining
CC normal diacylglycerol levels in the Golgi apparatus (By similarity).
CC Necessary for maintaining the normal structure of the endoplasmic
CC reticulum and the Golgi apparatus (By similarity). Required for protein
CC export from the endoplasmic reticulum and the Golgi (By similarity).
CC Binds calcium ions (By similarity). {ECO:0000250|UniProtKB:O00562}.
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 PIK4CA and VAPB. Interacts with PTK2B via its
CC C-terminus. Interacts with RHOA. Has higher affinity for the inactive,
CC GDP-bound form of RHOA. The CDK1-phosphorylated form interacts with
CC PLK1 (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 -!- 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; BC085945; AAH85945.1; -; mRNA.
DR RefSeq; NP_001008370.1; NM_001008369.1.
DR AlphaFoldDB; Q5U2N3; -.
DR SMR; Q5U2N3; -.
DR BioGRID; 262881; 1.
DR STRING; 10116.ENSRNOP00000025084; -.
DR iPTMnet; Q5U2N3; -.
DR PhosphoSitePlus; Q5U2N3; -.
DR PaxDb; Q5U2N3; -.
DR PRIDE; Q5U2N3; -.
DR Ensembl; ENSRNOT00000025084; ENSRNOP00000025084; ENSRNOG00000018553.
DR GeneID; 361694; -.
DR KEGG; rno:361694; -.
DR UCSC; RGD:1306710; rat.
DR CTD; 9600; -.
DR RGD; 1306710; Pitpnm1.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000161522; -.
DR HOGENOM; CLU_007179_0_0_1; -.
DR InParanoid; Q5U2N3; -.
DR OMA; DPLGHKA; -.
DR OrthoDB; 122895at2759; -.
DR PhylomeDB; Q5U2N3; -.
DR TreeFam; TF312967; -.
DR Reactome; R-RNO-1483226; Synthesis of PI.
DR PRO; PR:Q5U2N3; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018553; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q5U2N3; RN.
DR GO; GO:0044297; C:cell body; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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:RGD.
DR GO; GO:0070300; F:phosphatidic acid binding; ISO:RGD.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:RGD.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISO:RGD.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; ISS:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:RGD.
DR GO; GO:0015914; P:phospholipid transport; ISO:RGD.
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..1242
FT /note="Membrane-associated phosphatidylinositol transfer
FT protein 1"
FT /id="PRO_0000232740"
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..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..285
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 581..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..670
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:0000250|UniProtKB:O35954"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35954"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35954"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35954"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:22673903"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00562"
FT MOD_RES 1209
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35954"
FT MOD_RES 1235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00562"
SQ SEQUENCE 1242 AA; 134984 MW; AEC9040877E2979E CRC64;
MLIKEYHILL PMSLDEYQVA QLYMIQKKSR EESSGEGSGV EILANRPYTD GPGGNGQYTH
KVYHVGSHIP GWFRALLPKA ALQVEEESWN AYPYTRTRYT CPFVEKFSIE IETYYLPDGG
QQPNVFNLSG AERRQRILDT IDIVRDAVAP GEYKAEEDPR LYRSVKTGRG PLADDWARTA
AQTGPLMCAY KLCKVEFRYW GMQAKIEQFI HDVGLRRVML RAHRQAWCWQ DEWIELSMAD
IRALEEETAR MLAQRMAKCN TGSEGPEAQT PGKPSTETQP GTRTAGTPDG PEAPPGPDAS
PDASFGKQWS SSSRSSYSSQ HGGGVSPQSL SEWRMQNIAR DSENSSEEEF FDAHEGFSDS
DEVFPKEMTK WNSNDFIDAF ASPTEVEGVP DPAIMATKGI EDEARAPRDS EGLDGTGDLG
VEACSVHALF LILHSGSILD SGPGDTNSKQ ADVQTLSTAF EAVTRVHFPE ALGHVALRLV
PCPPICAAAY ALVSNLSPYS HDGDSLSRSQ DHIPLAALPL LATSSSRYQG AVATVIARTN
QAYAAFLRSS EGTGFCGQVV LIGDGVGGIL GFDALCHSAS AGTGSRGSSR RGSMNNEMLS
PEVGPVRDPL ADGVEVLGRA SPEPSALPAQ RTSSDMANPD PDGSQNSLQV APTVTSGEPR
RASTASCPPA SSEAPDGPTN AARLDFKVSG FFLFGSPLGL VLALRKTVMP ALEVAQMRPA
CEQIYNLFHA ADPCASRLEP LLAPKFQAIA PLAVPRYQKF PLGDGSSLLL ADTLQTHSSL
FLEELEMMVP STPTSASGAF WKGNELGNEP AAQPAAPSTT SEVVKILDRW WGNKRIDYSL
YCPEALTAFP TVTLPHLFHA SYWESADVVA FILRQVIEKE RPQLTECEEP SIYSPAFPRE
KWQRKRTQVK IRNVTSNHRA SDTVVCEGRP QVLNGRFMYG PLDVVTLTGE KVDVYVMTQP
LSGKWIHFGT EVTNSSGRLT FPVPSERALG IGVYPVRMVV RGDHTYAECC LTVVSRGTEA
VVFSIDGSFT ASVSIMGSDP KVRAGAVDVV RHWQDSGYLI VYVTGRPDMQ KHRVVAWLSQ
HNFPHGVVSF CDGLTHDPLR QKAMFLQSLV QEVELNIVAG YGSPKDVAVY AALGLSPSQT
YIVGRAVRKL QAQCQFLSDG YVAHLGQLEA GSHSHAPSGP PRAALAKSSY AVAAPVDFLR
KQSQLLRSRG PSQVDLEGPG TPPTTLARGK TRSISLKLDS EE
