PITC1_MOUSE
ID PITC1_MOUSE Reviewed; 332 AA.
AC Q8K4R4; A2A650; A2A651; Q3TBB3; Q3U5F5; Q8K4R5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cytoplasmic phosphatidylinositol transfer protein 1;
DE AltName: Full=Mammalian rdgB homolog beta;
DE Short=M-rdgB beta;
DE Short=MrdgBbeta;
DE Short=mM-rdgBbeta;
DE AltName: Full=Retinal degeneration B homolog beta;
DE Short=RdgBbeta;
GN Name=Pitpnc1;
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] (ISOFORMS 1 AND 2), FUNCTION (ISOFORM 2),
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY (ISOFORMS 1
RP AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=12562526; DOI=10.1046/j.1471-4159.2003.01591.x;
RA Takano N., Owada Y., Suzuki R., Sakagami H., Shimosegawa T., Kondo H.;
RT "Cloning and characterization of a novel variant (mM-rdgBbeta1) of mouse M-
RT rdgBs, mammalian homologs of Drosophila retinal degeneration B gene
RT proteins, and its mRNA localization in mouse brain in comparison with other
RT M-rdgBs.";
RL J. Neurochem. 84:829-839(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Olfactory epithelium;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-122; SER-270;
RP SER-274 AND THR-278, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Heart, Lung, 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).
CC -!- FUNCTION: [Isoform 1]: Catalyzes the transfer of phosphatidylinositol
CC (PI) and phosphatidic acid (PA) between membranes (By similarity).
CC Binds PA derived from the phospholipase D signaling pathway and among
CC the cellular PA species, preferably binds to the C16:0/16:1 and
CC C16:1/18:1 PA species (By similarity). {ECO:0000250|UniProtKB:Q9UKF7}.
CC -!- FUNCTION: [Isoform 2]: Specifically binds to phosphatidylinositol but
CC not to other phospholipids and may play a role in the phosphoinositide-
CC mediated signaling in the neural development.
CC {ECO:0000269|PubMed:12562526}.
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:Q9UKF7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000250|UniProtKB:Q9UKF7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate(in) = a 1,2-diacyl-sn-
CC glycero-3-phosphate(out); Xref=Rhea:RHEA:36435, ChEBI:CHEBI:58608;
CC Evidence={ECO:0000250|UniProtKB:Q9UKF7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36436;
CC Evidence={ECO:0000250|UniProtKB:Q9UKF7};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:12562526}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:12562526}. Nucleus {ECO:0000269|PubMed:12562526}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=mM-rdgBbeta;
CC IsoId=Q8K4R4-1; Sequence=Displayed;
CC Name=2; Synonyms=mM-rdgBbeta1;
CC IsoId=Q8K4R4-2; Sequence=VSP_025549, VSP_025551;
CC Name=3;
CC IsoId=Q8K4R4-3; Sequence=VSP_025548, VSP_025550;
CC Name=4;
CC IsoId=Q8K4R4-4; Sequence=VSP_025546, VSP_025547;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Widely expressed in brain, with
CC expression in the gray matters of pre- and postnatal brains.
CC {ECO:0000269|PubMed:12562526}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Weakly expressed in brain and is
CC rather confined to the embryonic stage. {ECO:0000269|PubMed:12562526}.
CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer
CC class IIB subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM17314.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM17315.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM20627.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM25441.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM25442.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB077281; BAC02913.1; -; mRNA.
DR EMBL; AB077282; BAC02914.1; -; mRNA.
DR EMBL; AK153625; BAE32124.1; -; mRNA.
DR EMBL; AK171340; BAE42401.1; -; mRNA.
DR EMBL; AL596116; CAM20633.1; -; Genomic_DNA.
DR EMBL; AL645687; CAM20633.1; JOINED; Genomic_DNA.
DR EMBL; AL645905; CAM20633.1; JOINED; Genomic_DNA.
DR EMBL; AL596116; CAM20627.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL645687; CAM20627.1; JOINED; Genomic_DNA.
DR EMBL; AL645905; CAM20627.1; JOINED; Genomic_DNA.
DR EMBL; AL596116; CAM20628.1; -; Genomic_DNA.
DR EMBL; AL645687; CAM20628.1; JOINED; Genomic_DNA.
DR EMBL; AL645905; CAM20628.1; JOINED; Genomic_DNA.
DR EMBL; AL645687; CAM25441.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL596116; CAM25441.1; JOINED; Genomic_DNA.
DR EMBL; AL645905; CAM25441.1; JOINED; Genomic_DNA.
DR EMBL; AL645687; CAM25442.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL596116; CAM25442.1; JOINED; Genomic_DNA.
DR EMBL; AL645905; CAM25442.1; JOINED; Genomic_DNA.
DR EMBL; AL645687; CAM25443.1; -; Genomic_DNA.
DR EMBL; AL596116; CAM25443.1; JOINED; Genomic_DNA.
DR EMBL; AL645905; CAM25443.1; JOINED; Genomic_DNA.
DR EMBL; AL645905; CAM17314.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL596116; CAM17314.1; JOINED; Genomic_DNA.
DR EMBL; AL645687; CAM17314.1; JOINED; Genomic_DNA.
DR EMBL; AL645905; CAM17315.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL596116; CAM17315.1; JOINED; Genomic_DNA.
DR EMBL; AL645687; CAM17315.1; JOINED; Genomic_DNA.
DR EMBL; AL645905; CAM17317.1; -; Genomic_DNA.
DR EMBL; AL596116; CAM17317.1; JOINED; Genomic_DNA.
DR EMBL; AL645687; CAM17317.1; JOINED; Genomic_DNA.
DR EMBL; BC108351; AAI08352.1; -; mRNA.
DR CCDS; CCDS25567.1; -. [Q8K4R4-2]
DR RefSeq; NP_665822.1; NM_145823.2. [Q8K4R4-2]
DR RefSeq; XP_006534325.1; XM_006534262.3.
DR AlphaFoldDB; Q8K4R4; -.
DR SMR; Q8K4R4; -.
DR STRING; 10090.ENSMUSP00000099353; -.
DR iPTMnet; Q8K4R4; -.
DR PhosphoSitePlus; Q8K4R4; -.
DR SwissPalm; Q8K4R4; -.
DR EPD; Q8K4R4; -.
DR MaxQB; Q8K4R4; -.
DR PaxDb; Q8K4R4; -.
DR PeptideAtlas; Q8K4R4; -.
DR PRIDE; Q8K4R4; -.
DR ProteomicsDB; 289427; -. [Q8K4R4-1]
DR ProteomicsDB; 289428; -. [Q8K4R4-2]
DR ProteomicsDB; 289429; -. [Q8K4R4-3]
DR ProteomicsDB; 289430; -. [Q8K4R4-4]
DR Antibodypedia; 9639; 77 antibodies from 17 providers.
DR DNASU; 71795; -.
DR Ensembl; ENSMUST00000103064; ENSMUSP00000099353; ENSMUSG00000040430. [Q8K4R4-2]
DR GeneID; 71795; -.
DR KEGG; mmu:71795; -.
DR UCSC; uc007mak.1; mouse. [Q8K4R4-1]
DR UCSC; uc007mal.1; mouse. [Q8K4R4-2]
DR UCSC; uc007man.1; mouse. [Q8K4R4-3]
DR UCSC; uc007mao.1; mouse. [Q8K4R4-4]
DR CTD; 26207; -.
DR MGI; MGI:1919045; Pitpnc1.
DR VEuPathDB; HostDB:ENSMUSG00000040430; -.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000160720; -.
DR HOGENOM; CLU_046509_3_0_1; -.
DR InParanoid; Q8K4R4; -.
DR OMA; VENRPCE; -.
DR OrthoDB; 951268at2759; -.
DR TreeFam; TF313279; -.
DR BioGRID-ORCS; 71795; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Pitpnc1; mouse.
DR PRO; PR:Q8K4R4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K4R4; protein.
DR Bgee; ENSMUSG00000040430; Expressed in lateral geniculate body and 270 other tissues.
DR ExpressionAtlas; Q8K4R4; baseline and differential.
DR Genevisible; Q8K4R4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070300; F:phosphatidic acid binding; ISO:MGI.
DR GO; GO:1990050; F:phosphatidic acid transfer activity; ISS:UniProtKB.
DR GO; GO:1901611; F:phosphatidylglycerol binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; ISS:UniProtKB.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:MGI.
DR GO; GO:0015914; P:phospholipid transport; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR001666; PI_transfer.
DR InterPro; IPR023393; START-like_dom_sf.
DR PANTHER; PTHR10658; PTHR10658; 1.
DR Pfam; PF02121; IP_trans; 1.
DR PRINTS; PR00391; PITRANSFER.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Lipid transport; Lipid-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..332
FT /note="Cytoplasmic phosphatidylinositol transfer protein 1"
FT /id="PRO_0000287531"
FT REGION 272..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 278
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 208..209
FT /note="VR -> GC (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025546"
FT VAR_SEQ 210..332
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025547"
FT VAR_SEQ 228..234
FT /note="DMTMDEV -> GKSDGPK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025548"
FT VAR_SEQ 233..268
FT /note="EVREFERATQEATNKKIGVFPPAISISSIALLPSSV -> DVREYEKNMHEQ
FT TNIKVCNQHSSTVDDIESHAQTST (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12562526,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025549"
FT VAR_SEQ 235..332
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025550"
FT VAR_SEQ 269..332
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12562526,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025551"
SQ SEQUENCE 332 AA; 38384 MW; A20BF9EEAB80E178 CRC64;
MLLKEYRICM PLTVDEYKIG QLYMISKHSH EQSDRGEGVE VVQNEPFEDP HHGNGQFTEK
RVYLNSKLPS WARAVVPKIF YVTEKAWNYY PYTITEYTCS FLPKFSIHIE TKYEDNKGSN
DSIFDSEAKD LEREVCFIDI ACDEIPERYY KESEDPKHFK SEKTGRGQLR EGWRDNHQPI
MCSYKLVTVK FEVWGLQTRV EQFVHKVVRD ILLIGHRQAF AWVDEWYDMT MDEVREFERA
TQEATNKKIG VFPPAISISS IALLPSSVRS APSSAPSTPL STDAPEFLSI PKDRPRKKSA
PETLTLPDPE KKATLNLPGV YTSEKPCRPK SE
