PITC1_HUMAN
ID PITC1_HUMAN Reviewed; 332 AA.
AC Q9UKF7; A8K473; J3QR20; Q96I07;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cytoplasmic phosphatidylinositol transfer protein 1;
DE AltName: Full=Mammalian rdgB homolog beta;
DE Short=M-rdgB beta;
DE Short=MrdgBbeta;
DE AltName: Full=Retinal degeneration B homolog beta;
DE Short=RdgBbeta;
GN Name=PITPNC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10531358; DOI=10.1074/jbc.274.44.31553;
RA Fullwood Y., dos Santos M., Hsuan J.J.;
RT "Cloning and characterization of a novel human phosphatidylinositol
RT transfer protein, rdgBbeta.";
RL J. Biol. Chem. 274:31553-31558(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye, and Skin;
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=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP FUNCTION (ISOFORMS 1 AND 2), AND CATALYTIC ACTIVITY (ISOFORMS 1 AND 2).
RX PubMed=22822086; DOI=10.1074/jbc.m112.375840;
RA Garner K., Hunt A.N., Koster G., Somerharju P., Groves E., Li M., Raghu P.,
RA Holic R., Cockcroft S.;
RT "Phosphatidylinositol transfer protein, cytoplasmic 1 (PITPNC1) binds and
RT transfers phosphatidic acid.";
RL J. Biol. Chem. 287:32263-32276(2012).
CC -!- FUNCTION: [Isoform 1]: Catalyzes the transfer of phosphatidylinositol
CC (PI) and phosphatidic acid (PA) between membranes (PubMed:10531358,
CC PubMed:22822086). Binds PA derived from the phospholipase D signaling
CC pathway and among the cellular PA species, preferably binds to the
CC C16:0/16:1 and C16:1/18:1 PA species (PubMed:22822086).
CC {ECO:0000269|PubMed:10531358, ECO:0000269|PubMed:22822086}.
CC -!- FUNCTION: [Isoform 2]: Catalyzes the transfer of phosphatidylinositol
CC between membranes. {ECO:0000269|PubMed:22822086}.
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:0000269|PubMed:10531358, ECO:0000269|PubMed:22822086};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000305|PubMed:10531358};
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:0000269|PubMed:22822086};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36436;
CC Evidence={ECO:0000305|PubMed:22822086};
CC -!- INTERACTION:
CC Q9UKF7; Q6RW13: AGTRAP; NbExp=6; IntAct=EBI-749241, EBI-741181;
CC Q9UKF7; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-749241, EBI-2548702;
CC Q9UKF7-1; Q9H0U4: RAB1B; NbExp=4; IntAct=EBI-11687286, EBI-1045214;
CC Q9UKF7-2; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-14223623, EBI-11522760;
CC Q9UKF7-2; Q68DC2: ANKS6; NbExp=3; IntAct=EBI-14223623, EBI-7054139;
CC Q9UKF7-2; Q9UGQ2: CACFD1; NbExp=3; IntAct=EBI-14223623, EBI-8652492;
CC Q9UKF7-2; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-14223623, EBI-11522780;
CC Q9UKF7-2; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-14223623, EBI-12831978;
CC Q9UKF7-2; Q2KHT4-3: GSG1; NbExp=3; IntAct=EBI-14223623, EBI-12951679;
CC Q9UKF7-2; Q9BUP3-3: HTATIP2; NbExp=3; IntAct=EBI-14223623, EBI-12937691;
CC Q9UKF7-2; Q9BW62: KATNAL1; NbExp=3; IntAct=EBI-14223623, EBI-743591;
CC Q9UKF7-2; Q969L2: MAL2; NbExp=3; IntAct=EBI-14223623, EBI-944295;
CC Q9UKF7-2; Q00765: REEP5; NbExp=3; IntAct=EBI-14223623, EBI-1549827;
CC Q9UKF7-2; Q8TAC9: SCAMP5; NbExp=3; IntAct=EBI-14223623, EBI-2695784;
CC Q9UKF7-2; O60906: SMPD2; NbExp=3; IntAct=EBI-14223623, EBI-12828299;
CC Q9UKF7-2; P08247: SYP; NbExp=3; IntAct=EBI-14223623, EBI-9071725;
CC Q9UKF7-2; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-14223623, EBI-1044859;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10531358}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=sp1 {ECO:0000303|PubMed:22822086};
CC IsoId=Q9UKF7-1; Sequence=Displayed;
CC Name=2; Synonyms=sp2 {ECO:0000303|PubMed:22822086};
CC IsoId=Q9UKF7-2; Sequence=VSP_025545;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10531358}.
CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer
CC class IIB subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF171102; AAF06148.1; -; mRNA.
DR EMBL; AK290838; BAF83527.1; -; mRNA.
DR EMBL; AC079331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007905; AAH07905.1; -; mRNA.
DR EMBL; BC067095; AAH67095.1; -; mRNA.
DR CCDS; CCDS58587.1; -. [Q9UKF7-2]
DR CCDS; CCDS58588.1; -. [Q9UKF7-1]
DR RefSeq; NP_036549.2; NM_012417.3. [Q9UKF7-1]
DR RefSeq; NP_858057.1; NM_181671.2.
DR AlphaFoldDB; Q9UKF7; -.
DR SMR; Q9UKF7; -.
DR BioGRID; 117607; 17.
DR IntAct; Q9UKF7; 22.
DR STRING; 9606.ENSP00000464006; -.
DR SwissLipids; SLP:000000413; -.
DR SwissLipids; SLP:000000992; -. [Q9UKF7-1]
DR SwissLipids; SLP:000000993; -. [Q9UKF7-2]
DR iPTMnet; Q9UKF7; -.
DR PhosphoSitePlus; Q9UKF7; -.
DR BioMuta; PITPNC1; -.
DR DMDM; 147720965; -.
DR EPD; Q9UKF7; -.
DR jPOST; Q9UKF7; -.
DR MassIVE; Q9UKF7; -.
DR PaxDb; Q9UKF7; -.
DR PeptideAtlas; Q9UKF7; -.
DR PRIDE; Q9UKF7; -.
DR ProteomicsDB; 84783; -. [Q9UKF7-1]
DR ProteomicsDB; 84784; -. [Q9UKF7-2]
DR Antibodypedia; 9639; 77 antibodies from 17 providers.
DR DNASU; 26207; -.
DR Ensembl; ENST00000581322.6; ENSP00000464006.1; ENSG00000154217.16. [Q9UKF7-1]
DR GeneID; 26207; -.
DR KEGG; hsa:26207; -.
DR MANE-Select; ENST00000581322.6; ENSP00000464006.1; NM_012417.4; NP_036549.2.
DR UCSC; uc002jgb.5; human. [Q9UKF7-1]
DR CTD; 26207; -.
DR DisGeNET; 26207; -.
DR GeneCards; PITPNC1; -.
DR HGNC; HGNC:21045; PITPNC1.
DR HPA; ENSG00000154217; Tissue enhanced (brain).
DR MIM; 605134; gene.
DR neXtProt; NX_Q9UKF7; -.
DR OpenTargets; ENSG00000154217; -.
DR PharmGKB; PA128394642; -.
DR VEuPathDB; HostDB:ENSG00000154217; -.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000160720; -.
DR HOGENOM; CLU_046509_2_0_1; -.
DR InParanoid; Q9UKF7; -.
DR OrthoDB; 951268at2759; -.
DR PathwayCommons; Q9UKF7; -.
DR SignaLink; Q9UKF7; -.
DR BioGRID-ORCS; 26207; 14 hits in 1067 CRISPR screens.
DR ChiTaRS; PITPNC1; human.
DR GenomeRNAi; 26207; -.
DR Pharos; Q9UKF7; Tbio.
DR PRO; PR:Q9UKF7; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UKF7; protein.
DR Bgee; ENSG00000154217; Expressed in endothelial cell and 188 other tissues.
DR ExpressionAtlas; Q9UKF7; baseline and differential.
DR Genevisible; Q9UKF7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:BHF-UCL.
DR GO; GO:1990050; F:phosphatidic acid transfer activity; IDA:UniProtKB.
DR GO; GO:1901611; F:phosphatidylglycerol binding; IDA:BHF-UCL.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:BHF-UCL.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:BHF-UCL.
DR GO; GO:0015914; P:phospholipid transport; IDA:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; IMP: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;
KW Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..332
FT /note="Cytoplasmic phosphatidylinositol transfer protein 1"
FT /id="PRO_0000287530"
FT REGION 267..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..284
FT /note="Polar residues"
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:0000250|UniProtKB:Q8K4R4"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4R4"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4R4"
FT MOD_RES 278
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4R4"
FT VAR_SEQ 237..332
FT /note="FERATQEATNKKIGIFPPAISISSIPLLPSSVRSAPSSAPSTPLSTDAPEFL
FT SVPKDRPRKKSAPETLTLPDPEKKATLNLPGMHSSDKPCRPKSE -> YEKNMHEQTNI
FT KVCNQHSSPVDDIESHAQTST (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025545"
FT CONFLICT 18
FT /note="K -> R (in Ref. 2; BAF83527)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="N -> S (in Ref. 1; AAF06148)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="F -> S (in Ref. 1; AAF06148)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="E -> D (in Ref. 2; BAF83527 and 4; AAH07905/
FT AAH67095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 38388 MW; D42C8F00FFA54C6A CRC64;
MLLKEYRICM PLTVDEYKIG QLYMISKHSH EQSDRGEGVE VVQNEPFEDP HHGNGQFTEK
RVYLNSKLPS WARAVVPKIF YVTEKAWNYY PYTITEYTCS FLPKFSIHIE TKYEDNKGSN
DTIFDNEAKD VEREVCFIDI ACDEIPERYY KESEDPKHFK SEKTGRGQLR EGWRDSHQPI
MCSYKLVTVK FEVWGLQTRV EQFVHKVVRD ILLIGHRQAF AWVDEWYDMT MDEVREFERA
TQEATNKKIG IFPPAISISS IPLLPSSVRS APSSAPSTPL STDAPEFLSV PKDRPRKKSA
PETLTLPDPE KKATLNLPGM HSSDKPCRPK SE
