PITM2_MOUSE
ID PITM2_MOUSE Reviewed; 1335 AA.
AC Q6ZPQ6; Q9R1P5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Membrane-associated phosphatidylinositol transfer protein 2;
DE AltName: Full=Drosophila retinal degeneration B homolog 2;
DE Short=RdgB2;
DE AltName: Full=Phosphatidylinositol transfer protein, membrane-associated 2;
DE Short=PITPnm 2;
DE AltName: Full=Pyk2 N-terminal domain-interacting receptor 3;
DE Short=NIR-3;
GN Name=Pitpnm2; Synonyms=Kiaa1457, Nir3;
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] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=10460238; DOI=10.1523/jneurosci.19-17-07317.1999;
RA Lu C., Vihtelic T.S., Hyde D.R., Li T.;
RT "A neuronal-specific mammalian homolog of the Drosophila retinal
RT degeneration B gene with expression restricted to the retina and dentate
RT gyrus.";
RL J. Neurosci. 19:7317-7325(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP INTERACTION WITH CPNE4.
RX PubMed=12522145; DOI=10.1074/jbc.m212632200;
RA Tomsig J.L., Snyder S.L., Creutz C.E.;
RT "Identification of targets for calcium signaling through the copine family
RT of proteins. Characterization of a coiled-coil copine-binding motif.";
RL J. Biol. Chem. 278:10048-10054(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-338; SER-365;
RP SER-586; SER-686; SER-687; SER-688 AND SER-1263, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
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-814, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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 and
CC phosphatidylcholine between membranes (in vitro). Binds calcium ions
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CPNE4 (via VWFA domain) (PubMed:12522145).
CC Interacts with PTK2B via its C-terminus (By similarity).
CC {ECO:0000250|UniProtKB:Q9BZ72, ECO:0000269|PubMed:12522145}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:10460238}. Note=May associate with the
CC cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZPQ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZPQ6-2; Sequence=VSP_017964;
CC -!- TISSUE SPECIFICITY: Detected in retina and in the dentate gyrus of the
CC cerebellum. {ECO:0000269|PubMed:10460238}.
CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer
CC class IIA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98174.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF058693; AAD51375.1; -; mRNA.
DR EMBL; AK129364; BAC98174.1; ALT_INIT; mRNA.
DR CCDS; CCDS19674.1; -. [Q6ZPQ6-2]
DR CCDS; CCDS71669.1; -. [Q6ZPQ6-1]
DR RefSeq; NP_001276401.1; NM_001289472.1. [Q6ZPQ6-1]
DR RefSeq; NP_035386.1; NM_011256.3. [Q6ZPQ6-2]
DR RefSeq; XP_017176233.1; XM_017320744.1.
DR AlphaFoldDB; Q6ZPQ6; -.
DR SMR; Q6ZPQ6; -.
DR BioGRID; 202842; 4.
DR IntAct; Q6ZPQ6; 4.
DR MINT; Q6ZPQ6; -.
DR STRING; 10090.ENSMUSP00000124111; -.
DR iPTMnet; Q6ZPQ6; -.
DR PhosphoSitePlus; Q6ZPQ6; -.
DR SwissPalm; Q6ZPQ6; -.
DR jPOST; Q6ZPQ6; -.
DR MaxQB; Q6ZPQ6; -.
DR PRIDE; Q6ZPQ6; -.
DR ProteomicsDB; 288172; -. [Q6ZPQ6-1]
DR ProteomicsDB; 288173; -. [Q6ZPQ6-2]
DR Antibodypedia; 1085; 71 antibodies from 13 providers.
DR DNASU; 19679; -.
DR Ensembl; ENSMUST00000086123; ENSMUSP00000083292; ENSMUSG00000029406. [Q6ZPQ6-2]
DR Ensembl; ENSMUST00000161938; ENSMUSP00000124111; ENSMUSG00000029406. [Q6ZPQ6-1]
DR Ensembl; ENSMUST00000162812; ENSMUSP00000124740; ENSMUSG00000029406. [Q6ZPQ6-2]
DR GeneID; 19679; -.
DR KEGG; mmu:19679; -.
DR UCSC; uc008zpb.3; mouse. [Q6ZPQ6-1]
DR UCSC; uc008zpc.3; mouse. [Q6ZPQ6-2]
DR CTD; 57605; -.
DR MGI; MGI:1336192; Pitpnm2.
DR VEuPathDB; HostDB:ENSMUSG00000029406; -.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000153849; -.
DR HOGENOM; CLU_007179_0_0_1; -.
DR InParanoid; Q6ZPQ6; -.
DR OMA; TPPSKIH; -.
DR OrthoDB; 122895at2759; -.
DR PhylomeDB; Q6ZPQ6; -.
DR TreeFam; TF312967; -.
DR Reactome; R-MMU-1483226; Synthesis of PI.
DR BioGRID-ORCS; 19679; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Pitpnm2; mouse.
DR PRO; PR:Q6ZPQ6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6ZPQ6; protein.
DR Bgee; ENSMUSG00000029406; Expressed in superior frontal gyrus and 203 other tissues.
DR ExpressionAtlas; Q6ZPQ6; baseline and differential.
DR Genevisible; Q6ZPQ6; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISA:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:MGI.
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; 1.
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 Alternative splicing; Calcium; Cytoplasm; Cytoskeleton; Lipid-binding;
KW Membrane; Metal-binding; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..1335
FT /note="Membrane-associated phosphatidylinositol transfer
FT protein 2"
FT /id="PRO_0000232742"
FT DOMAIN 701..949
FT /note="DDHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378"
FT REGION 32..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ72"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 814
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 843..897
FT /note="KGPSSLNHTPSIRRLSLLALPPPSPTTQGPRARARQVSPNLERAPCLPDLDI
FT GEV -> I (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10460238"
FT /id="VSP_017964"
SQ SEQUENCE 1335 AA; 148035 MW; 6119814AF6D15CBC CRC64;
MIIKEYRIPL PMTVDEYRIA QLYMIQKKSR NETHGQGSGV EILENRPYTD GPGGSGQYTH
KVYHVGMHIP GWFRSILPKA ALRVVEESWN AYPYTRTRFT CPFVEKFSID IETFYKTDTG
ENNNVFNLSP VEKSQLITDI IDIVKDPVPP SEYKTEEDPK LFQSVKTCRG PLSENWIQEY
KKRLLPIMCA YKLCKVEFRY WGMQSKIERF IHDTGLRRVM VRAHRQAWCW QDEWYGLTME
KIRELEREVQ LMLSRKMAQF SEEGPSELSK DSATKDQASG TTSDPGSKNG EPLGRGLKKQ
WSTSSKSSRS SKRGASPSRH SISEWRMQSI ARDSDEGSEE EFFDAHENLY CTEEKQAKDM
TKWNSNDLMD KMESPEPEES QDEIYQQSGS EFRVASSVEQ LNIIEDEVSQ PLAAPPSKIH
VLLLVLHGGT ILDTGAGDPS SKQGDTNTIT NVFDTVMRVH YPSALGHLAI RLVPCPPICA
DAFALVSNLS PYGHDEGCLS SSQDHIPLAA LPLLATSSPQ YQEAVATVIQ RANLAYGDFI
KSQEGVTFNG QVCLIGDCVG GILAFDALCY SGQPVSESQS SSRRGSVVSM QDADLLSPGT
LANAAHCSGG SGGGGSGGSS LESSRHLSRS NIDIPRSNGT EDSRRQLPRK RSDSSTYELD
TIQQHQAFLS SLHASVLRNE PSSRRSSSST MLDGAGALGK FDFEIADLFL FGCPLGLVLA
LRKTVIPSLD VFQLRPACQQ VYNLFHPADP SASRLEPLLE RRFHSLPPFS IPRYQRYPLG
DGCSTLLADV LQTHNTVFQE HAAPSSPGTA PAGRGFRRAS EISIASQVSG MAESYTASSI
AQKGPSSLNH TPSIRRLSLL ALPPPSPTTQ GPRARARQVS PNLERAPCLP DLDIGEVAAK
WWGQKRIDYA LYCPDALTAF PTVALPHLFH ASYWESTDVV SFLLRQVMRH DSSSILELDG
KEVSVFTPSQ PRERWQRKRT HVKLRNVAAN HRINDAVANE DGPQVVTGRF MYGPLDMVTL
TGEKVDVHIM TQPPSGEWLH LDTLVTNSSG RVSYTIPETH RLGVGVYPIK MVVRGDHTFA
DSYITVLPRG TEFVVFSIDG SFAASVSIMG SDPKVRAGAV DVVRHWQDLG YLIIYVTGRP
DMQKQRVVAW LAQHNFPHGV VSFCDGLVHD PLRHKANFLK LLISELHLRA HAAYGSTKDV
AVYNSISLSP MHIYIVGRPT KKLQQQCQFI TDGYAAHLAQ LKYNHRARPA RNTATRMALR
KGSFGLPGQS DFLRSRNHLL RTISAQPSGP SHRHDRTQTQ MDSEQRGQRS MSVAASCWGR
AMAGRLEPGA ATGPK
