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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
 
 
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