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Protein

Membrane-associated phosphatidylinositol transfer protein 1

Gene

Pitpnm1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates RHOA activity, and plays a role in cytoskeleton remodeling. Necessary for normal completion of cytokinesis. Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus. Binds phosphatidyl inositol phosphates (in vitro). May catalyze the transfer of phosphatidylinositol and phosphatidylcholine between membranes (By similarity). Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus. Required for protein export from the endoplasmic reticulum and the Golgi. Binds calcium ions (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-associated phosphatidylinositol transfer protein 1
Alternative name(s):
Drosophila retinal degeneration B homolog 1
Short name:
RdgB1
Mpt-1
Phosphatidylinositol transfer protein, membrane-associated 1
Short name:
PITPnm 1
Pyk2 N-terminal domain-interacting receptor 2
Short name:
NIR-2
Gene namesi
Name:Pitpnm1
Synonyms:Dres9, Mpt1, Nir2, Pitpnm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1197524. Pitpnm1.

Subcellular locationi

  • Cytoplasm By similarity
  • Golgi apparatusGolgi stack membrane By similarity; Peripheral membrane protein By similarity
  • Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity
  • Lipid droplet By similarity
  • Cleavage furrow By similarity
  • Midbody By similarity

  • Note: Peripheral membrane protein associated with Golgi stacks in interphase cells. A minor proportion is associated with the endoplasmic reticulum. Associated with lipid droplets. Dissociates from the Golgi early on in mitosis and localizes to the cleavage furrow and midbody during cytokinesis.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Lipid droplet, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12431243Membrane-associated phosphatidylinositol transfer protein 1PRO_0000232739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei282 – 2821PhosphothreonineCombined sources
Modified residuei287 – 2871PhosphothreonineCombined sources
Modified residuei300 – 3001PhosphoserineCombined sources
Modified residuei304 – 3041PhosphoserineCombined sources
Modified residuei319 – 3191PhosphoserineCombined sources
Modified residuei326 – 3261PhosphoserineCombined sources
Modified residuei329 – 3291PhosphoserineCombined sources
Modified residuei342 – 3421PhosphoserineBy similarity
Modified residuei345 – 3451PhosphoserineBy similarity
Modified residuei346 – 3461PhosphoserineBy similarity
Modified residuei373 – 3731PhosphoserineCombined sources
Modified residuei382 – 3821Phosphoserine; by CDK1By similarity
Modified residuei593 – 5931PhosphoserineCombined sources
Modified residuei600 – 6001PhosphoserineBy similarity
Modified residuei621 – 6211PhosphoserineBy similarity
Modified residuei895 – 8951PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on multiple sites by CDK1 at the onset of mitosis. Phosphorylation facilitates dissociation from the Golgi complex and is required for interaction with PLK1 (By similarity).By similarity
Phosphorylated on threonine residues upon treatment with oleic acid.By similarity
Phosphorylated on tyrosine residues by PTK2B.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO35954.
MaxQBiO35954.
PaxDbiO35954.
PRIDEiO35954.

PTM databases

iPTMnetiO35954.
PhosphoSiteiO35954.

Expressioni

Tissue specificityi

Detected at high levels in brain, and at lower levels in lung, kidney, spleen and liver (at protein level). Ubiquitous. Highly expressed in embryonic retina and the central nervous system.2 Publications

Developmental stagei

Detected at low levels during fetal development up to day 15. Highly expressed at day 17.

Gene expression databases

BgeeiO35954.
CleanExiMM_PITPNM1.
ExpressionAtlasiO35954. baseline and differential.
GenevisibleiO35954. MM.

Interactioni

Subunit structurei

Interacts with PTK2B via its C-terminus. Interacts with RHOA. Has higher affinity for the inactive, GDP-bound form of RHOA. The CDK1-phosphorylated form interacts with PLK1. Interacts with VAPB and PIK4CA (By similarity).By similarity

Protein-protein interaction databases

BioGridi202185. 1 interaction.
IntActiO35954. 1 interaction.
MINTiMINT-4104925.
STRINGi10090.ENSMUSP00000054309.

Structurei

3D structure databases

ProteinModelPortaliO35954.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini684 – 878195DDHDPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi310 – 31910Poly-Ser

Sequence similaritiesi

Contains 1 DDHD domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3668. Eukaryota.
COG5083. LUCA.
GeneTreeiENSGT00760000119216.
HOGENOMiHOG000294231.
HOVERGENiHBG052733.
InParanoidiO35954.
OMAiVKILERW.
OrthoDBiEOG7NW69J.
PhylomeDBiO35954.
TreeFamiTF312967.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
3.40.50.1000. 1 hit.
InterProiIPR004177. DDHD_dom.
IPR023214. HAD-like_dom.
IPR031315. LNS2/PITP.
IPR001666. PI_transfer.
IPR023393. START-like_dom.
[Graphical view]
PANTHERiPTHR10658. PTHR10658. 1 hit.
PfamiPF02862. DDHD. 1 hit.
PF02121. IP_trans. 1 hit.
[Graphical view]
PRINTSiPR00391. PITRANSFER.
SMARTiSM01127. DDHD. 1 hit.
SM00775. LNS2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
PROSITEiPS51043. DDHD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35954-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIKEYHILL PMSLDEYQVA QLYMIQKKSR EESSGEGSGV EILANRPYTD
60 70 80 90 100
GPGGNGQYTH KVYHVGSHIP GWFRALLPKA ALQVEEESWN AYPYTRTRYT
110 120 130 140 150
CPFVEKFSIE IETYYLPDGG QQPNVFNLSG AERRQRIVDT IDIVRDAVAP
160 170 180 190 200
GEYKAEEDPR LYRSAKTGRG PLADDWARTA AQTGPLMCAY KLCKVEFRYW
210 220 230 240 250
GMQAKIEQFI HDVGLRRVML RAHRQAWCWQ DEWIELSMAD IRALEEETAR
260 270 280 290 300
MLAQRMAKCN TGSEGPEAQT PGKSSTEARP GTSTAGTPDG PEAPPGPDAS
310 320 330 340 350
PDASFGKQWS SSSRSSYSSQ HGGGVSPQSL SEWRMQNIAR DSENSSEEEF
360 370 380 390 400
FDAHEGFSDS DEVFPKEMTK WNSNDFIDAF ASPTEVEGVP DPTVMATKGI
410 420 430 440 450
EDGARAPRDS EGLDGAGDLV VEACSVHALF LILHSGSILD SGPGDTNSKQ
460 470 480 490 500
ADVQTLSTAF EAVTRVHFPE ALGHVALRLV PCPPICAAAY ALVSNLSPYS
510 520 530 540 550
HDGDSLSRSQ DHIPLAALPL LATSSSRYQG AVATVIARTN QAYAAFLRSS
560 570 580 590 600
EGTGFCGQVV LIGDGVGGIL GFDALCHSAS AGPGSRGSSR RGSMNNEMLS
610 620 630 640 650
PEVGPVRDPL ADGVEVLGRA SPEPSALPAQ RTFSDMANPD PDGSQNSLQV
660 670 680 690 700
ASTATSSGEP RRASTASCPP ASSEAPDGPT NAARLDFKVS GFFLFGSPLG
710 720 730 740 750
LVLALRKTVM PALEVAQLRP ACEQIYNLFH AADPCASRLE PLLAPKFQAI
760 770 780 790 800
APLAVPRYQK FPLGDGSSLL LADTLQTHSS LFLEELEMMV PSTPTSASGA
810 820 830 840 850
FWKGSELGNE PASQTAAPST TSEVVKILDR WWGNKRIDYS LYCPEALTAF
860 870 880 890 900
PTVTLPHLFH ASYWESADVV AFILRQVIEK ERPQLTECEE PSIYSPAFPR
910 920 930 940 950
EKWQRKRTQV KIRNVTSNHR ASDTVVCEGR PQVLNGRFMY GPLDVVTLTG
960 970 980 990 1000
EKVDVYVMTQ PLSGKWIHFG TEVTNSSGRL TFPVPSERAL GIGVYPVRMV
1010 1020 1030 1040 1050
VRGDHTYAEC CLTVVSRGTE AVVFSIDGSF TASVSIMGSD PKVRAGAVDV
1060 1070 1080 1090 1100
VRHWQDSGYL IVYVTGRPDM QKHRVVAWLS QHNFPHGVVS FCDGLTHDPL
1110 1120 1130 1140 1150
RQKAMFLQSL VQEVELNIVA GYGSPKDVAV YAALGLSPSQ TYIVGRAVRK
1160 1170 1180 1190 1200
LQAQCQFLSD GYVAHLGQLE AGSHSHAPSG PPRAALAKSS YAVAAPVDFL
1210 1220 1230 1240
RKQSQLLRSR GPSQVDREGP GTPPTTLARG KTRSISLKLD SEE
Length:1,243
Mass (Da):134,940
Last modified:January 1, 1998 - v1
Checksum:i98E247536527D83E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006467 mRNA. Translation: AAB84393.1.
Y08922 mRNA. Translation: CAA70127.1.
BC044893 mRNA. Translation: AAH44893.1.
BC048150 mRNA. Translation: AAH48150.1.
CCDSiCCDS37883.1.
PIRiJC5615.
RefSeqiNP_032877.1. NM_008851.4.
UniGeneiMm.1860.

Genome annotation databases

EnsembliENSMUST00000049658; ENSMUSP00000054309; ENSMUSG00000024851.
ENSMUST00000100022; ENSMUSP00000097599; ENSMUSG00000024851.
ENSMUST00000180660; ENSMUSP00000137958; ENSMUSG00000097096.
ENSMUST00000181715; ENSMUSP00000137663; ENSMUSG00000097096.
GeneIDi18739.
KEGGimmu:18739.
UCSCiuc008fyn.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006467 mRNA. Translation: AAB84393.1.
Y08922 mRNA. Translation: CAA70127.1.
BC044893 mRNA. Translation: AAH44893.1.
BC048150 mRNA. Translation: AAH48150.1.
CCDSiCCDS37883.1.
PIRiJC5615.
RefSeqiNP_032877.1. NM_008851.4.
UniGeneiMm.1860.

3D structure databases

ProteinModelPortaliO35954.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202185. 1 interaction.
IntActiO35954. 1 interaction.
MINTiMINT-4104925.
STRINGi10090.ENSMUSP00000054309.

PTM databases

iPTMnetiO35954.
PhosphoSiteiO35954.

Proteomic databases

EPDiO35954.
MaxQBiO35954.
PaxDbiO35954.
PRIDEiO35954.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049658; ENSMUSP00000054309; ENSMUSG00000024851.
ENSMUST00000100022; ENSMUSP00000097599; ENSMUSG00000024851.
ENSMUST00000180660; ENSMUSP00000137958; ENSMUSG00000097096.
ENSMUST00000181715; ENSMUSP00000137663; ENSMUSG00000097096.
GeneIDi18739.
KEGGimmu:18739.
UCSCiuc008fyn.3. mouse.

Organism-specific databases

CTDi9600.
MGIiMGI:1197524. Pitpnm1.

Phylogenomic databases

eggNOGiKOG3668. Eukaryota.
COG5083. LUCA.
GeneTreeiENSGT00760000119216.
HOGENOMiHOG000294231.
HOVERGENiHBG052733.
InParanoidiO35954.
OMAiVKILERW.
OrthoDBiEOG7NW69J.
PhylomeDBiO35954.
TreeFamiTF312967.

Miscellaneous databases

ChiTaRSiPitpnm1. mouse.
NextBioi294877.
PROiO35954.
SOURCEiSearch...

Gene expression databases

BgeeiO35954.
CleanExiMM_PITPNM1.
ExpressionAtlasiO35954. baseline and differential.
GenevisibleiO35954. MM.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
3.40.50.1000. 1 hit.
InterProiIPR004177. DDHD_dom.
IPR023214. HAD-like_dom.
IPR031315. LNS2/PITP.
IPR001666. PI_transfer.
IPR023393. START-like_dom.
[Graphical view]
PANTHERiPTHR10658. PTHR10658. 1 hit.
PfamiPF02862. DDHD. 1 hit.
PF02121. IP_trans. 1 hit.
[Graphical view]
PRINTSiPR00391. PITRANSFER.
SMARTiSM01127. DDHD. 1 hit.
SM00775. LNS2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
PROSITEiPS51043. DDHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of mammalian homologues of the Drosophila retinal degeneration B gene."
    Aikawa Y., Hara H., Watanabe T.
    Biochem. Biophys. Res. Commun. 236:559-564(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "A mammalian homologue of the Drosophila retinal degeneration B gene: implications for the evolution of phototransduction mechanisms."
    Rubboli F., Bulfone A., Bogni S., Marchitiello A., Zollo M., Borsani G., Ballabio A., Banfi S.
    Genes Funct. 1:205-213(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Retina.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain and Eye.
  4. "Involvement of PITPnm, a mammalian homologue of Drosophila rdgB, in phosphoinositide synthesis on Golgi membranes."
    Aikawa Y., Kuraoka A., Kondo H., Kawabuchi M., Watanabe T.
    J. Biol. Chem. 274:20569-20577(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PIK4CA.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-282; THR-287; SER-300; SER-304; SER-319; SER-326; SER-329; SER-373 AND SER-593, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung, Pancreas and Spleen.

Entry informationi

Entry nameiPITM1_MOUSE
AccessioniPrimary (citable) accession number: O35954
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.