PKHA3_MOUSE
ID PKHA3_MOUSE Reviewed; 297 AA.
AC Q9ERS4;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Pleckstrin homology domain-containing family A member 3;
DE Short=PH domain-containing family A member 3;
DE AltName: Full=Phosphatidylinositol-four-phosphate adapter protein 1;
DE Short=FAPP-1;
DE Short=Phosphoinositol 4-phosphate adapter protein 1;
GN Name=Plekha3; Synonyms=Fapp1;
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].
RX PubMed=11001876; DOI=10.1042/0264-6021:3510019;
RA Dowler S.J., Currie R.A., Campbell D.G., Deak M., Kular G., Downes C.P.,
RA Alessi D.R.;
RT "Identification of pleckstrin-homology-domain-containing proteins with
RT novel phosphoinositide-binding specificities.";
RL Biochem. J. 351:19-31(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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).
CC -!- FUNCTION: Plays a role in regulation of vesicular cargo transport from
CC the trans-Golgi network (TGN) to the plasma membrane (By similarity).
CC Regulates Golgi phosphatidylinositol 4-phosphate (PtdIns(4)P) levels
CC and activates the PtdIns(4)P phosphatase activity of SACM1L when it
CC binds PtdIns(4)P in 'trans' configuration (By similarity). Binds
CC preferentially to PtdIns(4)P (By similarity). Negatively regulates APOB
CC secretion from hepatocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q9HB20}.
CC -!- SUBUNIT: Interacts with GTP-bound ARF1 (By similarity). Interacts with
CC SACM1L and VAPA and/or VAPB to form a ternary complex (By similarity).
CC {ECO:0000250|UniProtKB:Q9HB20}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9HB20}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9HB20}. Note=Localizes to ER-trans Golgi
CC network (TGN) contacts sites. {ECO:0000250|UniProtKB:Q9HB20}.
CC -!- DOMAIN: The PH domain binds the small GTPase ARF1 and
CC phosphatidylinositol-4-phosphate (PtdIns4P) with high selectivity, and
CC is required for its recruitment to the trans-Golgi network (TGN).
CC {ECO:0000250|UniProtKB:Q9HB20}.
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DR EMBL; AF286163; AAG15200.1; -; mRNA.
DR EMBL; BC031110; AAH31110.1; -; mRNA.
DR CCDS; CCDS16162.1; -.
DR RefSeq; NP_112546.1; NM_031256.3.
DR RefSeq; XP_006500509.1; XM_006500446.3.
DR AlphaFoldDB; Q9ERS4; -.
DR BMRB; Q9ERS4; -.
DR SMR; Q9ERS4; -.
DR STRING; 10090.ENSMUSP00000107551; -.
DR iPTMnet; Q9ERS4; -.
DR PhosphoSitePlus; Q9ERS4; -.
DR EPD; Q9ERS4; -.
DR MaxQB; Q9ERS4; -.
DR PaxDb; Q9ERS4; -.
DR PeptideAtlas; Q9ERS4; -.
DR PRIDE; Q9ERS4; -.
DR ProteomicsDB; 289440; -.
DR Antibodypedia; 33940; 121 antibodies from 19 providers.
DR DNASU; 83435; -.
DR Ensembl; ENSMUST00000111920; ENSMUSP00000107551; ENSMUSG00000002733.
DR GeneID; 83435; -.
DR KEGG; mmu:83435; -.
DR UCSC; uc008kfk.2; mouse.
DR CTD; 65977; -.
DR MGI; MGI:1932515; Plekha3.
DR VEuPathDB; HostDB:ENSMUSG00000002733; -.
DR eggNOG; ENOG502QPTX; Eukaryota.
DR GeneTree; ENSGT00940000155850; -.
DR HOGENOM; CLU_062751_0_0_1; -.
DR InParanoid; Q9ERS4; -.
DR OMA; VHHDETH; -.
DR OrthoDB; 952122at2759; -.
DR PhylomeDB; Q9ERS4; -.
DR TreeFam; TF317467; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR BioGRID-ORCS; 83435; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q9ERS4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9ERS4; protein.
DR Bgee; ENSMUSG00000002733; Expressed in pineal body and 258 other tissues.
DR Genevisible; Q9ERS4; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:1902387; F:ceramide 1-phosphate binding; IBA:GO_Central.
DR GO; GO:1902388; F:ceramide 1-phosphate transfer activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISO:MGI.
DR GO; GO:0035627; P:ceramide transport; IBA:GO_Central.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; IBA:GO_Central.
DR GO; GO:0120009; P:intermembrane lipid transfer; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Golgi apparatus; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..297
FT /note="Pleckstrin homology domain-containing family A
FT member 3"
FT /id="PRO_0000053879"
FT DOMAIN 1..93
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..100
FT /note="Interaction with SACM1L"
FT /evidence="ECO:0000250|UniProtKB:Q9HB20"
FT REGION 97..297
FT /note="Interaction with VAPA and VAPB"
FT /evidence="ECO:0000250|UniProtKB:Q9HB20"
FT REGION 198..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB20"
SQ SEQUENCE 297 AA; 33423 MW; BD942266DF2A1602 CRC64;
MEGVLYKWTN YLTGWQPRWF VLDNGILSYY DSQDDVCKGS KGSIKMAVCE IKVHPADNTR
MELIIPGEQH FYMKAVNAAE RQRWLVALGS SKACLTDTRT AKEKEISETS ESLKTKMSEL
RLYCDLLMQQ VHTIQEFVHR DERHPSPSVE NMNEASSLLS ATCNTFITTL EECVKIANAK
FKPEMFQLPH PDPLVSPVSP SPVQMMKRSA SHPGSCSSER SSCSIKEPAS ALHRLPQRRR
RTYSDTDSCN DVPPEDPERP LHCSGNTLNG DLASATIPEE SRLMAKTQSE EPLLPFS
