ID PKHA8_BOVIN Reviewed; 520 AA.
AC F1MS15;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Pleckstrin homology domain-containing family A member 8;
DE Short=PH domain-containing family A member 8;
DE AltName: Full=Phosphatidylinositol-four-phosphate adapter protein 2;
DE Short=FAPP-2;
DE Short=Phosphoinositol 4-phosphate adapter protein 2;
GN Name=PLEKHA8; Synonyms=FAPP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Cargo transport protein that is required for apical transport
CC from the trans-Golgi network (TGN). Transports AQP2 from the trans-
CC Golgi network (TGN) to sites of AQP2 phosphorylation. Mediates the non-
CC vesicular transport of glucosylceramide (GlcCer) from the trans-Golgi
CC network (TGN) to the plasma membrane and plays a pivotal role in the
CC synthesis of complex glycosphingolipids. Binding of both
CC phosphatidylinositol 4-phosphate (PIP) and ARF1 are essential for the
CC GlcCer transfer ability. Also required for primary cilium formation,
CC possibly by being involved in the transport of raft lipids to the
CC apical membrane, and for membrane tubulation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with ARF1; the interaction together with
CC phosphatidylinositol 4-phosphate binding is required for FAPP2 GlcCer
CC transfer ability. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus, trans-
CC Golgi network membrane {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=Mainly localized to the
CC trans-Golgi network (TGN) but also found at the rims of Golgi
CC cisternae. Associates with ARF1 at Golgi apparatus membranes (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The PH domain of FAPPS binds the small GTPase ARF1 and
CC phosphatidylinositol-4-phosphate (PtdIns4P) with high selectivity, and
CC is required for recruitment of FAPPs to the trans-Golgi network (TGN).
CC {ECO:0000250}.
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DR EMBL; DAAA02010917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001183961.1; NM_001197032.1.
DR AlphaFoldDB; F1MS15; -.
DR SMR; F1MS15; -.
DR STRING; 9913.ENSBTAP00000071141; -.
DR PaxDb; 9913-ENSBTAP00000000679; -.
DR Ensembl; ENSBTAT00000083674.1; ENSBTAP00000071141.1; ENSBTAG00000000521.6.
DR GeneID; 538919; -.
DR KEGG; bta:538919; -.
DR CTD; 84725; -.
DR VEuPathDB; HostDB:ENSBTAG00000000521; -.
DR VGNC; VGNC:53664; PLEKHA8.
DR eggNOG; KOG3221; Eukaryota.
DR GeneTree; ENSGT00940000157288; -.
DR HOGENOM; CLU_039839_0_0_1; -.
DR InParanoid; F1MS15; -.
DR OMA; ERQMEMN; -.
DR OrthoDB; 642641at2759; -.
DR TreeFam; TF317467; -.
DR Reactome; R-BTA-1660499; Synthesis of PIPs at the plasma membrane.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000000521; Expressed in oocyte and 107 other cell types or tissues.
DR ExpressionAtlas; F1MS15; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
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:0097001; F:ceramide binding; ISS:UniProtKB.
DR GO; GO:0051861; F:glycolipid binding; ISS:UniProtKB.
DR GO; GO:0017089; F:glycolipid transfer activity; ISS:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; ISS:UniProtKB.
DR GO; GO:0120009; P:intermembrane lipid transfer; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd01247; PH_FAPP1_FAPP2; 1.
DR Gene3D; 1.10.3520.10; Glycolipid transfer protein; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR036497; GLTP_sf.
DR InterPro; IPR014830; Glycolipid_transfer_prot_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10219; GLYCOLIPID TRANSFER PROTEIN-RELATED; 1.
DR PANTHER; PTHR10219:SF43; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY A MEMBER 8; 1.
DR Pfam; PF08718; GLTP; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF110004; Glycolipid transfer protein, GLTP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Golgi apparatus; Lipid transport; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..520
FT /note="Pleckstrin homology domain-containing family A
FT member 8"
FT /id="PRO_0000419606"
FT DOMAIN 1..93
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 275..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..520
FT /note="Glycolipid transfer protein homology domain"
FT /evidence="ECO:0000250"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D3ZY60"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZY60"
FT MOD_RES 153
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D3ZY60"
SQ SEQUENCE 520 AA; 58270 MW; B26C41230AE2EC41 CRC64;
MEGVLYKWTN YLSGWQPRWF LLCGGILSYY DSPEDAWKGC KGSIQMAVCE IQVHSVDNTR
MDLIIPGEQY FYLKARSVAE RQRWLVALGS AKACLTDSRT QKEKEFAENT ENLKTKMSEL
RLYCDLLVQQ VDKTKEVTTT GVSSSEEGID VGTLLKSTCN TFLKTLEECM QIANAAFTSE
LLYRTPPGSP QLAMLKSNKM KHPIVPIHNS LERQMELNSC ENGSLNMEIN DDEEILVRNK
SSLCLKPAET DCSISSEENT DDNITVQGEM MKENGEESLG NHDSDLAQPE LHSTSSSPES
HWEEDQEVIP TFFSTMNTSF SDIELLEDSG IPTEAFLASC YAVVPVLDKL GPTVFAPVKM
DLVGNIKKVN QKYITNKEEF TTLQKIVLHE VEADVAQVRN SATEALLWLK RGLKFLKGFL
TEVKNGEKDI QTALNNAYGK TLRQHHGWVV RGVFALALRA APSYEDFVAA LTIKEGDHQK
AAFSVGMQRD LSLYLPAMEK QLAILDTLYE VHGLESDEVV
//
