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   03-AUG-2022, entry version 73.
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.ENSBTAP00000000679; -.
DR   PaxDb; F1MS15; -.
DR   Ensembl; ENSBTAT00000083674; ENSBTAP00000071141; ENSBTAG00000000521.
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; SKMKHPV; -.
DR   OrthoDB; 952122at2759; -.
DR   TreeFam; TF317467; -.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000000521; Expressed in oocyte and 107 other 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:0005654; C:nucleoplasm; IEA:Ensembl.
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:0035627; P:ceramide transport; IBA:GO_Central.
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   Gene3D; 1.10.3520.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 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   Pfam; PF08718; GLTP; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF110004; SSF110004; 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