PKHA8_MOUSE
ID PKHA8_MOUSE Reviewed; 519 AA.
AC Q80W71;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
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 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 [LARGE SCALE GENOMIC DNA].
RC TISSUE=Testis;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-158 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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).
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: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q96JA3}. Membrane
CC {ECO:0000250|UniProtKB:Q96JA3}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96JA3}. Note=Binds through its PH domain to
CC PtdIns(4)P and ARF1, and subsequently localizes to TGN exit sites.
CC {ECO:0000250|UniProtKB:Q96JA3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80W71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80W71-2; Sequence=VSP_028547;
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; AC084800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052360; AAH52360.1; -; mRNA.
DR EMBL; BB865855; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS39491.1; -. [Q80W71-2]
DR CCDS; CCDS51781.1; -. [Q80W71-1]
DR RefSeq; NP_001001335.1; NM_001001335.2. [Q80W71-2]
DR RefSeq; NP_001157833.1; NM_001164361.1. [Q80W71-1]
DR AlphaFoldDB; Q80W71; -.
DR SMR; Q80W71; -.
DR STRING; 10090.ENSMUSP00000112466; -.
DR iPTMnet; Q80W71; -.
DR PhosphoSitePlus; Q80W71; -.
DR MaxQB; Q80W71; -.
DR PaxDb; Q80W71; -.
DR PRIDE; Q80W71; -.
DR ProteomicsDB; 289908; -. [Q80W71-1]
DR ProteomicsDB; 289909; -. [Q80W71-2]
DR Antibodypedia; 26151; 176 antibodies from 29 providers.
DR DNASU; 231999; -.
DR Ensembl; ENSMUST00000101385; ENSMUSP00000098935; ENSMUSG00000005225. [Q80W71-2]
DR Ensembl; ENSMUST00000119706; ENSMUSP00000112466; ENSMUSG00000005225. [Q80W71-1]
DR GeneID; 231999; -.
DR KEGG; mmu:231999; -.
DR UCSC; uc009cab.2; mouse. [Q80W71-1]
DR CTD; 84725; -.
DR MGI; MGI:2681164; Plekha8.
DR VEuPathDB; HostDB:ENSMUSG00000005225; -.
DR eggNOG; KOG3221; Eukaryota.
DR GeneTree; ENSGT00940000157288; -.
DR HOGENOM; CLU_039839_0_0_1; -.
DR InParanoid; Q80W71; -.
DR OMA; SKMKHPV; -.
DR OrthoDB; 952122at2759; -.
DR PhylomeDB; Q80W71; -.
DR TreeFam; TF317467; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR BioGRID-ORCS; 231999; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Plekha8; mouse.
DR PRO; PR:Q80W71; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80W71; protein.
DR Bgee; ENSMUSG00000005225; Expressed in manus and 221 other tissues.
DR Genevisible; Q80W71; 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-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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 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 1: Evidence at protein level;
KW Alternative splicing; Golgi apparatus; Lipid transport; Lipid-binding;
KW Membrane; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..519
FT /note="Pleckstrin homology domain-containing family A
FT member 8"
FT /id="PRO_0000306866"
FT DOMAIN 1..93
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 275..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..473
FT /note="Glycolipid transfer protein homology domain"
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"
FT VAR_SEQ 1..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028547"
SQ SEQUENCE 519 AA; 57962 MW; 9184716C4D22FABF CRC64;
MEGVLYKWTN YLSGWQPRWF LLCGGILSYY DSPEDAWKGC KGSIQMAVCE IQVHSVDNTR
MDLIIPGEQY FYLKARSVAE RQRWLVALGS AKACLTDSRT QKEKEFAENT ENLKTKMSEL
RLYCDLLVQQ VDKTKEVATA GVTDSEEGID VGTLLKSTCN TFLKTLEECM QIANAAFTSE
LLYHTPPGSP QLAVLKSSKM KHPIIPIHNS LERSMELNSC ENGSLSIEVN GDEEILMKTK
SSLYLKSTEV DCSISSEENT DDNVTVQGEI MKEDGEENLE SHDKDPAQPG SDSVCSPESP
WEDNEEVIPT FFSTMNTSFS DIELLEDSGI PTEAFLASCY AVVPVLDKLG PTVFAPVKMD
LVGNIKKVNQ KYITNKEEFT TLQKIVLHEV EADVAQVRNS ATEALLWLKR GLKFLKGFLT
EVKNGEKDIQ TALNNAYGKT LRQHHGWVVR GVFALALRAA PSYEDFVAAL TIKEGDHQKE
AFSAGMQRDL SLYLPAMEKQ LAILDTLYEI HGLESDEVV
