ID   GP3LA_XENLA             Reviewed;         280 AA.
AC   Q5PPU5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Golgi phosphoprotein 3-like A;
GN   Name=golph3l-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphatidylinositol-4-phosphate-binding protein that may
CC       play a role in the process of vesicle budding at the Golgi and
CC       anterograde transport to the plasma membrane. {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=Phosphatidylinositol 4-phosphate (PtdIns4P)-
CC       binding mediates recruitment to Golgi membranes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GOLPH3/VPS74 family. {ECO:0000305}.
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DR   EMBL; BC087493; AAH87493.1; -; mRNA.
DR   RefSeq; NP_001088809.1; NM_001095340.1.
DR   RefSeq; XP_018087582.1; XM_018232093.1.
DR   AlphaFoldDB; Q5PPU5; -.
DR   SMR; Q5PPU5; -.
DR   DNASU; 496077; -.
DR   GeneID; 496077; -.
DR   KEGG; xla:496077; -.
DR   CTD; 496077; -.
DR   Xenbase; XB-GENE-6252815; golph3l.S.
DR   OMA; KEXGYTS; -.
DR   OrthoDB; 1117244at2759; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 496077; Expressed in internal ear and 19 other tissues.
DR   GO; GO:0031985; C:Golgi cisterna; ISS:UniProtKB.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR   GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
DR   Gene3D; 1.10.3630.10; -; 1.
DR   InterPro; IPR008628; GPP34-like.
DR   InterPro; IPR038261; GPP34-like_sf.
DR   PANTHER; PTHR12704; PTHR12704; 1.
DR   Pfam; PF05719; GPP34; 1.
PE   2: Evidence at transcript level;
KW   Golgi apparatus; Lipid-binding; Membrane; Reference proteome.
FT   CHAIN           1..280
FT                   /note="Golgi phosphoprotein 3-like A"
FT                   /id="PRO_0000324139"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..182
FT                   /note="Beta-hairpin required for oligomerization"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT                   4-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58178"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT                   4-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58178"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT                   4-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58178"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT                   4-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58178"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   280 AA;  32281 MW;  6B23D45C08CBC0CC CRC64;
     MTTLIRRGRR AEEGQERRAD SEDSIKDKDE EESADSKDIR LTLMEEVLLL GLKDKEGYTS
     FWNDCISSGL RGGILIELFL RGRVVLEPAT IRKKRLIDKK VLLKSDKLTG DVLLDETIKH
     MKATEPAETV QSWIELLTGE TWNPFKLQYQ LRNVRERIAK NLVEKGILTT EKQNFLLFDM
     TTHPVTNTTE KQRLVKKLQE SLLERWVNDP HRMDKRTLSL LVLAHSSDVL ENAFSSLSDE
     KYDMAMNRSK ELLELDPDTE GMKPNACEMI WAVLSAFNKS