ID   GLP3L_BOVIN             Reviewed;         285 AA.
AC   A6H7F6;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Golgi phosphoprotein 3-like;
GN   Name=GOLPH3L;
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 MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphatidylinositol-4-phosphate-binding protein that may
CC       antagonize the action of GOLPH3 which is required for the process of
CC       vesicle budding at the Golgi and anterograde transport to the plasma
CC       membrane. {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer. Does not interact MYO18; differs from GOLPH3 by
CC       its inability to interact with MYO18. May interact with ARF1 (By
CC       similarity). {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; BC146227; AAI46228.1; -; mRNA.
DR   RefSeq; NP_001092522.1; NM_001099052.1.
DR   RefSeq; XP_005203965.1; XM_005203908.3.
DR   RefSeq; XP_015318243.1; XM_015462757.1.
DR   AlphaFoldDB; A6H7F6; -.
DR   SMR; A6H7F6; -.
DR   STRING; 9913.ENSBTAP00000027131; -.
DR   PaxDb; A6H7F6; -.
DR   PRIDE; A6H7F6; -.
DR   Ensembl; ENSBTAT00000027131; ENSBTAP00000027131; ENSBTAG00000020357.
DR   GeneID; 532555; -.
DR   KEGG; bta:532555; -.
DR   CTD; 55204; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020357; -.
DR   VGNC; VGNC:29493; GOLPH3L.
DR   eggNOG; KOG3983; Eukaryota.
DR   GeneTree; ENSGT00390000007153; -.
DR   HOGENOM; CLU_036311_0_0_1; -.
DR   InParanoid; A6H7F6; -.
DR   OMA; KEXGYTS; -.
DR   OrthoDB; 1117244at2759; -.
DR   TreeFam; TF314360; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000020357; Expressed in oviduct epithelium and 107 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0031985; C:Golgi cisterna; ISS:UniProtKB.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:GOC.
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:0043001; P:Golgi to plasma membrane protein transport; IBA:GO_Central.
DR   GO; GO:0048194; P:Golgi vesicle budding; IBA:GO_Central.
DR   GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
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; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..285
FT                   /note="Golgi phosphoprotein 3-like"
FT                   /id="PRO_0000324136"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..187
FT                   /note="Beta-hairpin required for oligomerization"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        8..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         67
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         76
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         157
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         160
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   MOD_RES         112
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4A5"
SQ   SEQUENCE   285 AA;  32814 MW;  C732610778D86538 CRC64;
     MTTLTHRARR TEVGKNSEKK VESEENVNQD RNQDNEDIGD SKDIRLTLME EVLLLGLKDK
     EGYTSFWNDC ISSGLRGGIL IELAMRGRIY LEPPTMRKKR LLDRKVLLKS DSPTGDVLLD
     ETLKHIKATE PTETVQTWIE LLTGETWNPF KLQYQLRNVR ERIAKNLVEK GILTTEKQNF
     LLFDMTTHPV TNTTEKQRLV KKLQDSVLER WVNDPQRMDK RTLALLVLAH SSDVLENVFS
     SLTDDKYDMA MNRAKDLVEL DPEVEGTKHS ATEMIWAVLA AFNKS