GLP3L_RAT
ID GLP3L_RAT Reviewed; 285 AA.
AC Q66H74;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Golgi phosphoprotein 3-like;
GN Name=Golph3l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP SUBCELLULAR LOCATION.
RX PubMed=11042173; DOI=10.1074/jbc.m006143200;
RA Bell A.W., Ward M.A., Blackstock W.P., Freeman H.N.M., Choudhary J.S.,
RA Lewis A.P., Chotai D., Fazel A., Gushue J.N., Paiement J., Palcy S.,
RA Chevet E., Lafreniere-Roula M., Solari R., Thomas D.Y., Rowley A.,
RA Bergeron J.J.M.;
RT "Proteomics characterization of abundant Golgi membrane proteins.";
RL J. Biol. Chem. 276:5152-5165(2001).
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; BC081987; AAH81987.1; -; mRNA.
DR RefSeq; NP_001007699.1; NM_001007698.1.
DR AlphaFoldDB; Q66H74; -.
DR SMR; Q66H74; -.
DR STRING; 10116.ENSRNOP00000064938; -.
DR PaxDb; Q66H74; -.
DR Ensembl; ENSRNOT00000070919; ENSRNOP00000064938; ENSRNOG00000047620.
DR GeneID; 310669; -.
DR KEGG; rno:310669; -.
DR CTD; 55204; -.
DR RGD; 1359281; Golph3l.
DR eggNOG; KOG3983; Eukaryota.
DR GeneTree; ENSGT00390000007153; -.
DR HOGENOM; CLU_036311_0_0_1; -.
DR InParanoid; Q66H74; -.
DR OrthoDB; 1117244at2759; -.
DR PhylomeDB; Q66H74; -.
DR PRO; PR:Q66H74; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000047620; Expressed in colon and 19 other tissues.
DR ExpressionAtlas; Q66H74; baseline and differential.
DR Genevisible; Q66H74; RN.
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_0000324138"
FT REGION 1..43
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..43
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; 32922 MW; 3F6E262B27C6E26D CRC64;
MTTLTHRTRR TEVSKSCEKK IESEEDTNQE RSPDNEDPGD SKDIRLTLME EVLLLGLKDK
EGYTSFWNDC ISSGLRGGIL IELAMRGRIY LEPPTMRKKR LLDRKVLLKS DSPTGDVLLD
ETLKHIKATE PTETVQTWIE LLTGETWNPF KLQYQLRNVR ERIAKNLVEK GILTTEKQNF
LLFDMTTHPV TNTTEKQRLM KKLQDSVLER WVNDPQRMDR RTLALLVLAH SSDVLENVFS
CLTDDKYDVA MNRTKDLVEL DPEVEGTKHN ATEMIWAVLA AFNKS
