GLP3L_HUMAN
ID GLP3L_HUMAN Reviewed; 285 AA.
AC Q9H4A5; B1AN09; B7Z6N3; Q9NVK0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Golgi phosphoprotein 3-like;
DE AltName: Full=GPP34-related protein;
GN Name=GOLPH3L; Synonyms=GPP34R;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP MUTAGENESIS OF 7-ARG--ARG-10, COATOMER-BINDING, AND INTERACTION WITH ARF1.
RX PubMed=22889169; DOI=10.1111/j.1600-0854.2012.01403.x;
RA Tu L., Chen L., Banfield D.K.;
RT "A conserved N-terminal arginine-motif in GOLPH3-family proteins mediates
RT binding to coatomer.";
RL Traffic 13:1496-1507(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP FUNCTION, LIPID-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=23345592; DOI=10.1091/mbc.e12-07-0525;
RA Ng M.M., Dippold H.C., Buschman M.D., Noakes C.J., Field S.J.;
RT "GOLPH3L antagonizes GOLPH3 to determine Golgi morphology.";
RL Mol. Biol. Cell 24:796-808(2013).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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:0000269|PubMed:23345592}.
CC -!- SUBUNIT: Homooligomer (By similarity). Does not interact MYO18; differs
CC from GOLPH3 by its inability to interact with MYO18. May interact with
CC ARF1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9H4A5; P50570-2: DNM2; NbExp=3; IntAct=EBI-4403434, EBI-10968534;
CC Q9H4A5; P42858: HTT; NbExp=20; IntAct=EBI-4403434, EBI-466029;
CC Q9H4A5; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-4403434, EBI-739832;
CC Q9H4A5; O14656-2: TOR1A; NbExp=3; IntAct=EBI-4403434, EBI-25847109;
CC Q9H4A5; Q8IUH5: ZDHHC17; NbExp=2; IntAct=EBI-4403434, EBI-524753;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:23345592}; Peripheral membrane protein
CC {ECO:0000269|PubMed:23345592}; Cytoplasmic side
CC {ECO:0000269|PubMed:23345592}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:23345592}; Peripheral membrane protein
CC {ECO:0000269|PubMed:23345592}; Cytoplasmic side
CC {ECO:0000269|PubMed:23345592}. Note=Phosphatidylinositol 4-phosphate
CC (PtdIns4P)-binding mediates recruitment to Golgi membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H4A5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H4A5-2; Sequence=VSP_055229;
CC -!- SIMILARITY: Belongs to the GOLPH3/VPS74 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91750.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ296153; CAC13125.1; -; mRNA.
DR EMBL; AK001549; BAA91750.1; ALT_INIT; mRNA.
DR EMBL; AK300635; BAH13319.1; -; mRNA.
DR EMBL; AK315594; BAG37966.1; -; mRNA.
DR EMBL; AL356292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53526.1; -; Genomic_DNA.
DR EMBL; BC013870; AAH13870.1; -; mRNA.
DR CCDS; CCDS966.1; -. [Q9H4A5-1]
DR RefSeq; NP_060648.2; NM_018178.5. [Q9H4A5-1]
DR AlphaFoldDB; Q9H4A5; -.
DR SMR; Q9H4A5; -.
DR BioGRID; 120500; 43.
DR IntAct; Q9H4A5; 23.
DR MINT; Q9H4A5; -.
DR STRING; 9606.ENSP00000271732; -.
DR iPTMnet; Q9H4A5; -.
DR PhosphoSitePlus; Q9H4A5; -.
DR BioMuta; GOLPH3L; -.
DR DMDM; 74752638; -.
DR EPD; Q9H4A5; -.
DR jPOST; Q9H4A5; -.
DR MassIVE; Q9H4A5; -.
DR MaxQB; Q9H4A5; -.
DR PaxDb; Q9H4A5; -.
DR PeptideAtlas; Q9H4A5; -.
DR PRIDE; Q9H4A5; -.
DR ProteomicsDB; 80810; -. [Q9H4A5-1]
DR Antibodypedia; 34036; 137 antibodies from 19 providers.
DR DNASU; 55204; -.
DR Ensembl; ENST00000271732.8; ENSP00000271732.3; ENSG00000143457.11. [Q9H4A5-1]
DR GeneID; 55204; -.
DR KEGG; hsa:55204; -.
DR MANE-Select; ENST00000271732.8; ENSP00000271732.3; NM_018178.6; NP_060648.2.
DR UCSC; uc001evj.3; human. [Q9H4A5-1]
DR CTD; 55204; -.
DR DisGeNET; 55204; -.
DR GeneCards; GOLPH3L; -.
DR HGNC; HGNC:24882; GOLPH3L.
DR HPA; ENSG00000143457; Low tissue specificity.
DR MIM; 612208; gene.
DR neXtProt; NX_Q9H4A5; -.
DR OpenTargets; ENSG00000143457; -.
DR PharmGKB; PA134922683; -.
DR VEuPathDB; HostDB:ENSG00000143457; -.
DR eggNOG; KOG3983; Eukaryota.
DR GeneTree; ENSGT00390000007153; -.
DR InParanoid; Q9H4A5; -.
DR OMA; KEXGYTS; -.
DR OrthoDB; 1117244at2759; -.
DR PhylomeDB; Q9H4A5; -.
DR TreeFam; TF314360; -.
DR PathwayCommons; Q9H4A5; -.
DR SignaLink; Q9H4A5; -.
DR BioGRID-ORCS; 55204; 6 hits in 1080 CRISPR screens.
DR ChiTaRS; GOLPH3L; human.
DR GenomeRNAi; 55204; -.
DR Pharos; Q9H4A5; Tbio.
DR PRO; PR:Q9H4A5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H4A5; protein.
DR Bgee; ENSG00000143457; Expressed in corpus epididymis and 204 other tissues.
DR ExpressionAtlas; Q9H4A5; baseline and differential.
DR Genevisible; Q9H4A5; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0031985; C:Golgi cisterna; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IC:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; IC:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP: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; IMP: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 1: Evidence at protein level;
KW Alternative splicing; Golgi apparatus; Lipid-binding; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..285
FT /note="Golgi phosphoprotein 3-like"
FT /id="PRO_0000324135"
FT REGION 1..42
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..42
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:0007744|PubMed:23186163"
FT VAR_SEQ 62..105
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055229"
FT MUTAGEN 7..10
FT /note="RARR->AAAA: Loss of binding to coatomer."
FT /evidence="ECO:0000269|PubMed:22889169"
FT CONFLICT 112
FT /note="S -> G (in Ref. 2; BAH13319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 32767 MW; E618915FD86F3772 CRC64;
MTTLTHRARR TEISKNSEKK MESEEDSNWE KSPDNEDSGD SKDIRLTLME EVLLLGLKDK
EGYTSFWNDC ISSGLRGGIL IELAMRGRIY LEPPTMRKKR LLDRKVLLKS DSPTGDVLLD
ETLKHIKATE PTETVQTWIE LLTGETWNPF KLQYQLRNVR ERIAKNLVEK GILTTEKQNF
LLFDMTTHPV TNTTEKQRLV KKLQDSVLER WVNDPQRMDK RTLALLVLAH SSDVLENVFS
SLTDDKYDVA MNRAKDLVEL DPEVEGTKPS ATEMIWAVLA AFNKS
