GOPC_HUMAN
ID GOPC_HUMAN Reviewed; 462 AA.
AC Q9HD26; A6NM30; Q59FS4; Q969U8;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Golgi-associated PDZ and coiled-coil motif-containing protein {ECO:0000312|HGNC:HGNC:17643};
DE AltName: Full=CFTR-associated ligand;
DE AltName: Full=Fused in glioblastoma;
DE AltName: Full=PDZ protein interacting specifically with TC10 {ECO:0000303|PubMed:11162552};
DE Short=PIST {ECO:0000303|PubMed:11162552};
GN Name=GOPC {ECO:0000312|HGNC:HGNC:17643};
GN Synonyms=CAL {ECO:0000303|PubMed:14570915}, FIG;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11162552; DOI=10.1006/bbrc.2000.4160;
RA Neudauer C.L., Joberty G., Macara I.G.;
RT "PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family
RT GTPase TC10.";
RL Biochem. Biophys. Res. Commun. 280:541-547(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, INTERACTION WITH STX6, AND MUTAGENESIS OF LEU-175; LEU-182;
RP LEU-189 AND LEU-196.
RC TISSUE=Myeloid leukemia cell;
RX PubMed=11384996; DOI=10.1074/jbc.m104137200;
RA Charest A., Lane K., McMahon K., Housman D.E.;
RT "Association of a novel PDZ domain-containing peripheral Golgi protein with
RT the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF)
RT attachment protein receptor) protein syntaxin 6.";
RL J. Biol. Chem. 276:29456-29465(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, OLIGOMERIZATION, INTERACTION WITH CFTR, AND DOMAIN.
RC TISSUE=Lung;
RX PubMed=11707463; DOI=10.1074/jbc.m110177200;
RA Cheng J., Moyer B.D., Milewski M., Loffing J., Ikeda M., Mickle J.E.,
RA Cutting G.R., Li M., Stanton B.A., Guggino W.B.;
RT "A Golgi-associated PDZ domain protein modulates cystic fibrosis
RT transmembrane regulator plasma membrane expression.";
RL J. Biol. Chem. 277:3520-3529(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
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 [8]
RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH ROS1.
RX PubMed=12661006; DOI=10.1002/gcc.10207;
RA Charest A., Lane K., McMahon K., Park J., Preisinger E., Conroy H.,
RA Housman D.;
RT "Fusion of FIG to the receptor tyrosine kinase ROS in a glioblastoma with
RT an interstitial del(6)(q21q21).";
RL Genes Chromosomes Cancer 37:58-71(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [10]
RP FUNCTION.
RX PubMed=14570915; DOI=10.1074/jbc.m308640200;
RA Cheng J., Wang H., Guggino W.B.;
RT "Modulation of mature cystic fibrosis transmembrane regulator protein by
RT the PDZ domain protein CAL.";
RL J. Biol. Chem. 279:1892-1898(2004).
RN [11]
RP INTERACTION WITH ASIC3.
RX PubMed=15317815; DOI=10.1074/jbc.m405874200;
RA Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J.;
RT "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have
RT opposite effects on H+- gated current.";
RL J. Biol. Chem. 279:46962-46968(2004).
RN [12]
RP INTERACTION WITH ADRB1, DOMAIN, AND FUNCTION.
RX PubMed=15358775; DOI=10.1074/jbc.m404876200;
RA He J., Bellini M., Xu J., Castleberry A.M., Hall R.A.;
RT "Interaction with cystic fibrosis transmembrane conductance regulator-
RT associated ligand (CAL) inhibits beta1-adrenergic receptor surface
RT expression.";
RL J. Biol. Chem. 279:50190-50196(2004).
RN [13]
RP INTERACTION WITH RHOQ.
RX PubMed=15546864; DOI=10.1074/jbc.m410026200;
RA Cheng J., Wang H., Guggino W.B.;
RT "Regulation of cystic fibrosis transmembrane regulator trafficking and
RT protein expression by a Rho family small GTPase TC10.";
RL J. Biol. Chem. 280:3731-3739(2005).
RN [14]
RP INTERACTION WITH GOLGA3, AND SUBCELLULAR LOCATION.
RX PubMed=15951434; DOI=10.1074/jbc.m504937200;
RA Hicks S.W., Machamer C.E.;
RT "Isoform-specific interaction of golgin-160 with the Golgi-associated
RT protein PIST.";
RL J. Biol. Chem. 280:28944-28951(2005).
RN [15]
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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP FUNCTION, INTERACTION WITH MARCHF2, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF 216-GLY--PRO-404.
RX PubMed=23818989; DOI=10.1371/journal.pone.0068001;
RA Cheng J., Guggino W.;
RT "Ubiquitination and degradation of CFTR by the E3 ubiquitin ligase MARCH2
RT through its association with adaptor proteins CAL and STX6.";
RL PLoS ONE 8:e68001-e68001(2013).
RN [19]
RP STRUCTURE BY NMR OF 278-371, AND INTERACTION WITH NLGN1 AND FZD8.
RX PubMed=16882988; DOI=10.1110/ps.062087506;
RA Li X., Zhang J., Cao Z., Wu J., Shi Y.;
RT "Solution structure of GOPC PDZ domain and its interaction with the C-
RT terminal motif of neuroligin.";
RL Protein Sci. 15:2149-2158(2006).
CC -!- FUNCTION: Plays a role in intracellular protein trafficking and
CC degradation (PubMed:11707463, PubMed:14570915, PubMed:15358775). May
CC regulate CFTR chloride currents and acid-induced ASIC3 currents by
CC modulating cell surface expression of both channels (By similarity).
CC May also regulate the intracellular trafficking of the ADR1B receptor
CC (PubMed:15358775). May play a role in autophagy (By similarity).
CC Together with MARCHF2 mediates the ubiquitination and lysosomal
CC degradation of CFTR (PubMed:23818989). Overexpression results in CFTR
CC intracellular retention and lysosomaldegradation in the lysosomes
CC (PubMed:11707463, PubMed:14570915). {ECO:0000250|UniProtKB:Q8BH60,
CC ECO:0000269|PubMed:11707463, ECO:0000269|PubMed:14570915,
CC ECO:0000269|PubMed:15358775, ECO:0000269|PubMed:23818989}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with FZD5 (By
CC similarity). Interacts with FZD8 (PubMed:16882988). Interacts with
CC GRID2 and BECN1 (By similarity). Interacts with CSPG5 (By similarity).
CC Interacts with CLCN3 (By similarity). Interacts with STX6
CC (PubMed:11384996). Interacts with CFTR (PubMed:11707463). Interacts
CC with ASIC3 (PubMed:15317815). Interacts with GOLGA3 (PubMed:15951434).
CC Interacts with NLGN1 (PubMed:16882988). Interacs with RHOQ
CC (PubMed:15546864). Interacts with MARCHF2; the interaction leads to
CC CFTR ubiquitination and degradation (PubMed:23818989). Interacts with
CC ADRB1 (PubMed:15358775). May interact with CACNG2 (By similarity).
CC {ECO:0000250|UniProtKB:Q8BH60, ECO:0000269|PubMed:11384996,
CC ECO:0000269|PubMed:11707463, ECO:0000269|PubMed:15317815,
CC ECO:0000269|PubMed:15358775, ECO:0000269|PubMed:15546864,
CC ECO:0000269|PubMed:15951434, ECO:0000269|PubMed:16882988,
CC ECO:0000269|PubMed:23818989}.
CC -!- INTERACTION:
CC Q9HD26; Q9H9L7: AKIRIN1; NbExp=3; IntAct=EBI-349832, EBI-10309796;
CC Q9HD26; Q16520: BATF; NbExp=3; IntAct=EBI-349832, EBI-749503;
CC Q9HD26; Q0P5P2: C17orf67; NbExp=3; IntAct=EBI-349832, EBI-10226540;
CC Q9HD26; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-349832, EBI-10171570;
CC Q9HD26; P13569: CFTR; NbExp=4; IntAct=EBI-349832, EBI-349854;
CC Q9HD26; Q12882: DPYD; NbExp=3; IntAct=EBI-349832, EBI-2839838;
CC Q9HD26; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-349832, EBI-6658203;
CC Q9HD26; P15408: FOSL2; NbExp=4; IntAct=EBI-349832, EBI-3893419;
CC Q9HD26; P08631: HCK; NbExp=3; IntAct=EBI-349832, EBI-346340;
CC Q9HD26; V9HWD0: HEL-S-42; NbExp=4; IntAct=EBI-349832, EBI-10330219;
CC Q9HD26; P05412: JUN; NbExp=3; IntAct=EBI-349832, EBI-852823;
CC Q9HD26; Q6UWP7: LCLAT1; NbExp=3; IntAct=EBI-349832, EBI-10254507;
CC Q9HD26; Q8WVZ3: MORN4; NbExp=3; IntAct=EBI-349832, EBI-10277137;
CC Q9HD26; Q9BYD6: MRPL1; NbExp=3; IntAct=EBI-349832, EBI-5325394;
CC Q9HD26; Q15746: MYLK; NbExp=3; IntAct=EBI-349832, EBI-968482;
CC Q9HD26; Q8IZQ8: MYOCD; NbExp=4; IntAct=EBI-349832, EBI-493384;
CC Q9HD26; Q99497: PARK7; NbExp=3; IntAct=EBI-349832, EBI-1164361;
CC Q9HD26; Q7Z2X4: PID1; NbExp=3; IntAct=EBI-349832, EBI-10256685;
CC Q9HD26; Q2TAK8-2: PWWP3A; NbExp=3; IntAct=EBI-349832, EBI-10239402;
CC Q9HD26; Q96D59: RNF183; NbExp=3; IntAct=EBI-349832, EBI-743938;
CC Q9HD26; Q9BWG1: RNF220; NbExp=3; IntAct=EBI-349832, EBI-10300482;
CC Q9HD26; Q9NTN9: SEMA4G; NbExp=3; IntAct=EBI-349832, EBI-6447340;
CC Q9HD26; Q9H1K4: SLC25A18; NbExp=3; IntAct=EBI-349832, EBI-6269587;
CC Q9HD26; Q7LBE3-1: SLC26A9; NbExp=2; IntAct=EBI-349832, EBI-25464835;
CC Q9HD26; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-349832, EBI-8635958;
CC Q9HD26; O43805: SSNA1; NbExp=3; IntAct=EBI-349832, EBI-2515299;
CC Q9HD26; Q14849: STARD3; NbExp=3; IntAct=EBI-349832, EBI-9819324;
CC Q9HD26; P04004: VTN; NbExp=4; IntAct=EBI-349832, EBI-1036653;
CC Q9HD26; Q6ZSB9: ZBTB49; NbExp=5; IntAct=EBI-349832, EBI-2859943;
CC Q9HD26; Q32MK9: ZNF509; NbExp=3; IntAct=EBI-349832, EBI-10239929;
CC Q9HD26; Q8TBZ8: ZNF564; NbExp=3; IntAct=EBI-349832, EBI-10273713;
CC Q9HD26; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-349832, EBI-745520;
CC Q9HD26; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-349832, EBI-6427977;
CC Q9HD26; Q8NBB4: ZSCAN1; NbExp=3; IntAct=EBI-349832, EBI-5292994;
CC Q9HD26; Q9R0W0: mGluR1a; Xeno; NbExp=7; IntAct=EBI-349832, EBI-8505383;
CC Q9HD26-2; Q7Z3C6-3: ATG9A; NbExp=5; IntAct=EBI-11102276, EBI-12006308;
CC Q9HD26-2; Q68D86: CCDC102B; NbExp=4; IntAct=EBI-11102276, EBI-10171570;
CC Q9HD26-2; E9PSE9: CCDC198; NbExp=3; IntAct=EBI-11102276, EBI-11748295;
CC Q9HD26-2; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-11102276, EBI-10175124;
CC Q9HD26-2; P55040: GEM; NbExp=3; IntAct=EBI-11102276, EBI-744104;
CC Q9HD26-2; P08631-2: HCK; NbExp=3; IntAct=EBI-11102276, EBI-9834454;
CC Q9HD26-2; Q15746-7: MYLK; NbExp=5; IntAct=EBI-11102276, EBI-12189939;
CC Q9HD26-2; Q969R2-2: OSBP2; NbExp=3; IntAct=EBI-11102276, EBI-12211505;
CC Q9HD26-2; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-11102276, EBI-2557469;
CC Q9HD26-2; Q86X10: RALGAPB; NbExp=3; IntAct=EBI-11102276, EBI-1755842;
CC Q9HD26-2; Q96D59: RNF183; NbExp=3; IntAct=EBI-11102276, EBI-743938;
CC Q9HD26-2; Q8N9S9-2: SNX31; NbExp=3; IntAct=EBI-11102276, EBI-11745060;
CC Q9HD26-2; P04004: VTN; NbExp=3; IntAct=EBI-11102276, EBI-1036653;
CC Q9HD26-2; Q6ZSB9: ZBTB49; NbExp=3; IntAct=EBI-11102276, EBI-2859943;
CC Q9HD26-2; Q8WTX9: ZDHHC1; NbExp=3; IntAct=EBI-11102276, EBI-2818796;
CC Q9HD26-2; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-11102276, EBI-5667516;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane
CC {ECO:0000269|PubMed:23818989}; Peripheral membrane protein. Golgi
CC apparatus, trans-Golgi network membrane; Peripheral membrane protein.
CC Synapse {ECO:0000250}. Postsynaptic density {ECO:0000250}. Cell
CC projection, dendrite {ECO:0000250}. Note=Enriched in synaptosomal and
CC postsynaptic densities (PSD) fractions. Expressed in cell bodies and
CC dendrites of Purkinje cells. Localized at the trans-Golgi network (TGN)
CC of spermatids and the medulla of round spermatides. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9HD26-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HD26-2; Sequence=VSP_016062;
CC Name=3;
CC IsoId=Q9HD26-3; Sequence=VSP_016063, VSP_016064;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11162552, ECO:0000269|PubMed:11384996,
CC ECO:0000269|PubMed:11707463}.
CC -!- DOMAIN: The PDZ domain mediates interactions with FZD5, FZD8, ASIC3,
CC GRID2, CLCN3 (By similarity). Mediates also interaction with CFTR and
CC ADRB1. {ECO:0000250, ECO:0000269|PubMed:11707463,
CC ECO:0000269|PubMed:15358775}.
CC -!- DOMAIN: The coiled-coil region probably mediates association to
CC membranes, targeting to the Golgi, and interactions with GOLGA3, and
CC STX6. May also mediate interaction with RHOQ (By similarity).
CC {ECO:0000250}.
CC -!- DISEASE: Note=A chromosomal aberration involving GOPC is found in a
CC glioblastoma multiforme sample. An intra-chromosomal deletion
CC del(6)(q21q21) is responsible for the formation of GOPC-ROS1 chimeric
CC protein which has a constitutive receptor tyrosine kinase activity.
CC {ECO:0000269|PubMed:12661006}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92622.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF287894; AAG00572.1; -; mRNA.
DR EMBL; AY033606; AAK57733.1; -; mRNA.
DR EMBL; AF450008; AAL47160.1; -; mRNA.
DR EMBL; AB209385; BAD92622.1; ALT_INIT; mRNA.
DR EMBL; AL589939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z85999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48205.1; -; Genomic_DNA.
DR EMBL; BC009553; AAH09553.1; -; mRNA.
DR CCDS; CCDS34523.1; -. [Q9HD26-2]
DR CCDS; CCDS5117.1; -. [Q9HD26-1]
DR RefSeq; NP_001017408.1; NM_001017408.2. [Q9HD26-2]
DR RefSeq; NP_065132.1; NM_020399.3. [Q9HD26-1]
DR PDB; 2DC2; NMR; -; A=278-371.
DR PDB; 2LOB; NMR; -; A=286-370.
DR PDB; 4E34; X-ray; 1.40 A; A/B=284-370.
DR PDB; 4E35; X-ray; 1.40 A; A/B=284-370.
DR PDB; 4JOE; X-ray; 1.14 A; A/B=284-370.
DR PDB; 4JOF; X-ray; 1.20 A; A/B=284-370.
DR PDB; 4JOG; X-ray; 1.46 A; A/B=284-370.
DR PDB; 4JOH; X-ray; 1.47 A; A/B=284-370.
DR PDB; 4JOJ; X-ray; 1.20 A; A/B=284-370.
DR PDB; 4JOK; X-ray; 1.09 A; A/B=284-370.
DR PDB; 4JOP; X-ray; 1.80 A; A/B=284-370.
DR PDB; 4JOR; X-ray; 1.34 A; A/B=284-370.
DR PDB; 4K6Y; X-ray; 1.48 A; A/B=284-370.
DR PDB; 4K72; X-ray; 1.90 A; A/B=284-370.
DR PDB; 4K75; X-ray; 1.50 A; A=284-370.
DR PDB; 4K76; X-ray; 1.75 A; A/B/C/D=284-370.
DR PDB; 4K78; X-ray; 1.80 A; A=284-370.
DR PDB; 4NMO; X-ray; 1.40 A; A/B=284-370.
DR PDB; 4NMP; X-ray; 1.30 A; A/B=284-370.
DR PDB; 4NMQ; X-ray; 1.40 A; A/B=284-370.
DR PDB; 4NMR; X-ray; 1.55 A; A/B=284-370.
DR PDB; 4NMS; X-ray; 1.70 A; A/B=284-370.
DR PDB; 4NMT; X-ray; 1.40 A; A/B=284-370.
DR PDB; 4NMV; X-ray; 1.40 A; A/B=284-370.
DR PDB; 4Q6H; X-ray; 1.90 A; A=284-370.
DR PDB; 4Q6S; X-ray; 1.45 A; A/B=284-370.
DR PDB; 5IC3; X-ray; 1.70 A; A/B=284-370.
DR PDB; 5K4F; X-ray; 1.36 A; A/B=284-370.
DR PDB; 6OV7; X-ray; 1.71 A; A/B=284-370.
DR PDB; 6V84; X-ray; 1.64 A; A/B=284-370.
DR PDB; 6XNJ; X-ray; 1.85 A; A=280-370.
DR PDB; 7JZO; X-ray; 1.61 A; A/B=284-370.
DR PDB; 7JZP; X-ray; 1.95 A; A/B=284-370.
DR PDB; 7JZQ; X-ray; 1.35 A; A=284-370.
DR PDB; 7JZR; X-ray; 1.54 A; A/B=284-370.
DR PDBsum; 2DC2; -.
DR PDBsum; 2LOB; -.
DR PDBsum; 4E34; -.
DR PDBsum; 4E35; -.
DR PDBsum; 4JOE; -.
DR PDBsum; 4JOF; -.
DR PDBsum; 4JOG; -.
DR PDBsum; 4JOH; -.
DR PDBsum; 4JOJ; -.
DR PDBsum; 4JOK; -.
DR PDBsum; 4JOP; -.
DR PDBsum; 4JOR; -.
DR PDBsum; 4K6Y; -.
DR PDBsum; 4K72; -.
DR PDBsum; 4K75; -.
DR PDBsum; 4K76; -.
DR PDBsum; 4K78; -.
DR PDBsum; 4NMO; -.
DR PDBsum; 4NMP; -.
DR PDBsum; 4NMQ; -.
DR PDBsum; 4NMR; -.
DR PDBsum; 4NMS; -.
DR PDBsum; 4NMT; -.
DR PDBsum; 4NMV; -.
DR PDBsum; 4Q6H; -.
DR PDBsum; 4Q6S; -.
DR PDBsum; 5IC3; -.
DR PDBsum; 5K4F; -.
DR PDBsum; 6OV7; -.
DR PDBsum; 6V84; -.
DR PDBsum; 6XNJ; -.
DR PDBsum; 7JZO; -.
DR PDBsum; 7JZP; -.
DR PDBsum; 7JZQ; -.
DR PDBsum; 7JZR; -.
DR AlphaFoldDB; Q9HD26; -.
DR BMRB; Q9HD26; -.
DR SMR; Q9HD26; -.
DR BioGRID; 121384; 285.
DR CORUM; Q9HD26; -.
DR IntAct; Q9HD26; 126.
DR MINT; Q9HD26; -.
DR STRING; 9606.ENSP00000357484; -.
DR BindingDB; Q9HD26; -.
DR ChEMBL; CHEMBL1741218; -.
DR TCDB; 8.A.24.1.10; the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family.
DR GlyGen; Q9HD26; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HD26; -.
DR MetOSite; Q9HD26; -.
DR PhosphoSitePlus; Q9HD26; -.
DR BioMuta; GOPC; -.
DR DMDM; 74762751; -.
DR EPD; Q9HD26; -.
DR jPOST; Q9HD26; -.
DR MassIVE; Q9HD26; -.
DR MaxQB; Q9HD26; -.
DR PaxDb; Q9HD26; -.
DR PeptideAtlas; Q9HD26; -.
DR PRIDE; Q9HD26; -.
DR ProteomicsDB; 81817; -. [Q9HD26-1]
DR ProteomicsDB; 81818; -. [Q9HD26-2]
DR ProteomicsDB; 81819; -. [Q9HD26-3]
DR Antibodypedia; 19468; 473 antibodies from 40 providers.
DR DNASU; 57120; -.
DR Ensembl; ENST00000052569.10; ENSP00000052569.6; ENSG00000047932.14. [Q9HD26-2]
DR Ensembl; ENST00000368498.7; ENSP00000357484.2; ENSG00000047932.14. [Q9HD26-1]
DR GeneID; 57120; -.
DR KEGG; hsa:57120; -.
DR MANE-Select; ENST00000368498.7; ENSP00000357484.2; NM_020399.4; NP_065132.1.
DR UCSC; uc003pxu.4; human. [Q9HD26-1]
DR CTD; 57120; -.
DR DisGeNET; 57120; -.
DR GeneCards; GOPC; -.
DR GeneReviews; GOPC; -.
DR HGNC; HGNC:17643; GOPC.
DR HPA; ENSG00000047932; Low tissue specificity.
DR MalaCards; GOPC; -.
DR MIM; 606845; gene.
DR neXtProt; NX_Q9HD26; -.
DR OpenTargets; ENSG00000047932; -.
DR Orphanet; 171709; Male infertility due to globozoospermia.
DR PharmGKB; PA134904944; -.
DR VEuPathDB; HostDB:ENSG00000047932; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000156535; -.
DR HOGENOM; CLU_045744_0_0_1; -.
DR InParanoid; Q9HD26; -.
DR OMA; QCNLRQE; -.
DR OrthoDB; 1038418at2759; -.
DR PhylomeDB; Q9HD26; -.
DR TreeFam; TF317932; -.
DR PathwayCommons; Q9HD26; -.
DR Reactome; R-HSA-5627083; RHO GTPases regulate CFTR trafficking.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR SignaLink; Q9HD26; -.
DR SIGNOR; Q9HD26; -.
DR BioGRID-ORCS; 57120; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; GOPC; human.
DR EvolutionaryTrace; Q9HD26; -.
DR GeneWiki; GOPC; -.
DR GenomeRNAi; 57120; -.
DR Pharos; Q9HD26; Tbio.
DR PRO; PR:Q9HD26; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9HD26; protein.
DR Bgee; ENSG00000047932; Expressed in tibia and 194 other tissues.
DR ExpressionAtlas; Q9HD26; baseline and differential.
DR Genevisible; Q9HD26; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0045176; P:apical protein localization; NAS:UniProtKB.
DR GO; GO:0043004; P:cytoplasmic sequestering of CFTR protein; IMP:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; NAS:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; NAS:UniProtKB.
DR GO; GO:0010360; P:negative regulation of anion channel activity; IMP:UniProtKB.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR DisProt; DP02150; -.
DR Gene3D; 2.30.42.10; -; 1.
DR IDEAL; IID00520; -.
DR InterPro; IPR038879; GOPC.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR16528; PTHR16528; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell projection;
KW Chromosomal rearrangement; Coiled coil; Cytoplasm; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..462
FT /note="Golgi-associated PDZ and coiled-coil motif-
FT containing protein"
FT /id="PRO_0000087542"
FT DOMAIN 288..371
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 426..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 83..200
FT /evidence="ECO:0000255"
FT SITE 419..420
FT /note="Breakpoint for translocation to form GOPC-ROS1
FT fusion protein"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT VAR_SEQ 150..157
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11384996,
FT ECO:0000303|PubMed:11707463, ECO:0000303|PubMed:15489334"
FT /id="VSP_016062"
FT VAR_SEQ 305..319
FT /note="GGKEHGVPILISEIH -> VRSSTSSIIFYSYLV (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_016063"
FT VAR_SEQ 320..462
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_016064"
FT MUTAGEN 175
FT /note="L->V: No effect on subcellular location; when
FT associated with V-182; V-189 and V-196."
FT /evidence="ECO:0000269|PubMed:11384996"
FT MUTAGEN 182
FT /note="L->V: No effect on subcellular location; when
FT associated with V-175; V-189 and V-196."
FT /evidence="ECO:0000269|PubMed:11384996"
FT MUTAGEN 189
FT /note="L->V: No effect on subcellular location; when
FT associated with V-175; V-182 and V-196."
FT /evidence="ECO:0000269|PubMed:11384996"
FT MUTAGEN 196
FT /note="L->V: No effect on subcellular location; when
FT associated with V-175; V-182 and V-189."
FT /evidence="ECO:0000269|PubMed:11384996"
FT MUTAGEN 216..404
FT /note="Missing: Abolishes interaction with MARCHF2."
FT /evidence="ECO:0000269|PubMed:23818989"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:4JOK"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:4NMO"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:4JOK"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:4JOK"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:4JOK"
FT HELIX 323..327
FT /evidence="ECO:0007829|PDB:4JOK"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:4JOK"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2DC2"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:2LOB"
FT HELIX 349..357
FT /evidence="ECO:0007829|PDB:4JOK"
FT STRAND 361..369
FT /evidence="ECO:0007829|PDB:4JOK"
SQ SEQUENCE 462 AA; 50520 MW; 8A19DDC376DCD0F4 CRC64;
MSAGGPCPAA AGGGPGGASC SVGAPGGVSM FRWLEVLEKE FDKAFVDVDL LLGEIDPDQA
DITYEGRQKM TSLSSCFAQL CHKAQSVSQI NHKLEAQLVD LKSELTETQA EKVVLEKEVH
DQLLQLHSIQ LQLHAKTGQS ADSGTIKAKL SGPSVEELER ELEANKKEKM KEAQLEAEVK
LLRKENEALR RHIAVLQAEV YGARLAAKYL DKELAGRVQQ IQLLGRDMKG PAHDKLWNQL
EAEIHLHRHK TVIRACRGRN DLKRPMQAPP GHDQDSLKKS QGVGPIRKVL LLKEDHEGLG
ISITGGKEHG VPILISEIHP GQPADRCGGL HVGDAILAVN GVNLRDTKHK EAVTILSQQR
GEIEFEVVYV APEVDSDDEN VEYEDESGHR YRLYLDELEG GGNPGASCKD TSGEIKVLQG
FNKKAVTDTH ENGDLGTASE TPLDDGASKL DDLHTLYHKK SY
