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UniProtKB/Swiss-Prot entry Q9HD26


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GOPC_HUMAN
Primary accession number Q9HD26
Secondary accession numbers A6NM30 Q59FS4 Q969U8
Integrated into Swiss-Prot on November 8, 2005
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    June 10, 2008 (Entry version 61)
Name and origin of the protein
Protein name Golgi-associated PDZ and coiled-coil motif-containing protein
Synonyms PDZ protein interacting specifically with TC10
PIST
CFTR-associated ligand
Fused in glioblastoma
Gene name
Name: GOPC
Synonyms: CAL, FIG
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Brain;
DOI=10.1006/bbrc.2000.4160; PubMed=11162552 [NCBI, ExPASy, EBI, Israel, Japan]
Neudauer C.L., Joberty G., Macara I.G.;
"PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10.";
Biochem. Biophys. Res. Commun. 280:541-547(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH STX6, AND MUTAGENESIS OF LEU-175; LEU-182; LEU-189 AND LEU-196.
TISSUE=Myeloid leukemia cell;
DOI=10.1074/jbc.M104137200; PubMed=11384996 [NCBI, ExPASy, EBI, Israel, Japan]
Charest A., Lane K., McMahon K., Housman D.E.;
"Association of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6.";
J. Biol. Chem. 276:29456-29465(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, OLIGOMERIZATION, INTERACTION WITH CFTR, AND DOMAIN.
TISSUE=Lung;
DOI=10.1074/jbc.M110177200; PubMed=11707463 [NCBI, ExPASy, EBI, Israel, Japan]
Cheng J., Moyer B.D., Milewski M., Loffing J., Ikeda M., Mickle J.E., Cutting G.R., Li M., Stanton B.A., Guggino W.B.;
"A Golgi-associated PDZ domain protein modulates cystic fibrosis transmembrane regulator plasma membrane expression.";
J. Biol. Chem. 277:3520-3529(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno F.R.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH ROS1.
DOI=10.1002/gcc.10207; PubMed=12661006 [NCBI, ExPASy, EBI, Israel, Japan]
Charest A., Lane K., McMahon K., Park J., Preisinger E., Conroy H., Housman D.;
"Fusion of FIG to the receptor tyrosine kinase ROS in a glioblastoma with an interstitial del(6)(q21q21).";
Genes Chromosomes Cancer 37:58-71(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-457 AND TYR-462, AND MASS SPECTROMETRY.
TISSUE=T-cell;
DOI=10.1021/ac035352d; PubMed=15144186 [NCBI, ExPASy, EBI, Israel, Japan]
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[10]
FUNCTION.
DOI=10.1074/jbc.M308640200; PubMed=14570915 [NCBI, ExPASy, EBI, Israel, Japan]
Cheng J., Wang H., Guggino W.B.;
"Modulation of mature cystic fibrosis transmembrane regulator protein by the PDZ domain protein CAL.";
J. Biol. Chem. 279:1892-1898(2004).
[11]
INTERACTION WITH ACCN3.
DOI=10.1074/jbc.M405874200; PubMed=15317815 [NCBI, ExPASy, EBI, Israel, Japan]
Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J.;
"PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current.";
J. Biol. Chem. 279:46962-46968(2004).
[12]
INTERACTION WITH ADRB1, DOMAIN, AND FUNCTION.
DOI=10.1074/jbc.M404876200; PubMed=15358775 [NCBI, ExPASy, EBI, Israel, Japan]
He J., Bellini M., Xu J., Castleberry A.M., Hall R.A.;
"Interaction with cystic fibrosis transmembrane conductance regulator-associated ligand (CAL) inhibits beta1-adrenergic receptor surface expression.";
J. Biol. Chem. 279:50190-50196(2004).
[13]
INTERACTION WITH RHOQ.
DOI=10.1074/jbc.M410026200; PubMed=15546864 [NCBI, ExPASy, EBI, Israel, Japan]
Cheng J., Wang H., Guggino W.B.;
"Regulation of cystic fibrosis transmembrane regulator trafficking and protein expression by a Rho family small GTPase TC10.";
J. Biol. Chem. 280:3731-3739(2005).
[14]
INTERACTION WITH GOLGA3, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.M504937200; PubMed=15951434 [NCBI, ExPASy, EBI, Israel, Japan]
Hicks S.W., Machamer C.E.;
"Isoform-specific interaction of golgin-160 with the Golgi-associated protein PIST.";
J. Biol. Chem. 280:28944-28951(2005).
Comments
  • FUNCTION: Plays a role in intracellular protein trafficking and degradation. May regulate CFTR chloride currents and acid-induced ACCN3 currents by modulating cell surface expression of both channels. May also regulate the intracellular trafficking of the ADR1B receptor. May play a role in autophagy. Overexpression results in CFTR intracellular retention and degradation in the lysosomes.
  • SUBUNIT: Homooligomer. Interacts with FZD5, FZD8, GRID2, BECN1, CSPG5 and CLCN3. May interact with CACNG2 (By similarity). Interacts with STX6, CFTR, ACCN3, GOLGA3 and RHOQ.
  • INTERACTION:
    P08588:ADRB1; NbExp=1; IntAct=EBI-349832, EBI-991009;
    P13569:CFTR; NbExp=1; IntAct=EBI-349832, EBI-349854;
    P51790:CLCN3; NbExp=1; IntAct=EBI-349832, EBI-349797;
  • SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. Cell junction, synapse (By similarity). Cell junction, synapse, postsynaptic cell membrane, postsynaptic density (By similarity). Cell projection, dendrite (By similarity). Note=Enriched in synaptosomal and postsynaptic densities (PSD) fractions (By similarity). Expressed in cell bodies and dendrites of Purkinje cells (By similarity). Localized at the trans-Golgi network (TGN) of spermatids and the medulla of round spermatides (By similarity).
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ9HD26-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ9HD26-2
    Features which should be applied to build the isoform sequence: VSP_016062.
    Name3
    Isoform IDQ9HD26-3
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_016063, VSP_016064.
  • TISSUE SPECIFICITY: Ubiquitously expressed.
  • DOMAIN: The PDZ domain mediates interactions with FZD5, FZD8, ACCN3, GRID2, CLCN3 (By similarity). Mediates also interaction with CFTR and ADRB1.
  • DOMAIN: The coiled-coil region probably mediates association to membranes, targeting to the Golgi, and interactions with GOLGA3, and STX6. May also mediate interaction with RHOQ (By similarity).
  • DISEASE: A chromosomal aberration involving GOPC is found in glioblastoma multiform (GBM). An homozygous deletion in chromosome 6q21 results in expression of a GOPC-ROS1 chimeric protein which has a constitutive receptor tyrosine kinase activity.
  • SIMILARITY: Contains 1 PDZ (DHR) domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF287894; AAG00572.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY033606; AAK57733.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF450008; AAL47160.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB209385; BAD92622.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL589939; CAH70198.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z85999; CAH70198.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL589939; CAH70199.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z85999; CAH70199.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z85999; CAI43172.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL589939; CAI43172.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z85999; CAI43173.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL589939; CAI43173.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471051; EAW48205.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009553; AAH09553.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001017408.1; -.
NP_065132.1; -.
UniGene Hs.191539
3D structure databases
PDB
2DC2; NMR; -; A=278-373.[ExPASy / RCSB / EBI]
PDBsum 2DC2; -.
ModBase Q9HD26.
Protein-protein interaction databases
IntAct Q9HD26; -.
PTM databases
PhosphoSite Q9HD26; -.
Organism-specific databases
HGNC HGNC:17643; GOPC.
GeneLynx GOPC; Homo sapiens.
GenAtlas GOPC.
MIM 606845; gene. [NCBI / EBI]
PharmGKB PA134904944; -.
GeneCards Q9HD26.
Gene expression databases
ArrayExpress Q9HD26; -.
CleanEx HS_GOPC; -.
GermOnline ENSG00000047932; Homo sapiens.
Ontologies
GO
GO:0005624; Cellular component: membrane fraction (inferred from direct assay from UniProtKB).
GO:0005886; Cellular component: plasma membrane (non-traceable author statement from UniProtKB).
GO:0030140; Cellular component: trans-Golgi network transport vesicle (inferred from direct assay from UniProtKB).
GO:0042980; Molecular function: cystic fibrosis transmembrane conductance regulator binding (inferred from physical interaction from UniProtKB).
GO:0050430; Molecular function: syntaxin-6 binding (inferred from physical interaction from UniProtKB).
GO:0045176; Biological process: apical protein localization (non-traceable author statement from UniProtKB).
GO:0043004; Biological process: cytoplasmic sequestering of CFTR protein (non-traceable author statement from UniProtKB).
GO:0006888; Biological process: ER to Golgi vesicle-mediated transport (non-traceable author statement from UniProtKB).
GO:0051260; Biological process: protein homooligomerization (inferred from physical interaction from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001478; PDZ.
Graphical view of domain structure.
Pfam PF00595; PDZ; 1.
Pfam graphical view of domain structure.
SMART SM00228; PDZ; 1.
SMART graphical view of domain structure.
PROSITE PS50106; PDZ; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9HD26.
Genome annotation databases
Ensembl ENSG00000047932; Homo sapiens. [Contig view]
GeneID 57120; -.
KEGG hsa:57120; -.
Phylogenomic databases
HOGENOM Q9HD26; -.
HOVERGEN Q9HD26; -.
Other
SOURCE GOPC; Homo sapiens.
ProtoNet Q9HD26.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cell junction; Cell projection; Chromosomal rearrangement; Coiled coil; Cytoplasm; Golgi apparatus; Membrane; Phosphoprotein; Postsynaptic cell membrane; Protein transport; Synapse; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   462  462     Golgi-associated PDZ and coiled-coil motif-containing protein. PRO_0000087542
DOMAIN   288   371  84     PDZ. 
COILED   83   200  118     Potential. 
SITE   419   420  2     Breakpoint for translocation to form GOPC-ROS1 fusion protein. 
MOD_RES   457   457        Phosphotyrosine. 
MOD_RES   462   462        Phosphotyrosine. 
VAR_SEQ   150   157        Missing (in isoform 2). VSP_016062
VAR_SEQ   305   319        GGKEHGVPILISEIH -> VRSSTSSIIFYSYLV (in isoform 3). VSP_016063
VAR_SEQ   320   462        Missing (in isoform 3). VSP_016064
MUTAGEN   175   175        L->V: No effect on subcellular location; when associated with V-182; V-189 and V-196. 
MUTAGEN   182   182        L->V: No effect on subcellular location; when associated with V-175; V-189 and V-196. 
MUTAGEN   189   189        L->V: No effect on subcellular location; when associated with V-175; V-182 and V-196. 
MUTAGEN   196   196        L->V: No effect on subcellular location; when associated with V-175; V-182 and V-189. 
STRAND   286   292  7      
STRAND   295   297  3      
STRAND   301   306  6      
HELIX   307   309  3      
STRAND   311   318  8      
HELIX   323   327  5      
STRAND   332   339  8      
STRAND   342   344  3      
HELIX   349   358  10      
STRAND   361   369  9      
Sequence information
Length: 462 AA [This is the length of the unprocessed precursor] Molecular weight: 50520 Da [This is the MW of the unprocessed precursor] CRC64: 8A19DDC376DCD0F4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSAGGPCPAA AGGGPGGASC SVGAPGGVSM FRWLEVLEKE FDKAFVDVDL LLGEIDPDQA 

        70         80         90        100        110        120 
DITYEGRQKM TSLSSCFAQL CHKAQSVSQI NHKLEAQLVD LKSELTETQA EKVVLEKEVH 

       130        140        150        160        170        180 
DQLLQLHSIQ LQLHAKTGQS ADSGTIKAKL SGPSVEELER ELEANKKEKM KEAQLEAEVK 

       190        200        210        220        230        240 
LLRKENEALR RHIAVLQAEV YGARLAAKYL DKELAGRVQQ IQLLGRDMKG PAHDKLWNQL 

       250        260        270        280        290        300 
EAEIHLHRHK TVIRACRGRN DLKRPMQAPP GHDQDSLKKS QGVGPIRKVL LLKEDHEGLG 

       310        320        330        340        350        360 
ISITGGKEHG VPILISEIHP GQPADRCGGL HVGDAILAVN GVNLRDTKHK EAVTILSQQR 

       370        380        390        400        410        420 
GEIEFEVVYV APEVDSDDEN VEYEDESGHR YRLYLDELEG GGNPGASCKD TSGEIKVLQG 

       430        440        450        460 
FNKKAVTDTH ENGDLGTASE TPLDDGASKL DDLHTLYHKK SY 

Q9HD26 in FASTA format

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