GOPC_PONAB
ID GOPC_PONAB Reviewed; 462 AA.
AC Q5RD32;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Golgi-associated PDZ and coiled-coil motif-containing protein {ECO:0000250|UniProtKB:Q9HD26};
DE AltName: Full=CFTR-associated ligand {ECO:0000250|UniProtKB:Q9HD26};
DE AltName: Full=PDZ protein interacting specifically with TC10 {ECO:0000250|UniProtKB:Q9HD26};
DE Short=PIST {ECO:0000250|UniProtKB:Q9HD26};
GN Name=GOPC; Synonyms=CAL {ECO:0000250|UniProtKB:Q9HD26};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in intracellular protein trafficking and
CC degradation (By similarity). May regulate CFTR chloride currents and
CC acid-induced ASIC3 currents by modulating cell surface expression of
CC both channels (By similarity). May also regulate the intracellular
CC trafficking of the ADR1B receptor (By similarity). May play a role in
CC autophagy (By similarity). Together with MARCHF2 mediates the
CC ubiquitination and lysosomal degradation of CFTR (By similarity).
CC Overexpression results in CFTR intracellular retention and degradation
CC in the lysosomes (By similarity). {ECO:0000250|UniProtKB:Q8BH60,
CC ECO:0000250|UniProtKB:Q9HD26}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with FZD5 (By
CC similarity). Interacts with FZD8 (By similarity). Interacts with GRID2
CC and BECN1 (By similarity). Interacts with CSPG5 (By similarity).
CC Interacts with CLCN3 (By similarity). Interacts with STX6 (By
CC similarity). Interacts with CFTR (By similarity). Interacts with ASIC3
CC (By similarity). Interacts with GOLGA3 (By similarity). Interacts with
CC NLGN1 (By similarity). Interacts with RHOQ (By similarity). Interacts
CC with MARCHF2; the interaction leads to CFTR ubiquitination and
CC degradation (By similarity). May interact with CACNG2 (By similarity).
CC {ECO:0000250|UniProtKB:Q8BH60, ECO:0000250|UniProtKB:Q9HD26}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Synapse {ECO:0000250}. Postsynaptic
CC density {ECO:0000250}. Cell projection, dendrite {ECO:0000250}.
CC Note=Enriched in synaptosomal and postsynaptic densities (PSD)
CC fractions. Expressed in cell bodies and dendrites of Purkinje cells.
CC Localized at the trans-Golgi network (TGN) of spermatids and the
CC medulla of round spermatides (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The PDZ domain mediates interactions with FZD5, FZD8, ASIC3,
CC GRID2, CFTR, CLCN3 and ADRB1. {ECO:0000250}.
CC -!- DOMAIN: The coiled-coil region probably mediates association to
CC membranes, targeting to the Golgi, and interactions with GOLGA3, RHOQ,
CC and STX6. {ECO:0000250}.
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DR EMBL; CR858086; CAH90325.1; -; mRNA.
DR RefSeq; NP_001125151.1; NM_001131679.1.
DR AlphaFoldDB; Q5RD32; -.
DR BMRB; Q5RD32; -.
DR SMR; Q5RD32; -.
DR STRING; 9601.ENSPPYP00000018990; -.
DR GeneID; 100172038; -.
DR KEGG; pon:100172038; -.
DR CTD; 57120; -.
DR eggNOG; KOG3528; Eukaryota.
DR InParanoid; Q5RD32; -.
DR OrthoDB; 1038418at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0043004; P:cytoplasmic sequestering of CFTR protein; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
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 2: Evidence at transcript level;
KW Cell projection; Coiled coil; Cytoplasm; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Synapse; Transport.
FT CHAIN 1..462
FT /note="Golgi-associated PDZ and coiled-coil motif-
FT containing protein"
FT /id="PRO_0000087544"
FT DOMAIN 288..371
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 427..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 83..194
FT /evidence="ECO:0000255"
SQ SEQUENCE 462 AA; 50417 MW; F9036C986941434E CRC64;
MAAGGPCPAA AGGGPGGASC SVGAPGGVSM FRWLEVLEKE FDKAFVDVDL LLGEIDPDQA
DITYEGRQKM TSLSSCFAQL CHKAQSVSQI NHKLEAQLVD LKSELTETQA EKVVLEKEVH
DQLLQLHSIQ LQLHAKTGQS VDSGTIKAKL SGPSVEELER ELEANKKEKM KEAQLEAEVK
LLRKEDEALR GHIAVLQAEV YGARLAAKYL DKELAGRVQQ IQLLGRDMKG PAHDKLWNQL
EAEIHLHRHK TVIRACRGRN DLKRPMQAPP GHDQDSLKKS QGVGPIRKVL LLKEDHEGLG
ISITGGKEHG VPILISEIHP GQPADRCGGL HVGDAILAVD GVNLRDTKHK EAVTVLSQQR
GEIEFEVVYV APEVDSDDEN VEYEDESGHR YRLYLDELEG GGNPGASCKD PSGEIKVLQG
FNKKAVTDTH ENGDLGTASE TPLDDGASKL DDLHTLYHKK SY
