Reviewed, UniProtKB/Swiss-Prot Q8BH60 (GOPC_MOUSE)

Names and origin

Protein names

Recommended name:
    Golgi-associated PDZ and coiled-coil motif-containing protein
Alternative name(s):
    PDZ protein interacting specifically with TC10
      Short name=PIST

Gene names

Name:

Gopc

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Ref.6 Ref.7 Ref.11
Subunit structure	Homooligomer. Interacts with STX6 and GOLGA3 By similarity. Interacts with ACCN3, RHOQ, FZD5, FZD8, GRID2, BECN1, CSPG5, CFTR and CLCN3. May interact with CACNG2.
Subcellular location	Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Golgi apparatus › trans-Golgi network membrane; Peripheral membrane protein. Cell junction › synapse. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density. Cell projection › dendrite. Note: Enriched in synaptosomal and postsynaptic densities (PSD) fractions. Expressed in cell bodies and dendrites of Purkinje cells. Localized at the trans-Golgi network (TGN) of spermatids and the medulla of round spermatides. Ref.6 Ref.7 Ref.11 Ref.2 Ref.9
Tissue specificity	Ubiquitously expressed (at protein level). Expressed in dorsal root glanglion (DRG), spinal chord and brain. Isoform 1 is preferentially expressed in whole brain (at protein level) and cerebellum. Expressed in spermatocytes and spermatides but not in Sertoli cells and spermatogonia. Ref.6 Ref.7 Ref.11 Ref.5
Developmental stage	In the cerebellum, expression increases post-natally, following maturation of this tissue (at protein level). Ref.6
Domain	The coiled-coil region probably mediates targeting to the Golgi, oligomerization and interaction with RHOQ. May also mediates association to membranes and interactions with GOLGA3 and STX6 By similarity. The PDZ domain mediates interaction with ADRB1 By similarity. Mediates also interactions with FZD5, FZD8, ACCN3, GRID2, CFTR, CLCN3.
Disruption phenotype	Male mice are infertile with globozoospermia. Spermatozoa display a default in acrosome formation and are unable to activate oocytes. Ref.7
Sequence similarities	Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Golgi apparatus Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	autophagy Ref.9 Traceable author statement. Source: UniProtKB protein homooligomerization Inferred from sequence or structural similarity. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW spermatid nucleus differentiation Inferred from mutant phenotype. Source: MGI
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW dendrite Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic density Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW synaptosome Ref.6 Inferred from direct assay. Source: MGI trans-Golgi network transport vesicle Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	cystic fibrosis transmembrane conductance regulator binding Inferred from sequence or structural similarity. Source: UniProtKB small GTPase regulator activity Ref.1 Inferred from direct assay. Source: MGI syntaxin-6 binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CSPG5	O95196	2	EBI-296357,EBI-296349	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8BH60-1)

Also known as: NPIST; Beta;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8BH60-2)

Also known as: Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     151-158: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 463	463	Golgi-associated PDZ and coiled-coil motif-containing protein		PRO_0000087543
Regions
	Domain	289 – 372	84	PDZ
	Coiled coil	85 – 201	117	Potential
Amino acid modifications
	Modified residue	463	1	Phosphotyrosine By similarity
Natural variations
	Alternative sequence	151 – 158	8	Missing in isoform 2.		VSP_016065

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (NPIST) (Beta) [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 47BB5760BFFB6303	FASTA	463	50,662
	10 20 30 40 50 60 MSAGGPCPAG AGGGPGGSSC PVGVSPGGVS MFRWLEVLEK EFDKAFVDVD LLLGEIDPDQ 70 80 90 100 110 120 ADITYEGRQK MTSLSSCFAQ LCHKAQTVSQ INHKLEAQLV DLRSELTETQ AEKVVLEKEV 130 140 150 160 170 180 HEQLLQLHST QLQLHAKTGQ SVDSGAIKAK LSVHSVEDLE RELEANKTEK VKEARLEAEV 190 200 210 220 230 240 KLLRKENEAL RRHIAVLQAE VYGARLAAKY LDKELAGRVQ QIQLLGRDMK GPAHDKLWNQ 250 260 270 280 290 300 LEAEIHLHRH KTVIRACRGR NDLKRPMQAP PGHDQDSLKK SQGVGPIRKV LLLKEDHEGL 310 320 330 340 350 360 GISITGGKEH GVPILISEIH PGQPADRCGG LHVGDAILAV NGVNLRDTKH KEAVTILSQQ 370 380 390 400 410 420 RGEIEFEVVY VAPEVDSDDE NVEYEDESGH RYRLYLDELE GSGNSGASCK DSSGEMKMLQ 430 440 450 460 GYNKKAVRDA HENGDVGAAG ESPLDDTAAR AAHLHSLHQK KAY
	Isoform 2 (Alpha). Checksum: C75E9F6D2C243CFB	FASTA	455	49,795
	10 20 30 40 50 60 MSAGGPCPAG AGGGPGGSSC PVGVSPGGVS MFRWLEVLEK EFDKAFVDVD LLLGEIDPDQ 70 80 90 100 110 120 ADITYEGRQK MTSLSSCFAQ LCHKAQTVSQ INHKLEAQLV DLRSELTETQ AEKVVLEKEV 130 140 150 160 170 180 HEQLLQLHST QLQLHAKTGQ SVDSGAIKAK LERELEANKT EKVKEARLEA EVKLLRKENE 190 200 210 220 230 240 ALRRHIAVLQ AEVYGARLAA KYLDKELAGR VQQIQLLGRD MKGPAHDKLW NQLEAEIHLH 250 260 270 280 290 300 RHKTVIRACR GRNDLKRPMQ APPGHDQDSL KKSQGVGPIR KVLLLKEDHE GLGISITGGK 310 320 330 340 350 360 EHGVPILISE IHPGQPADRC GGLHVGDAIL AVNGVNLRDT KHKEAVTILS QQRGEIEFEV 370 380 390 400 410 420 VYVAPEVDSD DENVEYEDES GHRYRLYLDE LEGSGNSGAS CKDSSGEMKM LQGYNKKAVR 430 440 450 DAHENGDVGA AGESPLDDTA ARAAHLHSLH QKKAY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10." Neudauer C.L., Joberty G., Macara I.G. Biochem. Biophys. Res. Commun. 280:541-547(2001) [PubMed: 11162552] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), OLIGOMERIZATION, INTERACTION WITH RHOQ. Tissue: Embryo.
[2]	"Identification of a PDZ domain containing Golgi protein, GOPC, as an interaction partner of frizzled." Yao R., Maeda T., Takada S., Noda T. Biochem. Biophys. Res. Commun. 286:771-778(2001) [PubMed: 11520064] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DOMAIN, OLIGOMERIZATION, SUBCELLULAR LOCATION, INTERACTION WITH FZD5 AND FZD8. Tissue: Kidney.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Olfactory bulb and Pituitary.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Olfactory epithelium.
[5]	"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." Charest A., Lane K., McMahon K., Housman D.E. J. Biol. Chem. 276:29456-29465(2001) [PubMed: 11384996] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"A novel protein complex linking the delta 2 glutamate receptor and autophagy: implications for neurodegeneration in lurcher mice." Yue Z., Horton A., Bravin M., DeJager P.L., Selimi F., Heintz N. Neuron 35:921-933(2002) [PubMed: 12372286] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH GRID2 AND BECN1.
[7]	"Lack of acrosome formation in mice lacking a Golgi protein, GOPC." Yao R., Ito C., Natsume Y., Sugitani Y., Yamanaka H., Kuretake S., Yanagida K., Sato A., Toshimori K., Noda T. Proc. Natl. Acad. Sci. U.S.A. 99:11211-11216(2002) [PubMed: 12149515] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, DISRUPTION PHENOTYPE.
[8]	"The PDZ-binding chloride channel ClC-3B localizes to the Golgi and associates with cystic fibrosis transmembrane conductance regulator-interacting PDZ proteins." Gentzsch M., Cui L., Mengos A., Chang X.-B., Chen J.-H., Riordan J.R. J. Biol. Chem. 278:6440-6449(2003) [PubMed: 12471024] [Abstract] Cited for: INTERACTION WITH CLCN3 AND CFTR, DOMAIN.
[9]	"CALEB/NGC interacts with the Golgi-associated protein PIST." Hassel B., Schreff M., Stuebe E.-M., Blaich U., Schumacher S. J. Biol. Chem. 278:40136-40143(2003) [PubMed: 12885772] [Abstract] Cited for: INTERACTION WITH CSPG5, SUBCELLULAR LOCATION.
[10]	"Microtubule-associated protein light chain 2 is a stargazin-AMPA receptor complex-interacting protein in vivo." Ives J.H., Fung S., Tiwari P., Payne H.L., Thompson C.L. J. Biol. Chem. 279:31002-31009(2004) [PubMed: 15136571] [Abstract] Cited for: INTERACTION WITH CACNG2.
[11]	"PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current." Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J. J. Biol. Chem. 279:46962-46968(2004) [PubMed: 15317815] [Abstract] Cited for: INTERACTION WITH ACCN3, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF287893 mRNA. Translation: AAG00571.1. AB052838 mRNA. Translation: BAB69946.1. AK030427 mRNA. Translation: BAC26958.1. AK030637 mRNA. Translation: BAC27058.1. AK032613 mRNA. Translation: BAC27951.1. BC051171 mRNA. Translation: AAH51171.1.
IPI	IPI00221745. IPI00655113.
RefSeq	NP_444417.2.
UniGene	Mm.390258
3D structure databases
HSSP	HSSP built from PDB template 2PDZ based on UniProtKB Q61234.
SMR	Q8BH60. Positions 286-372.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8BH60. 2 interactions.
STRING	Q8BH60.
PTM databases
PhosphoSite	Q8BH60.
Proteomic databases
PRIDE	Q8BH60.
Genome annotation databases
Ensembl	ENSMUST00000020008; ENSMUSP00000020008; ENSMUSG00000019861; Mus musculus. [Genome view] ENSMUST00000105475; ENSMUSP00000101115; ENSMUSG00000019861; Mus musculus. [Genome view]
GeneID	94221.
KEGG	mmu:94221.
UCSC	uc007fbf.1. mouse. uc007fbg.1. mouse.
Organism-specific databases
CTD	94221.
MGI	MGI:2149946. Gopc.
Phylogenomic databases
HOGENOM	Q8BH60.
HOVERGEN	Q8BH60.
OMA	KAVTDGH.
Gene expression databases
ArrayExpress	Q8BH60.
Bgee	Q8BH60.
Genevestigator	Q8BH60.
GermOnline	ENSMUSG00000019861. Mus musculus.
Family and domain databases
InterPro	IPR001478. PDZ/DHR/GLGF. [Graphical view]
Pfam	PF00595. PDZ. 1 hit. [Graphical view]
SMART	SM00228. PDZ. 1 hit. [Graphical view]
PROSITE	PS50106. PDZ. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	352211.
SOURCE	Search...

Entry information

Entry name

GOPC_MOUSE

Accession

Primary (citable) accession number: Q8BH60
Secondary accession number(s): Q8BSV4, Q920R1, Q9ET11

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)