Q8BH60 (GOPC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
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 ASIC3 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 NLGN1, STX6 and GOLGA3 By similarity. Interacts with ASIC3, RHOQ, FZD5, FZD8, GRID2, BECN1, CSPG5, CFTR and CLCN3. May interact with CACNG2. Ref.1 Ref.2 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11
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.2 Ref.6 Ref.7 Ref.9 Ref.11
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.5 Ref.6 Ref.7 Ref.11
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. Ref.2 Ref.6 Ref.8 The PDZ domain mediates interaction with ADRB1 By similarity. Mediates also interactions with FZD5, FZD8, ASIC3, GRID2, CFTR, CLCN3. Ref.2 Ref.6 Ref.8
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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	autophagy Traceable author statement Ref.9. 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 PubMed 16765935. Source: MGI
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell junction Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.2. Source: BHF-UCL postsynaptic density Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW protein complex Inferred from sequence orthology PubMed 18468998. Source: MGI synapse Inferred from direct assay Ref.6. Source: MGI trans-Golgi network transport vesicle Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ion channel binding Inferred from sequence or structural similarity. Source: UniProtKB small GTPase regulator activity Inferred from direct assay Ref.1. Source: MGI syntaxin binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CSPG5	O95196	3	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
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) [UniParc]. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ASIC3, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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_001186201.1. NM_001199272.1. NP_444417.2. NM_053187.3.
UniGene	Mm.390258.
3D structure databases
ProteinModelPortal	Q8BH60.
SMR	Q8BH60. Positions 286-372.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8BH60. 2 interactions.
MINT	MINT-1489410.
PTM databases
PhosphoSite	Q8BH60.
Proteomic databases
PaxDb	Q8BH60.
PRIDE	Q8BH60.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020008; ENSMUSP00000020008; ENSMUSG00000019861.
GeneID	94221.
KEGG	mmu:94221.
UCSC	uc007fbf.2. mouse. uc007fbg.2. mouse.
Organism-specific databases
CTD	57120.
MGI	MGI:2149946. Gopc.
Phylogenomic databases
eggNOG	NOG278699.
GeneTree	ENSGT00550000074582.
HOGENOM	HOG000280727.
HOVERGEN	HBG057507.
InParanoid	Q8BH60.
OrthoDB	EOG4DR9CC.
Gene expression databases
Bgee	Q8BH60.
Genevestigator	Q8BH60.
GermOnline	ENSMUSG00000019861. Mus musculus.
Family and domain databases
InterPro	IPR001478. PDZ. [Graphical view]
Pfam	PF00595. PDZ. 1 hit. [Graphical view]
SMART	SM00228. PDZ. 1 hit. [Graphical view]
SUPFAM	SSF50156. PDZ. 1 hit.
PROSITE	PS50106. PDZ. 1 hit. [Graphical view]
ProtoNet	Search...
Other
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:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program