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Q8I0G5 (COPG_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coatomer subunit gamma
Alternative name(s):
Gamma-coat protein
Short name=Gamma-COP
Gene names
Name:gammaCop
Synonyms:copg, gamma-Cop
ORF Names:CG1528
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length883 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Required for limiting lipid storage in lipid droplets. Involved in the expansion of luminal extracellular matrices and apical membrane during tubulogenesis. Required in the tracheal epithelium for luminal protein secretion and diametric tube growth. In salivary glands, required for deposition of O-glycans and luminal extracellular matrix assembly. Required for epidermal morphogenesis and cuticle development. Ref.7 Ref.8 Ref.9

Subunit structure

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits By similarity.

Subcellular location

Cytoplasm By similarity. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicleCOPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum. Note: The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it By similarity. Ref.8 Ref.9

Tissue specificity

Expressed in ovary, testis, testis tip, young spermatocytes, germ cells and follicle cells. Up-regulated expression within centrally to posteriorly located germarial cysts and in migrating follicle cells. Widespread expression in imaginal disks including eye-antennal disk, wing disk, third leg and haltere disk. Ref.6

Developmental stage

Expressed during spermatogenesis and at later stages of oogenesis. During embryonic and larval development, expressed ubiquitously. Starting at stage 10 embryos and lasting until the end of embryonic development, strongly expressed in the salivary glands and in cells of the presumptive proventriculus. Maternal expression abundant in early embryos. Zygotic expression commences in the epidermis and salivary glands from stage 11, initiates in the trachea at stage 13, and at early stage 15 is also detected in the foregut and hindgut tubes. Ref.6 Ref.8

Disruption phenotype

Narrow tracheal tubes and thin salivary glands with reduced tube diameter and impaired tube elongation. Fails to complete dorsal closure. Fails to efficiently secrete luminal components and assemble the luminal chitinous matrix during tracheal tube expansion. In salivary glands, fails in the luminal deposition and assembly of a distinct, transient intraluminal matrix. Disrupted endoplasmic reticulum and Golgi in embryos. Null mutants die late in embryogenesis with a poorly differentiated cuticle and denticle. Defects in cell rearrangements, in branch elongation, in tube dilation and tube fusion. Ref.8 Ref.9

Sequence similarities

Belongs to the COPG family.

Contains 6 HEAT repeats.

Ontologies

Keywords
   Biological processER-Golgi transport
Protein transport
Transport
   Cellular componentCytoplasm
Cytoplasmic vesicle
Endoplasmic reticulum
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbranch fusion, open tracheal system

Inferred from mutant phenotype Ref.9. Source: FlyBase

chitin-based embryonic cuticle biosynthetic process

Inferred from mutant phenotype Ref.9. Source: FlyBase

cytokinesis

Inferred from mutant phenotype PubMed 15380073. Source: FlyBase

extracellular matrix organization

Inferred from mutant phenotype Ref.8. Source: FlyBase

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

larval salivary gland morphogenesis

Inferred from mutant phenotype Ref.8. Source: FlyBase

lumen formation, open tracheal system

Inferred from mutant phenotype Ref.9. Source: FlyBase

neuron projection morphogenesis

Inferred from mutant phenotype PubMed 18604272. Source: FlyBase

phagocytosis, engulfment

Inferred from mutant phenotype PubMed 16336044. Source: FlyBase

protein secretion

Inferred from mutant phenotype Ref.8Ref.9. Source: FlyBase

regulation of lipid storage

Inferred from direct assay Ref.7. Source: FlyBase

regulation of tube diameter, open tracheal system

Inferred from mutant phenotype Ref.8. Source: FlyBase

   Cellular_componentCOPI vesicle coat

Inferred from electronic annotation. Source: InterPro

Golgi apparatus

Inferred from direct assay Ref.9. Source: FlyBase

cis-Golgi network

Inferred from direct assay Ref.8. Source: FlyBase

endoplasmic reticulum

Inferred from direct assay Ref.8. Source: FlyBase

   Molecular_functionstructural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: Q8I0G5-1)

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.
Note: No experimental confirmation available.
Isoform A (identifier: Q8I0G5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2-17: NYFSLTSHKKHRGHPS → GSFRREKDDEED
Note: No experimental confirmation available.
Isoform C (identifier: Q8I0G5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     2-17: NYFSLTSHKKHRGHPS → GSFRREKDDEED
     18-18: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 883883Coatomer subunit gamma
PRO_0000405327

Regions

Repeat69 – 10638HEAT 1
Repeat292 – 32938HEAT 2
Repeat331 – 36434HEAT 3
Repeat365 – 40137HEAT 4
Repeat404 – 43936HEAT 5
Repeat476 – 51338HEAT 6

Natural variations

Alternative sequence2 – 1716NYFSL…RGHPS → GSFRREKDDEED in isoform A and isoform C.
VSP_040672
Alternative sequence181Missing in isoform C.
VSP_040673

Experimental info

Sequence conflict2801A → V in AAF05719. Ref.1
Sequence conflict5461S → W in AAM29550. Ref.5
Sequence conflict7241A → T in AAM29550. Ref.5
Sequence conflict7291T → A in AAM29550. Ref.5
Sequence conflict7711I → V in AAM29550. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform B [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 7C610B0F7A39692F

FASTA88397,690
        10         20         30         40         50         60 
MNYFSLTSHK KHRGHPSAGP SNAYQNLEKT SVLQETRTFN ETPVNPRKCI HILTKILYLI 

        70         80         90        100        110        120 
NQGEQLVARE ATDCFFAMTK LFQSKDVVLR RMVYLGIKEL SSIAEDVIIV TSSLTKDMTG 

       130        140        150        160        170        180 
KEDLYRAAAI RALCSITDNT MLQAVERYMK QCIVDKNAAV SCAALVSSLR LANTAGDVVK 

       190        200        210        220        230        240 
RWANEAQEAL NSDNIMVQYH ALGLLYHIRK SDRLAVSKLV NKLTRGSLKS PYAVCMLIRI 

       250        260        270        280        290        300 
ACKLIEEEDI PSEELSDSPL FTFIESCLRH KSEMVIYEAA HAIVNLKNTN PRMLSPAFSI 

       310        320        330        340        350        360 
LQLFCSSPKA TLRFAAVRTL NKVAMTHPAA VTTCNLDLEG LITDSNRSVA TLAITTLLKT 

       370        380        390        400        410        420 
GAESSVERLM KQISTFVAEI SDEFKVVVVQ AICALCTKYP RKHTVLMNFL SGMLREEGGL 

       430        440        450        460        470        480 
EYKTSIVDTI ITIIEENADA KESGLSHLCE FIEDCEHVSL AVRILHLLGK EGPFAATPSK 

       490        500        510        520        530        540 
YIRFIYNRVI LESPIVRAAA VTAMAQFGAS CPALLSNILV LLGRCQMDPD DEVRDRATYY 

       550        560        570        580        590        600 
LSILNSERPE LYKNYIIERE NCSLALLEKS LVEHLNGDVD TRFDISIVPK AAIVKPVIAN 

       610        620        630        640        650        660 
DVMLVTSSAP RPPKITREEE SAARLAQLPG IQVLGPIHRS TAPIQLTESE TEYTVQCIKH 

       670        680        690        700        710        720 
IFGQHVVFQF DCLNTLSDQI LENVRVELTL PEGFTTRAVI PCPKLPYNDL QTTFVIVEFP 

       730        740        750        760        770        780 
PDAANSIATF GATLRFVVKD CDPNTGEPES EEGYDDEYML EDLELTVADQ IQKTRKNNFQ 

       790        800        810        820        830        840 
VSWDAADSEE WLQAEDTFVL SAVTTLQDAV NTIVKILGLG AANLSENVPE GTHLHTLLCS 

       850        860        870        880 
GTFRGGAEIL VRAKLALSEG VTLNLTVRST DQDVAELITA AIG 

« Hide

Isoform A [UniParc].

Checksum: 2D306F2ACAE8B055
Show »

FASTA87997,277
Isoform C [UniParc].

Checksum: CD358D5D6AA1B423
Show »

FASTA87897,206

References

« Hide 'large scale' references
[1]"Duplication of genes encoding non-clathrin coat protein gamma-COP in vertebrate, insect and plant evolution."
Hahn Y., Lee Y.J., Yun J.H., Yang S.K., Park C.W., Mita K., Huh T.-L., Rhee M., Chung J.H.
FEBS Lett. 482:31-36(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Larva and Pupae.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[4]"Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."
Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., Karpen G.H.
Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
Strain: Berkeley.
Tissue: Embryo.
[6]"Expression of COPI components during development of Drosophila melanogaster."
Grieder N.C., Kloter U., Gehring W.J.
Gene Expr. Patterns 6:11-21(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]"COPI complex is a regulator of lipid homeostasis."
Beller M., Sztalryd C., Southall N., Bell M., Jackle H., Auld D.S., Oliver B.
PLoS Biol. 6:E292-E292(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"COPI vesicle transport is a common requirement for tube expansion in Drosophila."
Jayaram S.A., Senti K.A., Tiklova K., Tsarouhas V., Hemphala J., Samakovlis C.
PLoS ONE 3:E1964-E1964(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[9]"gammaCOP is required for apical protein secretion and epithelial morphogenesis in Drosophila melanogaster."
Grieder N.C., Caussinus E., Parker D.S., Cadigan K., Affolter M., Luschnig S.
PLoS ONE 3:E3241-E3241(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF191563 mRNA. Translation: AAF05719.1.
AE014297 Genomic DNA. Translation: AAN14275.1.
AE014297 Genomic DNA. Translation: AAF57160.1.
AE014297 Genomic DNA. Translation: ACZ95077.1.
AY113545 mRNA. Translation: AAM29550.1.
BT001628 mRNA. Translation: AAN71383.1.
RefSeqNP_001163784.1. NM_001170313.1.
NP_524608.1. NM_079869.3.
NP_733432.1. NM_170553.2.
UniGeneDm.1895.

3D structure databases

ProteinModelPortalQ8I0G5.
SMRQ8I0G5. Positions 25-320, 525-551, 616-883.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1018880.
STRING7227.FBpp0085155.

Proteomic databases

PaxDbQ8I0G5.
PRIDEQ8I0G5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085794; FBpp0085155; FBgn0028968.
GeneID43717.
KEGGdme:Dmel_CG1528.
UCSCCG1528-RA. d. melanogaster.
CG1528-RB. d. melanogaster.

Organism-specific databases

CTD43717.
FlyBaseFBgn0028968. gammaCop.

Phylogenomic databases

eggNOGCOG5240.
GeneTreeENSGT00390000016313.
HOGENOMHOG000250272.
InParanoidQ8MYW4.
OMAWDEVGEE.
PhylomeDBQ8I0G5.

Gene expression databases

BgeeQ8I0G5.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
2.60.40.1480. 1 hit.
3.30.310.30. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR015873. Clathrin_a/coatomer_app_sub_C.
IPR009028. Coatomer/calthrin_app_sub_C.
IPR013041. Coatomer/clathrin_app_Ig-like.
IPR017106. Coatomer_gsu.
IPR014863. Coatomer_gsu_app.
IPR013040. Coatomer_gsu_app_Ig-like-sub.
[Graphical view]
PANTHERPTHR10261. PTHR10261. 1 hit.
PfamPF01602. Adaptin_N. 1 hit.
PF08752. Gamma-COP. 1 hit.
[Graphical view]
PIRSFPIRSF037093. Coatomer_gamma_subunit. 1 hit.
SUPFAMSSF55711. AP2_adap_app. 1 hit.
SSF48371. ARM-type_fold. 1 hit.
SSF49348. Clath_adapt. 1 hit.
PROSITEPS50077. HEAT_REPEAT. False negative.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi43717.
NextBio835406.

Entry information

Entry nameCOPG_DROME
AccessionPrimary (citable) accession number: Q8I0G5
Secondary accession number(s): E1JJ29 expand/collapse secondary AC list , Q8MYW4, Q9U677, Q9V9W9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: March 1, 2003
Last modified: May 29, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families