COPG2_DANRE
ID COPG2_DANRE Reviewed; 873 AA.
AC Q9PUE4; Q1L8N9; Q4V9K1; Q7ZVC5; Q9PUE3;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Coatomer subunit gamma-2;
DE AltName: Full=Gamma-2-coat protein;
DE Short=Gamma-2-COP;
GN Name=copg2; ORFNames=si:ch211-285d14.8;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11018518; DOI=10.1016/s0014-5793(00)02033-0;
RA Hahn Y., Lee Y.J., Yun J.H., Yang S.K., Park C.W., Mita K., Huh T.-L.,
RA Rhee M., Chung J.H.;
RT "Duplication of genes encoding non-clathrin coat protein gamma-COP in
RT vertebrate, insect and plant evolution.";
RL FEBS Lett. 482:31-36(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC dilysine motifs and reversibly associates with Golgi non-clathrin-
CC coated vesicles, which further mediate biosynthetic protein transport
CC from the ER, via the Golgi up to the trans Golgi network. Coatomer
CC complex is required for budding from Golgi membranes, and is essential
CC for the retrograde Golgi-to-ER transport of dilysine-tagged proteins
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9PUE4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9PUE4-2; Sequence=VSP_034478, VSP_034479;
CC -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
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DR EMBL; AF191561; AAF05717.1; -; mRNA.
DR EMBL; AF191562; AAF05718.1; -; mRNA.
DR EMBL; CR749763; CAK04920.1; -; Genomic_DNA.
DR EMBL; BX004864; CAK04920.1; JOINED; Genomic_DNA.
DR EMBL; BX004864; CAK05111.1; -; Genomic_DNA.
DR EMBL; CR749763; CAK05111.1; JOINED; Genomic_DNA.
DR EMBL; BC045918; AAH45918.1; -; mRNA.
DR EMBL; BC096860; AAH96860.1; -; mRNA.
DR RefSeq; NP_571069.1; NM_130994.1.
DR AlphaFoldDB; Q9PUE4; -.
DR SMR; Q9PUE4; -.
DR STRING; 7955.ENSDARP00000043659; -.
DR PaxDb; Q9PUE4; -.
DR PRIDE; Q9PUE4; -.
DR Ensembl; ENSDART00000043660; ENSDARP00000043659; ENSDARG00000034823. [Q9PUE4-1]
DR GeneID; 30187; -.
DR KEGG; dre:30187; -.
DR CTD; 26958; -.
DR ZFIN; ZDB-GENE-000208-8; copg2.
DR eggNOG; KOG1078; Eukaryota.
DR GeneTree; ENSGT00390000016313; -.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; Q9PUE4; -.
DR OMA; YMTQYHA; -.
DR OrthoDB; 255234at2759; -.
DR PhylomeDB; Q9PUE4; -.
DR TreeFam; TF300324; -.
DR Reactome; R-DRE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DRE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q9PUE4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000034823; Expressed in caudal fin and 36 other tissues.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0072384; P:organelle transport along microtubule; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 2.60.40.1480; -; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR032154; Coatomer_g_Cpla.
DR InterPro; IPR017106; Coatomer_gsu.
DR InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
DR InterPro; IPR037067; Coatomer_gsu_app_sf.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR10261; PTHR10261; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF16381; Coatomer_g_Cpla; 1.
DR Pfam; PF08752; COP-gamma_platf; 1.
DR PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..873
FT /note="Coatomer subunit gamma-2"
FT /id="PRO_0000342519"
FT REPEAT 64..101
FT /note="HEAT 1"
FT REPEAT 283..320
FT /note="HEAT 2"
FT REPEAT 321..355
FT /note="HEAT 3"
FT REPEAT 356..392
FT /note="HEAT 4"
FT REPEAT 395..430
FT /note="HEAT 5"
FT REPEAT 467..504
FT /note="HEAT 6"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 296..299
FT /note="CSSP -> LLVR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_034478"
FT VAR_SEQ 300..873
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_034479"
FT CONFLICT 56
FT /note="N -> D (in Ref. 3; AAH45918)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="I -> V (in Ref. 3; AAH96860)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="M -> I (in Ref. 3; AAH96860)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="C -> F (in Ref. 1; AAF05718)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="I -> M (in Ref. 1; AAF05717/AAF05718 and 3;
FT AAH96860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 873 AA; 97529 MW; EE664350506B48FF CRC64;
MIKKFDKKDE ESGSGSNPFQ HLEKSAVLQE ARIFNETPIN PRRCLHILTK IIYLLNQGEH
FGTTEATEAF FAMTRLFQSN DQTLRRMCYL TIKEMANISE DVIIVTSSLT KDMTGKEDVY
RGPAIRALCR ITDTTMLQAI ERYMKQAIVD KVPSVSSSAL VSSLHMVKMS FDVVKRWVNE
AQEAASSDNI MVQYHALGLL YHLRKNDRLA VTKMLNKFTK SGLKSPFAYC MMIRIASKLL
EETEGGHDSP LFDFIESCLR NKHEMVVYEA ASAIVHMPNC TARELAPAVS VLQLFCSSPK
AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLITDSNRSI ATLAITTLLK TGSESSVDRL
MKQISSFVSE ISDEFKVVVV QAISALCQKY PRKHSVMMNF LSNMLRDDGG FEYKRAIVDC
IISIIEENPE SKETGLAHLC EFIEDCEHTV LATKILHLLG KEGPRTPTPS KYIRFIFNRV
VLESEAVRAA AVSALAKFGA QNDDLLPSVL VLMQRCMMDS DDEVRDRATF YMNVLQQKQK
ALNAAYIFNG LSVSVLGLEK SLHQYTLEPS EKPFDMKTVP LATAPITEHK TEIAPVATSK
LPEKLAPSRQ DIYQEQLSAI PEFQGLGPLF KSSEPVQLTE AETEYVVRCI KHTFANHMIF
QFDCTNTLND QLLQKVLVQM EPSESYEVLH YVPAANLPYS QPGSCYSLVR LPEDDPTAVS
CTFSCTMKYL VRDCDPNTGE PDDDGYDDEY VLEDLEVTVA DHIQKVLKPN FAAAWDEVGD
ECEKEETFAL ATVRTLDEAV NNIVSFLGMQ PCERSDKVPE NKNSHVLFLA GVFRGGHDVL
VRARLALADG VTIQVTVRST DDNVVDVILA SVG
