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Coatomer subunit gamma-1 (Gamma-1-coat protein) (Gamma-1-COP)

 COPG1_MOUSE             Reviewed;         874 AA.
Q9QZE5; Q3U9F4; Q8BP96; Q8R1A7; Q922C6;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-DEC-2017, entry version 130.
RecName: Full=Coatomer subunit gamma-1;
AltName: Full=Gamma-1-coat protein;
Short=Gamma-1-COP;
Name=Copg1; Synonyms=Copg;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11018518; DOI=10.1016/S0014-5793(00)02033-0;
Hahn Y., Lee Y.J., Yun J.H., Yang S.K., Park C.W., Mita K., Huh T.-L.,
Rhee M., Chung J.H.;
"Duplication of genes encoding non-clathrin coat protein gamma-COP in
vertebrate, insect and plant evolution.";
FEBS Lett. 482:31-36(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Bone marrow, Embryo, Kidney, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor, and Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION.
PubMed=17360540; DOI=10.1073/pnas.0611360104;
Moelleken J., Malsam J., Betts M.J., Movafeghi A., Reckmann I.,
Meissner I., Hellwig A., Russell R.B., Sollner T., Brugger B.,
Wieland F.T.;
"Differential localization of coatomer complex isoforms within the
Golgi apparatus.";
Proc. Natl. Acad. Sci. U.S.A. 104:4425-4430(2007).
[5]
FUNCTION.
PubMed=19067489; DOI=10.1371/journal.pbio.0060292;
Beller M., Sztalryd C., Southall N., Bell M., Jackle H., Auld D.S.,
Oliver B.;
"COPI complex is a regulator of lipid homeostasis.";
PLoS Biol. 6:E292-E292(2008).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. In mammals, the coatomer
can only be recruited by membranes associated to ADP-ribosylation
factors (ARFs), which are small GTP-binding proteins; the complex
also influences the Golgi structural integrity, as well as the
processing, activity, and endocytic recycling of LDL receptors (By
similarity). Required for limiting lipid storage in lipid
droplets. Involved in lipid homeostasis by regulating the presence
of perilipin family members PLIN2 and PLIN3 at the lipid droplet
surface and promoting the association of adipocyte triglyceride
lipase (PNPLA2) with the lipid droplet surface to mediate
lipolysis. {ECO:0000250, ECO:0000269|PubMed:19067489}.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits. Interacts
with ZNF289/ARFGAP2 through its C-terminal appendage domain (By
similarity). Interacts with EGFR upon EGF treatment; interaction
is essential for regulation of EGF-dependent nuclear transport of
EGFR by retrograde trafficking from the Golgi to the ER (By
similarity). Interacts with COPB1 (By similarity). Interacts with
TMED10 (via C-terminus). Interacts with TMED2, TMED3, TMED7 and
TMED9 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:17360540}. Golgi apparatus membrane
{ECO:0000269|PubMed:17360540}; Peripheral membrane protein
{ECO:0000269|PubMed:17360540}; Cytoplasmic side
{ECO:0000269|PubMed:17360540}. Cytoplasmic vesicle, COPI-coated
vesicle membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer
is cytoplasmic or polymerized on the cytoplasmic side of the
Golgi, as well as on the vesicles/buds originating from it.
Predominantly located in the cis-Golgi apparatus. {ECO:0000250}.
-!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC36811.1; Type=Frameshift; Positions=864; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF187079; AAF01325.1; -; mRNA.
EMBL; AK049417; BAC33743.1; -; mRNA.
EMBL; AK077461; BAC36811.1; ALT_FRAME; mRNA.
EMBL; AK147895; BAE28212.1; -; mRNA.
EMBL; AK151284; BAE30269.1; -; mRNA.
EMBL; AK151816; BAE30713.1; -; mRNA.
EMBL; AK153142; BAE31753.1; -; mRNA.
EMBL; AK164280; BAE37716.1; -; mRNA.
EMBL; AK169256; BAE41019.1; -; mRNA.
EMBL; AK171950; BAE42743.1; -; mRNA.
EMBL; AK172519; BAE43046.1; -; mRNA.
EMBL; BC008553; AAH08553.1; -; mRNA.
EMBL; BC024686; AAH24686.1; -; mRNA.
EMBL; BC024896; AAH24896.1; -; mRNA.
CCDS; CCDS39549.1; -.
RefSeq; NP_059505.1; NM_017477.2.
UniGene; Mm.258785; -.
PDB; 5A1U; EM; 13.00 A; E=1-874.
PDB; 5A1V; EM; 21.00 A; E/M/V=1-874.
PDB; 5A1W; EM; 18.00 A; E=1-874.
PDB; 5A1X; EM; 23.00 A; E/M=1-874.
PDB; 5A1Y; EM; 21.00 A; E/M/V=1-874.
PDB; 5NZR; EM; 9.20 A; G/K=1-874.
PDB; 5NZS; EM; 10.10 A; G/K=1-874.
PDB; 5NZT; EM; 17.00 A; G/K=1-874.
PDB; 5NZU; EM; 15.00 A; G/K=1-874.
PDB; 5NZV; EM; 17.30 A; G/K/Q=1-874.
PDBsum; 5A1U; -.
PDBsum; 5A1V; -.
PDBsum; 5A1W; -.
PDBsum; 5A1X; -.
PDBsum; 5A1Y; -.
PDBsum; 5NZR; -.
PDBsum; 5NZS; -.
PDBsum; 5NZT; -.
PDBsum; 5NZU; -.
PDBsum; 5NZV; -.
ProteinModelPortal; Q9QZE5; -.
SMR; Q9QZE5; -.
BioGrid; 207587; 2.
CORUM; Q9QZE5; -.
IntAct; Q9QZE5; 1.
MINT; MINT-1865908; -.
STRING; 10090.ENSMUSP00000109237; -.
iPTMnet; Q9QZE5; -.
PhosphoSitePlus; Q9QZE5; -.
SwissPalm; Q9QZE5; -.
EPD; Q9QZE5; -.
MaxQB; Q9QZE5; -.
PaxDb; Q9QZE5; -.
PeptideAtlas; Q9QZE5; -.
PRIDE; Q9QZE5; -.
Ensembl; ENSMUST00000113607; ENSMUSP00000109237; ENSMUSG00000030058.
GeneID; 54161; -.
KEGG; mmu:54161; -.
UCSC; uc009cug.1; mouse.
CTD; 22820; -.
MGI; MGI:1858696; Copg1.
eggNOG; KOG1078; Eukaryota.
eggNOG; COG5240; LUCA.
GeneTree; ENSGT00390000016313; -.
HOGENOM; HOG000184434; -.
HOVERGEN; HBG004368; -.
InParanoid; Q9QZE5; -.
KO; K17267; -.
OMA; SPYAVCM; -.
OrthoDB; EOG091G0HWQ; -.
PhylomeDB; Q9QZE5; -.
TreeFam; TF300324; -.
Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
ChiTaRS; Copg1; mouse.
PRO; PR:Q9QZE5; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030058; -.
CleanEx; MM_COPG; -.
ExpressionAtlas; Q9QZE5; baseline and differential.
Genevisible; Q9QZE5; MM.
GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 2.60.40.1480; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR013041; Clathrin_app_Ig-like_sf.
InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
InterPro; IPR032154; Coatomer_g_Cpla.
InterPro; IPR017106; Coatomer_gsu.
InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
InterPro; IPR037067; Coatomer_gsu_app_sf.
PANTHER; PTHR10261; PTHR10261; 1.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF16381; Coatomer_g_Cpla; 1.
Pfam; PF08752; COP-gamma_platf; 1.
PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49348; SSF49348; 1.
SUPFAM; SSF55711; SSF55711; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
Protein transport; Reference proteome; Repeat; Transport.
CHAIN 1 874 Coatomer subunit gamma-1.
/FTId=PRO_0000304939.
REPEAT 64 101 HEAT 1.
REPEAT 283 320 HEAT 2.
REPEAT 322 355 HEAT 3.
REPEAT 356 392 HEAT 4.
REGION 609 874 Interaction with ZNF289/ARFGAP2.
{ECO:0000250}.
MOD_RES 594 594 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Y678}.
CONFLICT 811 811 H -> P (in Ref. 3; AAH24896).
{ECO:0000305}.
CONFLICT 841 841 L -> F (in Ref. 2; BAE31753/BAE30713/
BAE30269). {ECO:0000305}.
CONFLICT 843 843 R -> H (in Ref. 2; BAC36811).
{ECO:0000305}.
SEQUENCE 874 AA; 97513 MW; CAF3201AD1118728 CRC64;
MLKKFDKKDE ESGGGSNPLQ HLEKSAVLQE ARVFNETPIN PRKCAHILTK ILYLINQGEH
LGTTEATEAF FAMTKLFQSN DPTLRRMCYL TIKEMSCIAE DVIIVTSSLT KDMTGKEDNY
RGPAVRALCQ ITDSTMLQAV ERYMKQAIVD KVPSVSSSAL VSSLHLLKCS FDVVKRWVNE
AQEAASSDNI MVQYHALGLL YHVRKNDRLA VSKMISKFTR HGLKSPFAYC MMIRVASKQL
EEEDGSRDSP LFDFIESCLR NKHEMVVYEA ASAIVNLPGC SAKELAPAVS VLQLFCSSPK
AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLVTDSNRSI ATLAITTLLK TGSESSIDRL
MKQISSFMSE ISDEFKVVVV QAISALCQKY PRKHAVLMNF LFTMLREEGG FEYKRAIVDC
IISIIEENSE SKETGLSHLC EFIEDCEFTV LATRILHLLG QEGPKTNNPS KYIRFIYNRV
VLEHEEVRAG AVSALAKFGA QNEEMLPSIL VLLKRCVMDD DNEVRDRATF YLNVLEQKQK
ALNAGYILNG LTVSIPGLEK ALQQYTLEPS EKPFDLKSVP LATTPMAEQR PESTATAAVK
QPEKVAATRQ EIFQEQLAAV PEFQGLGPLF KSSPEPVALT ESETEYVIRC TKHTFSDHLV
FQFDCTNTLN DQTLENVTVQ MEPTEAYEVL SYVPARSLPY NQPGTCYTLV ALPTEDPTAV
ACTFSCVMKF TVKDCDPNTG EIDEEGYEDE YVLEDLEVTV ADHIQKVMKV NFEAAWDEVG
DEFEKEETFT LSTIKTLEEA VGNIVKFLGM HPCERSDKVP ENKNTHTLLL AGVFRGGHDI
LVRSRLLLLD TVTMQVTARS SEELPVDIIL ASVG


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