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Coatomer subunit delta

 C7GYF4_YEAS2            Unreviewed;       546 AA.
C7GYF4;
13-OCT-2009, integrated into UniProtKB/TrEMBL.
13-OCT-2009, sequence version 1.
22-NOV-2017, entry version 48.
RecName: Full=Coatomer subunit delta {ECO:0000256|RuleBase:RU364018};
Name=RET2 {ECO:0000313|EMBL:EEU04184.1};
ORFNames=C1Q_05582 {ECO:0000313|EMBL:EEU04184.1};
Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=574961 {ECO:0000313|EMBL:EEU04184.1, ECO:0000313|Proteomes:UP000008073};
[1] {ECO:0000313|EMBL:EEU04184.1, ECO:0000313|Proteomes:UP000008073}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=JAY291 {ECO:0000313|EMBL:EEU04184.1,
ECO:0000313|Proteomes:UP000008073};
PubMed=19812109; DOI=10.1101/gr.091777.109;
Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M.,
Netto O.V., Missawa S.K., Galzerani F., Costa G.G., Vidal R.O.,
Noronha M.F., Dominska M., Andrietta M.G., Andrietta S.R., Cunha A.F.,
Gomes L.H., Tavares F.C., Alcarde A.R., Dietrich F.S., McCusker J.H.,
Petes T.D., Pereira G.A.;
"Genome structure of a Saccharomyces cerevisiae strain widely used in
bioethanol production.";
Genome Res. 19:2258-2270(2009).
-!- 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.
{ECO:0000256|RuleBase:RU364018}.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits.
{ECO:0000256|RuleBase:RU364018}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364018}.
Cytoplasmic vesicle, COPI-coated vesicle membrane
{ECO:0000256|RuleBase:RU364018}; Peripheral membrane protein
{ECO:0000256|RuleBase:RU364018}; Cytoplasmic side
{ECO:0000256|RuleBase:RU364018}. Golgi apparatus membrane
{ECO:0000256|RuleBase:RU364018}; Peripheral membrane protein
{ECO:0000256|RuleBase:RU364018}; Cytoplasmic side
{ECO:0000256|RuleBase:RU364018}.
-!- SIMILARITY: Belongs to the adaptor complexes medium subunit
family. Delta-COP subfamily. {ECO:0000256|RuleBase:RU364018}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EEU04184.1}.
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EMBL; ACFL01000453; EEU04184.1; -; Genomic_DNA.
ProteinModelPortal; C7GYF4; -.
SMR; C7GYF4; -.
OrthoDB; EOG092C50I9; -.
Proteomes; UP000008073; Unassembled WGS sequence.
GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IEA:InterPro.
InterPro; IPR036168; AP2_Mu_C_sf.
InterPro; IPR022775; AP_mu_sigma_su.
InterPro; IPR027059; Coatomer_dsu.
InterPro; IPR011012; Longin-like_dom_sf.
InterPro; IPR028565; MHD.
PANTHER; PTHR10121; PTHR10121; 1.
Pfam; PF01217; Clat_adaptor_s; 1.
SUPFAM; SSF49447; SSF49447; 1.
SUPFAM; SSF64356; SSF64356; 1.
PROSITE; PS51072; MHD; 1.
3: Inferred from homology;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000008073};
Cytoplasm {ECO:0000256|RuleBase:RU364018};
Cytoplasmic vesicle {ECO:0000256|RuleBase:RU364018};
ER-Golgi transport {ECO:0000256|RuleBase:RU364018};
Golgi apparatus {ECO:0000256|RuleBase:RU364018};
Membrane {ECO:0000256|RuleBase:RU364018};
Protein transport {ECO:0000256|RuleBase:RU364018,
ECO:0000256|SAAS:SAAS00017283};
Transport {ECO:0000256|RuleBase:RU364018,
ECO:0000256|SAAS:SAAS00017283}.
DOMAIN 288 546 MHD. {ECO:0000259|PROSITE:PS51072}.
COILED 138 175 {ECO:0000256|SAM:Coils}.
SEQUENCE 546 AA; 60628 MW; AA730F046655EE5A CRC64;
MVVLAASITT RQGKPLLSRQ FKDLSKDRVL ELLSNFQNLV SEISSDHTFV EDKHVRYVYR
PFDNYYIILI TNRQSNIIKD LATLNLFSQT INSYLSSFQD QEIFHNAFEI LSSFDEIVSM
GGYKENLSFT QVQTYLSMES HEERIQEIIE RNKEIEATEE RKRRAKEIAR KEHERKHGFM
SSNGDYDGAN RFMGSKDPNV TNAINSYYSH ASPAAQQSYL QSSHAAAAEV APVASPMATS
QRAGHSATGG MKLGGGAGRR AGAAPRPSAI SSASSGTPPP PEEDVPENNG ILISIKEVIN
AEFSRDGTIH SSELKGVLEL RINDHDLSHS NLKLADSIDV RDKSFQFKTH PNIDKQSFLS
TKLISLRDKS KAFPANDQSL GVLRWRKVAP AEDDSLIPLT LTTWVSPSES QQGFDVIIEY
ESVLETELAD VIFTIPVFPQ EPVDINTESS TCSDAEVVNM DQEMGTSIKI SKIAANDAGA
LAFTIEAPYE DALYPMTVSF QESTRDKLAK SFTGMAIQSV VMANDHDQEL PYDVITSLKS
DEYLVQ


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