ID C6SYI1_SOYBN Unreviewed; 178 AA.
AC C6SYI1;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Coatomer subunit zeta {ECO:0000256|RuleBase:RU366053};
GN Name=547467 {ECO:0000313|EnsemblPlants:KRH11719};
GN ORFNames=GLYMA_15G125800 {ECO:0000313|EMBL:KRH11719.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:ACU14304.1};
RN [1] {ECO:0000313|EMBL:ACU14304.1}
RP NUCLEOTIDE SEQUENCE.
RA Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRH11719.1, ECO:0000313|EnsemblPlants:KRH11719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH11719};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH11719.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [3] {ECO:0000313|EnsemblPlants:KRH11719}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH11719};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KRH11719.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH11719.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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). The zeta subunit may be involved in regulating the
CC coat assembly and, hence, the rate of biosynthetic protein transport
CC due to its association-dissociation properties with the coatomer
CC complex. {ECO:0000256|ARBA:ARBA00025623}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC {ECO:0000256|ARBA:ARBA00011775, ECO:0000256|RuleBase:RU366053}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU366053}. Golgi
CC apparatus membrane {ECO:0000256|RuleBase:RU366053}; Peripheral membrane
CC protein {ECO:0000256|RuleBase:RU366053}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU366053}. Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000256|RuleBase:RU366053}; Peripheral membrane
CC protein {ECO:0000256|RuleBase:RU366053}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU366053}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC {ECO:0000256|ARBA:ARBA00006972, ECO:0000256|RuleBase:RU366053}.
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DR EMBL; BT090229; ACU14304.1; -; mRNA.
DR EMBL; CM000848; KRH11719.1; -; Genomic_DNA.
DR AlphaFoldDB; C6SYI1; -.
DR EnsemblPlants; KRH11719; KRH11719; GLYMA_15G125800.
DR Gramene; KRH11719; KRH11719; GLYMA_15G125800.
DR Proteomes; UP000008827; Chromosome 15.
DR ExpressionAtlas; C6SYI1; baseline and differential.
DR GO; GO:0030126; C:COPI vesicle coat; IEA:UniProtKB-UniRule.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:UniProtKB-UniRule.
DR CDD; cd14829; Zeta-COP; 1.
DR Gene3D; 3.30.450.60; -; 1.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR039652; Coatomer_zeta.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR PANTHER; PTHR11043:SF0; COATOMER SUBUNIT ZETA; 1.
DR PANTHER; PTHR11043; ZETA-COAT PROTEIN; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|RuleBase:RU366053};
KW Cytoplasmic vesicle {ECO:0000256|RuleBase:RU366053};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU366053};
KW Golgi apparatus {ECO:0000256|RuleBase:RU366053};
KW Membrane {ECO:0000256|RuleBase:RU366053};
KW Protein transport {ECO:0000256|RuleBase:RU366053};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366053}.
FT DOMAIN 9..146
FT /note="AP complex mu/sigma subunit"
FT /evidence="ECO:0000259|Pfam:PF01217"
SQ SEQUENCE 178 AA; 19719 MW; 391AEE692313003A CRC64;
MSHETCPSVK NVLLLDSDGK RVAVKYFSED WPTNSAKENF EKVVFNKTQK TNARTEEIAM
FENNIVLYKF VQDLHFFVTG GDYENELILA TVLQAFFDSV GLLLRGNVDK KEALENLDLI
LLCIDEIVDG GIILETDPNV IAGKVASNSI DSGAPLSEQT LSQALATARE HLARSLLK
//
