ID D8RVE6_SELML Unreviewed; 179 AA.
AC D8RVE6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Coatomer subunit zeta {ECO:0000256|RuleBase:RU366053};
GN ORFNames=SELMODRAFT_442701 {ECO:0000313|EMBL:EFJ23942.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ23942.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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; GL377591; EFJ23942.1; -; Genomic_DNA.
DR RefSeq; XP_002975157.1; XM_002975111.1.
DR AlphaFoldDB; D8RVE6; -.
DR STRING; 88036.D8RVE6; -.
DR EnsemblPlants; EFJ23942; EFJ23942; SELMODRAFT_442701.
DR GeneID; 9637850; -.
DR Gramene; EFJ23942; EFJ23942; SELMODRAFT_442701.
DR KEGG; smo:SELMODRAFT_442701; -.
DR eggNOG; KOG3343; Eukaryota.
DR HOGENOM; CLU_086803_1_1_1; -.
DR InParanoid; D8RVE6; -.
DR OMA; YDSHLAV; -.
DR OrthoDB; 7466at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
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 3: Inferred from homology;
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:UP000001514};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366053}.
FT DOMAIN 9..150
FT /note="AP complex mu/sigma subunit"
FT /evidence="ECO:0000259|Pfam:PF01217"
SQ SEQUENCE 179 AA; 20004 MW; 647CDC78A2698A0D CRC64;
MGELLDPFVS NILLLDDEGK RVAVKYYSDY WPNNAAKLAF EKSVFTKTQR MNARQEAEIG
LYEGHVVVFK FVADLYFYVT GREDENELIL ATVLQAFFDA VSILLRGNVD KKTVLENLDL
ILLCLDEIVD GGTVLETDAN SIASKVAMRG AESDVPFSEQ TFSQALATAK EHLTRSLLK
//
