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Database: UniProt
Entry: Q9MAZ7_SOLLC
LinkDB: Q9MAZ7_SOLLC
Original site: Q9MAZ7_SOLLC 
ID   Q9MAZ7_SOLLC            Unreviewed;       184 AA.
AC   Q9MAZ7;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Coatomer subunit zeta {ECO:0000256|RuleBase:RU366053};
GN   Name=copz1 {ECO:0000313|EMBL:BAA92781.1};
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081 {ECO:0000313|EMBL:BAA92781.1};
RN   [1] {ECO:0000313|EMBL:BAA92781.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Hahn Y., Chung J.H.;
RT   "Identification of zeta-COP genes from various organisms.";
RL   Submitted (MAR-2000) 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}.
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; AB040042; BAA92781.1; -; mRNA.
DR   RefSeq; NP_001233898.1; NM_001246969.1.
DR   AlphaFoldDB; Q9MAZ7; -.
DR   GeneID; 543512; -.
DR   KEGG; sly:543512; -.
DR   eggNOG; KOG3343; Eukaryota.
DR   HOGENOM; CLU_086803_1_1_1; -.
DR   OrthoDB; 7466at2759; -.
DR   PhylomeDB; Q9MAZ7; -.
DR   ExpressionAtlas; Q9MAZ7; 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:SF28; COATOMER SUBUNIT ZETA-2; 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|RuleBase:RU366053};
KW   Golgi apparatus {ECO:0000256|RuleBase:RU366053};
KW   Membrane {ECO:0000256|RuleBase:RU366053};
KW   Protein transport {ECO:0000256|RuleBase:RU366053};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366053}.
FT   DOMAIN          14..155
FT                   /note="AP complex mu/sigma subunit"
FT                   /evidence="ECO:0000259|Pfam:PF01217"
SQ   SEQUENCE   184 AA;  20535 MW;  851560EA2C353AFF CRC64;
     MAGFLLNYDS CPVVKNILLL DSEGKRVAVK YYSDDWPTNN AKVAFEKSIF TKTQKTNART
     EAEITMFENN IIVYKFVQDL HFFVTGGDDE NELVLATVLQ GFYDAVTLLL RNNVDQREAL
     ENLDLILLCL DEIVDGGMVL ETDGNTIAGK VSSHNMDDGA PLSEQTITQA LATAREHLTR
     SLLR
//
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