ID A0A0R3RYX7_9BILA Unreviewed; 165 AA.
AC A0A0R3RYX7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Coatomer subunit zeta {ECO:0000256|RuleBase:RU366053};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000750201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000750201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- FUNCTION: The zeta subunit may be involved in regulating the coat
CC assembly and, hence, the rate of biosynthetic protein transport due to
CC its association-dissociation properties with the coatomer complex.
CC {ECO:0000256|RuleBase:RU366053}.
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|ARBA:ARBA00004255,
CC ECO:0000256|RuleBase:RU366053}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|RuleBase:RU366053};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255,
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 AlphaFoldDB; A0A0R3RYX7; -.
DR STRING; 1147741.A0A0R3RYX7; -.
DR WBParaSite; EEL_0000750201-mRNA-1; EEL_0000750201-mRNA-1; EEL_0000750201.
DR Proteomes; UP000050640; Unplaced.
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 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|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU366053};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366053}.
FT DOMAIN 7..144
FT /note="AP complex mu/sigma subunit"
FT /evidence="ECO:0000259|Pfam:PF01217"
SQ SEQUENCE 165 AA; 18409 MW; 94C8CF7CE054F6A0 CRC64;
MTSLYSIKGI AVLDQDGNRI LAKYYDDKVF PSAKEQKAFE KSLFQKTCKA NAEIILLDGM
ICVYRSNVDL FFYVMGGADE NELILVSALN CLYDSISLVL RKNVEKKALI DDMDIAMLII
DEICDNGVLM ETEPQAVVSH CALRTDELTF GDQSISQVGM SVRMS
//