ID   A0A1L0BYK8_9ASCO        Unreviewed;       189 AA.
AC   A0A1L0BYK8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Coatomer subunit zeta {ECO:0000256|RuleBase:RU366053};
GN   ORFNames=SAMEA4029009_CIC11G00000002774 {ECO:0000313|EMBL:SGZ56417.1},
GN   SAMEA4029010_CIC11G00000004918 {ECO:0000313|EMBL:SGZ57682.1};
OS   [Candida] intermedia.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ56417.1, ECO:0000313|Proteomes:UP000182259};
RN   [1] {ECO:0000313|Proteomes:UP000182259, ECO:0000313|Proteomes:UP000182334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ57682.1,
RC   ECO:0000313|Proteomes:UP000182334}, and PYCC 4715
RC   {ECO:0000313|EMBL:SGZ56417.1, ECO:0000313|Proteomes:UP000182259};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|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; LT635767; SGZ56417.1; -; Genomic_DNA.
DR   EMBL; LT635761; SGZ57682.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L0BYK8; -.
DR   STRING; 45354.A0A1L0BYK8; -.
DR   OrthoDB; 7466at2759; -.
DR   Proteomes; UP000182259; Chromosome iv.
DR   Proteomes; UP000182334; Chromosome vi.
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   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:UP000182334};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366053}.
FT   DOMAIN          10..149
FT                   /note="AP complex mu/sigma subunit"
FT                   /evidence="ECO:0000259|Pfam:PF01217"
SQ   SEQUENCE   189 AA;  21170 MW;  B02112CF48450AD4 CRC64;
     MSLNLSLYTI SAALVLGNEG KRLYAKYYRT QDDSQVYKTT QQQEAFEKAI YSKINKLNQD
     VILYDNHLIT YKQTNDVTLV IVGAINENES MLYSLTSNIN EALTILLDNS LDKSTVLEKY
     DMVCLCFDEA IDDGVVLEID TAIIVSRVTN PPSSSSLPND LHIDISEKGL FNALSFASKK
     ISERLQQGL
//