COPZ1_BOVIN
ID COPZ1_BOVIN Reviewed; 177 AA.
AC P35604; Q5EA44;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Coatomer subunit zeta-1;
DE AltName: Full=Zeta-1-coat protein;
DE Short=Zeta-1 COP;
GN Name=COPZ1; Synonyms=COPZ;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 55-70; 113-129 AND
RP 146-160.
RC TISSUE=Liver;
RX PubMed=8276893; DOI=10.1083/jcb.123.6.1727;
RA Kuge O., Hara-Kuge S., Orci L., Ravazzola M., Amherdt M., Tanigawa G.,
RA Wieland F.T., Rothman J.E.;
RT "Zeta-COP, a subunit of coatomer, is required for COP-coated vesicle
RT assembly.";
RL J. Cell Biol. 123:1727-1734(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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 (By similarity). {ECO:0000250|UniProtKB:P53600}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC originating from it. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC {ECO:0000305}.
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DR EMBL; X75935; CAA53539.1; -; mRNA.
DR EMBL; BT020662; AAX08679.1; -; mRNA.
DR EMBL; BT020725; AAX08742.1; -; mRNA.
DR EMBL; BC102358; AAI02359.1; -; mRNA.
DR PIR; A49465; A49465.
DR RefSeq; NP_776707.2; NM_174282.3.
DR PDB; 3TJZ; X-ray; 2.90 A; C/F=1-153.
DR PDBsum; 3TJZ; -.
DR AlphaFoldDB; P35604; -.
DR BMRB; P35604; -.
DR SMR; P35604; -.
DR IntAct; P35604; 1.
DR STRING; 9913.ENSBTAP00000007088; -.
DR PaxDb; P35604; -.
DR PeptideAtlas; P35604; -.
DR PRIDE; P35604; -.
DR Ensembl; ENSBTAT00000007088; ENSBTAP00000007088; ENSBTAG00000005384.
DR GeneID; 281707; -.
DR KEGG; bta:281707; -.
DR CTD; 22818; -.
DR VEuPathDB; HostDB:ENSBTAG00000005384; -.
DR VGNC; VGNC:27607; COPZ1.
DR eggNOG; KOG3343; Eukaryota.
DR GeneTree; ENSGT00390000004405; -.
DR HOGENOM; CLU_086803_2_0_1; -.
DR InParanoid; P35604; -.
DR OMA; NEQTIMS; -.
DR OrthoDB; 1522668at2759; -.
DR TreeFam; TF300262; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000005384; Expressed in saliva-secreting gland and 105 other tissues.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB.
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 GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR000804; Clathrin_sm-chain_CS.
DR InterPro; IPR039652; Coatomer_zeta.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR PANTHER; PTHR11043; PTHR11043; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00989; CLAT_ADAPTOR_S; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; ER-Golgi transport; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..177
FT /note="Coatomer subunit zeta-1"
FT /id="PRO_0000193824"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61923"
FT CONFLICT 7
FT /note="E -> Q (in Ref. 1; CAA53539)"
FT /evidence="ECO:0000305"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:3TJZ"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3TJZ"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:3TJZ"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:3TJZ"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:3TJZ"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 87..105
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:3TJZ"
SQ SEQUENCE 177 AA; 20228 MW; D410249532C8BAF8 CRC64;
MEALILEPSL YTVKAILILD NDGDRLFAKY YDDTYPSVKE QKAFEKNIFN KTHRTDSEIA
LLEGLTVVYK SSIDLYFYVI GSSYENELML MTVLNCLFDS LSQMLRKNVE KRALLENMEG
LFLAVDEIVD GGVILESDPQ QVVHRVALRG EDVPLTEQTV SQVLQSAKEQ IKWSLLR
