COPD_BOVIN
ID COPD_BOVIN Reviewed; 511 AA.
AC P53619;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Coatomer subunit delta;
DE AltName: Full=Archain;
DE AltName: Full=Delta-coat protein;
DE Short=Delta-COP;
GN Name=ARCN1; Synonyms=COPD;
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] OF 2-511.
RC TISSUE=Brain;
RX PubMed=8858162; DOI=10.1083/jcb.135.1.53;
RA Faulstich D., Auerbach S., Orci L., Ravazzola M., Wegehingel S.,
RA Lottspeich F., Stenbeck G., Harter C., Wieland F.T., Tschochner H.;
RT "Architecture of coatomer: molecular characterization of delta-COP and
RT protein interactions within the complex.";
RL J. Cell Biol. 135:53-61(1996).
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 In mammals, the coatomer can only be recruited by membranes associated
CC to ADP-ribosylation factors (ARFs), which are small GTP-binding
CC proteins; the complex also influences the Golgi structural integrity,
CC as well as the processing, activity, and endocytic recycling of LDL
CC receptors (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC -!- INTERACTION:
CC P53619; P23514: Copb1; Xeno; NbExp=3; IntAct=EBI-620432, EBI-620488;
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 -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC Delta-COP subfamily. {ECO:0000305}.
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DR EMBL; X94265; CAA63941.1; -; mRNA.
DR RefSeq; NP_001181942.1; NM_001195013.1.
DR PDB; 4O8Q; X-ray; 2.15 A; A/B=268-511.
DR PDBsum; 4O8Q; -.
DR AlphaFoldDB; P53619; -.
DR SMR; P53619; -.
DR IntAct; P53619; 3.
DR STRING; 9913.ENSBTAP00000008799; -.
DR PaxDb; P53619; -.
DR PeptideAtlas; P53619; -.
DR PRIDE; P53619; -.
DR Ensembl; ENSBTAT00000008799; ENSBTAP00000008799; ENSBTAG00000006690.
DR Ensembl; ENSBTAT00000074257; ENSBTAP00000071995; ENSBTAG00000006690.
DR GeneID; 533078; -.
DR KEGG; bta:533078; -.
DR CTD; 372; -.
DR VEuPathDB; HostDB:ENSBTAG00000006690; -.
DR VGNC; VGNC:26057; ARCN1.
DR eggNOG; KOG2635; Eukaryota.
DR GeneTree; ENSGT00390000017207; -.
DR HOGENOM; CLU_019988_3_0_1; -.
DR InParanoid; P53619; -.
DR OMA; YDARKHV; -.
DR OrthoDB; 1027200at2759; -.
DR TreeFam; TF105760; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000006690; Expressed in saliva-secreting gland and 109 other tissues.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0021691; P:cerebellar Purkinje cell layer maturation; IEA:Ensembl.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0051645; P:Golgi localization; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; TAS:UniProtKB.
DR GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR027059; Coatomer_dsu.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR PANTHER; PTHR10121; PTHR10121; 1.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoplasmic vesicle;
KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..511
FT /note="Coatomer subunit delta"
FT /id="PRO_0000193840"
FT DOMAIN 271..511
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 168..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48444"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48444"
FT MOD_RES 241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5XJY5"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48444"
FT MOD_RES 309
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48444"
FT MOD_RES 351
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5XJY5"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48444"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 273..286
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 292..306
FT /evidence="ECO:0007829|PDB:4O8Q"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:4O8Q"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 359..368
FT /evidence="ECO:0007829|PDB:4O8Q"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 375..383
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 389..397
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 404..412
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 421..432
FT /evidence="ECO:0007829|PDB:4O8Q"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 451..459
FT /evidence="ECO:0007829|PDB:4O8Q"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 467..476
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 481..488
FT /evidence="ECO:0007829|PDB:4O8Q"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:4O8Q"
FT STRAND 498..510
FT /evidence="ECO:0007829|PDB:4O8Q"
SQ SEQUENCE 511 AA; 57274 MW; 6A285798F252CC7F CRC64;
MVLLAAAVCT KAGKAIVSRQ FVEMTRTRIE GLLAAFPKLM NTGKQHTFVE TESVRYVYQP
MEKLYMVLIT TKNSNILEDL ETLRLFSRVI PEYCRALEEN EISEHCFDLI FAFDEIVALG
YRENVNLAQI RTFTEMDSHE EKVFRAVRET QEREAKAEMR RKAKELQQAR RDAERQGKKA
PGFGGFGSST VSGGSTTSMI TETIIETDKP KVAPAPARPS GPSKALKLGA KGKEVDNFVD
KLKSEGENII SSNMGKRTSE ATKVHAPPIN MESVHMKIEE KITLTCGRDG GLQNMELHGM
IMLRISDDKF GRIRLHVENE DKKGVQLQTH PNVDKKLFTA ESLIGLKNPE KSFPVNSDVG
VLKWRLQTTE ESFIPLTINC WPSESGNGCD VNIEYELQED NLELNDVVIT IPLPSGVGAP
VIGEIDGEYR HDSRRNTLEW CLPVIDAKNK SGSLEFSIAG QPNDFFPVQV SFISKKNYCN
IQVTKVTQVD GNSPVRFSTE TTFLVDKYEI L
