ID   COPB_CHICK              Reviewed;         953 AA.
AC   Q5ZIA5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Coatomer subunit beta;
DE   AltName: Full=Beta-coat protein;
DE            Short=Beta-COP;
GN   Name=COPB1; Synonyms=COPB; ORFNames=RCJMB04_28l17;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=20728927; DOI=10.1016/j.theriogenology.2010.05.017;
RA   Lin Y.P., Chen L.R., Chen C.F., Liou J.F., Chen Y.L., Yang J.R.,
RA   Shiue Y.L.;
RT   "Identification of early transcripts related to male development in chicken
RT   embryos.";
RL   Theriogenology 74:1161-1178(2010).
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). {ECO:0000250}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits. {ECO:0000250}.
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   -!- DEVELOPMENTAL STAGE: Expressed more highly in male embryonic day 3 (E3)
CC       and E5 whole embryos, paired urogenital system at E7 and gonads at E9
CC       than in females. {ECO:0000269|PubMed:20728927}.
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DR   EMBL; AJ720879; CAG32538.1; -; mRNA.
DR   RefSeq; NP_001006467.1; NM_001006467.1.
DR   RefSeq; XP_015141877.1; XM_015286391.1.
DR   AlphaFoldDB; Q5ZIA5; -.
DR   SMR; Q5ZIA5; -.
DR   BioGRID; 683642; 1.
DR   STRING; 9031.ENSGALP00000009665; -.
DR   PaxDb; Q5ZIA5; -.
DR   Ensembl; ENSGALT00000009679; ENSGALP00000009665; ENSGALG00000006015.
DR   GeneID; 423063; -.
DR   KEGG; gga:423063; -.
DR   CTD; 1315; -.
DR   VEuPathDB; HostDB:geneid_423063; -.
DR   eggNOG; KOG1058; Eukaryota.
DR   GeneTree; ENSGT00390000005270; -.
DR   HOGENOM; CLU_006949_0_0_1; -.
DR   InParanoid; Q5ZIA5; -.
DR   OMA; QCGFMAA; -.
DR   OrthoDB; 195812at2759; -.
DR   PhylomeDB; Q5ZIA5; -.
DR   TreeFam; TF105737; -.
DR   Reactome; R-GGA-6798695; Neutrophil degranulation.
DR   Reactome; R-GGA-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-GGA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   PRO; PR:Q5ZIA5; -.
DR   Proteomes; UP000000539; Chromosome 5.
DR   Bgee; ENSGALG00000006015; Expressed in granulocyte and 12 other tissues.
DR   GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR011710; Coatomer_bsu_C.
DR   InterPro; IPR016460; COPB1.
DR   InterPro; IPR029446; COPB1_appendage_platform_dom.
DR   PANTHER; PTHR10635; PTHR10635; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF07718; Coatamer_beta_C; 1.
DR   Pfam; PF14806; Coatomer_b_Cpla; 1.
DR   PIRSF; PIRSF005727; Coatomer_beta_subunit; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Repeat; Transport.
FT   CHAIN           1..953
FT                   /note="Coatomer subunit beta"
FT                   /id="PRO_0000347230"
FT   REPEAT          17..54
FT                   /note="HEAT 1"
FT   REPEAT          96..131
FT                   /note="HEAT 2"
FT   REPEAT          132..168
FT                   /note="HEAT 3"
FT   REPEAT          240..276
FT                   /note="HEAT 4"
FT   REPEAT          277..314
FT                   /note="HEAT 5"
FT   REPEAT          316..353
FT                   /note="HEAT 6"
FT   REPEAT          396..433
FT                   /note="HEAT 7"
SQ   SEQUENCE   953 AA;  107121 MW;  8E1954813920C53C CRC64;
     MTAAENVCYT LINVPMDSEP PSEISLKNDL EKGDVKLKTE ALKKVIIMIL NGEKLPGLLM
     TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGRLLQEMIL VCDAYRKDLQ HPNEFIRGST
     LRFLCKLKEA ELLEPLMPAI RACLEHRHSY VRRNAVLAIY TIYRNFEHLI PDAPELIHDF
     LVNEKDASCK RNAFMMLIHA DQDRALDYLS TCIDQVQTFG DILQLVIVEL IYKVCHANPS
     ERARFIRCIY NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI
     VLDRLVELKE HPSHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS RNVEELVIVL
     KKEVIKTNNV TEHEDTDKYR QLLVRTLHSC SVRFPDMAAN VIPVLMEFLS DNNEAAAADV
     LEFVREAIQR FDNLRPLIVE KMLEVFHAIK SVKIYRGALW ILGEYCSTKE DIQSVMTEVR
     RSLGEIPIVE SEIKKEAGEL KPEEEVTVGP VQKLVTEMGT YATQSALSSS RPTKKEEDRP
     PLRGFLLDGD FFVAASLATT LTKIALRYVS LVQEKKKQNS FIAEAMLLMA TILHLGKSSL
     PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRQSLS HMLSAKLEEE KLSQKKESEK
     RNVTVQPDDP ISFMQLTAKN EMSSKEDQFQ LSLLAAMGNT QRKEAADPLA SKLNKVTQLT
     GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH
     DFANIKANVK VASTENGIIF GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPASCTDAEF
     RQMWAEFEWE NKVTVNTNII DLNEYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI
     FGEDALANVS IEKPIHLGPE APVTGHIRIR AKSQGMALSL GDKINLSQKK TSL