ID   COPB_TRYBB              Reviewed;         982 AA.
AC   Q9NFU6;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Coatomer subunit beta {ECO:0000250|UniProtKB:P23514};
DE   AltName: Full=Beta-coat protein {ECO:0000250|UniProtKB:P23514};
DE            Short=Beta-COP {ECO:0000250|UniProtKB:P23514};
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1] {ECO:0000312|EMBL:CAB87383.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX   PubMed=11377739; DOI=10.1016/s0166-6851(01)00268-7;
RA   Maier A.G., Webb H., Ding M., Bremser M., Carrington M., Clayton C.;
RT   "The coatomer of Trypanosoma brucei.";
RL   Mol. Biochem. Parasitol. 115:55-61(2001).
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|UniProtKB:P23514}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits.
CC       {ECO:0000250|UniProtKB:A0JN39}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11377739}. Golgi
CC       apparatus membrane {ECO:0000250|UniProtKB:P23514}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:P23514}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P23514}. Cytoplasmic vesicle, COPI-coated
CC       vesicle membrane {ECO:0000250|UniProtKB:P23514}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:P23514}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P23514}. Note=The coatomer is cytoplasmic or
CC       polymerized on the cytoplasmic side of the Golgi, as well as on the
CC       vesicles/buds originating from it. {ECO:0000250|UniProtKB:P23514}.
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DR   EMBL; AJ271083; CAB87383.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9NFU6; -.
DR   SMR; Q9NFU6; -.
DR   GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Protein transport; Repeat; Transport.
FT   CHAIN           1..982
FT                   /note="Coatomer subunit beta"
FT                   /id="PRO_0000408948"
FT   REPEAT          16..53
FT                   /note="HEAT 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          130..167
FT                   /note="HEAT 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          241..278
FT                   /note="HEAT 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          317..352
FT                   /note="HEAT 4"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   982 AA;  110021 MW;  9A52B163617CCBD9 CRC64;
     MEAKAEGFCS FLVGLSGAPV NSKELKSALE KGDMKARASA LEALIRMHLN GEPQNHMIMT
     VIKFITPLDD HYIKKLVLYF WEVVDKTDAS GKLLSEMILI CSFLREDLLH PNEYIRGLAL
     RFMCKVKERE LVEPLVSSVV QNLTHRVTYV RRNAVLAVHR IFKRFPELLP DAAELVEKFI
     SEENDVSASR NAFEMLVECS PDRVVKFLAE LRESKNLESL GATLQMSIVD FAGHMIRANP
     YDKGRYVTVL FSILQSNNPA VRYQCASTLL SISTSPTAIR QAALTFIDLL KTHTDISVRL
     IVVDQLDAMR ERFSKILQDS LLDILSVLAN GTMEIRKRIV TLGVELVSNQ NSEVFVQAIK
     KELYWVKNEC DVDDKESLLE YKKLLIRATR TAVARRPHMA SAVIPLVLEY LYEEDDSGFE
     VVSLIREVLQ LQPSLRSETL RQLRQTLRMI RCPSVIRTVL WLLGTHVTSA DDALEVIRLL
     INTLEPLPLE PTVKEQMKQQ EDFDGHKGGQ QKPRMQMTTI VQEDGTYVMS SVPSNKTQED
     AEGNDSNCGL RGVLTGGKFF IAAPLASTLS KLIIRLFNHH SSGVDESTMK EAQNSAIMLL
     NEVLRFCTMD GAAGMIDDAT HEQIRLALLN ITNPRSPLLA TFVEDSSKAL DSLTNKVGSI
     AGGDGFDFNK RNNDNVVGRT SFDEQQVALC SVDTPVMFTQ IMEGKGSLLE LEAVDDLGSV
     VANASIEKTE EFLIKLEKTV PLSGFCDPLY CEASVTVHQF DITVDWYIAN CTANVLRDVS
     IELTPLGSMK LCERPQVHTI QPHGSVRIRT ALKVGSPETG VICASVLYEG PQNERGCVVL
     NNVRVDIMNY VRPAKCSASE FRDKWCKYDW ENAVAIRTEK TDMREYVEYV MQGTNTRLLE
     PYPEEDDEVV SAFDGKGDNG HRYVSCNMYA RTLFGDDALL NVSIERDAEG KLSGMVRVRA
     NKRPVAYGFG EKLNILNRRI VS