COPB_TOXGO
ID COPB_TOXGO Reviewed; 1103 AA.
AC Q9U4N3;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 25-MAY-2022, entry version 76.
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 Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1] {ECO:0000312|EMBL:AAF02542.2}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=RH {ECO:0000312|EMBL:AAF02542.2};
RX PubMed=17485226; DOI=10.1016/j.ympev.2007.02.031;
RA Smith S.S., Pfluger S.L., Hjort E., McArthur A.G., Hager K.M.;
RT "Molecular evolution of the vesicle coat component betaCOP in Toxoplasma
RT gondii.";
RL Mol. Phylogenet. Evol. 44:1284-1294(2007).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF02542.2}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 911-1103, AND SUBCELLULAR LOCATION.
RC STRAIN=RH {ECO:0000312|EMBL:AAF02542.2};
RX PubMed=10413671; DOI=10.1242/jcs.112.16.2631;
RA Hager K.M., Striepen B., Tilney L.G., Roos D.S.;
RT "The nuclear envelope serves as an intermediary between the ER and Golgi
RT complex in the intracellular parasite Toxoplasma gondii.";
RL J. Cell Sci. 112:2631-2638(1999).
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:10413671}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:10413671}; Peripheral membrane
CC protein {ECO:0000269|PubMed:10413671}; Cytoplasmic side
CC {ECO:0000269|PubMed:10413671}. Cytoplasmic vesicle, COPI-coated vesicle
CC membrane {ECO:0000269|PubMed:10413671}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10413671}; Cytoplasmic side
CC {ECO:0000269|PubMed:10413671}. 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 (By similarity). Apical juxtanuclear
CC region. {ECO:0000250|UniProtKB:P23514, ECO:0000269|PubMed:10413671}.
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DR EMBL; DQ279721; AAF02542.2; -; mRNA.
DR AlphaFoldDB; Q9U4N3; -.
DR SMR; Q9U4N3; -.
DR VEuPathDB; ToxoDB:TGARI_266990A; -.
DR VEuPathDB; ToxoDB:TGARI_266990B; -.
DR VEuPathDB; ToxoDB:TGARI_266990C; -.
DR VEuPathDB; ToxoDB:TGCAST_266990A; -.
DR VEuPathDB; ToxoDB:TGCAST_266990B; -.
DR VEuPathDB; ToxoDB:TGCOUG_266990A; -.
DR VEuPathDB; ToxoDB:TGCOUG_266990B; -.
DR VEuPathDB; ToxoDB:TGCOUG_392750; -.
DR VEuPathDB; ToxoDB:TGDOM2_266990; -.
DR VEuPathDB; ToxoDB:TGFOU_266990A; -.
DR VEuPathDB; ToxoDB:TGFOU_266990B; -.
DR VEuPathDB; ToxoDB:TGFOU_405410; -.
DR VEuPathDB; ToxoDB:TGGT1_266990; -.
DR VEuPathDB; ToxoDB:TGMAS_266990A; -.
DR VEuPathDB; ToxoDB:TGMAS_266990B; -.
DR VEuPathDB; ToxoDB:TGME49_266990; -.
DR VEuPathDB; ToxoDB:TGP89_266990A; -.
DR VEuPathDB; ToxoDB:TGP89_266990B; -.
DR VEuPathDB; ToxoDB:TGPRC2_266990A; -.
DR VEuPathDB; ToxoDB:TGPRC2_266990B; -.
DR VEuPathDB; ToxoDB:TGPRC2_266990D; -.
DR VEuPathDB; ToxoDB:TGRH88_011020; -.
DR VEuPathDB; ToxoDB:TGRUB_266990A; -.
DR VEuPathDB; ToxoDB:TGRUB_266990B; -.
DR VEuPathDB; ToxoDB:TGVAND_266990A; -.
DR VEuPathDB; ToxoDB:TGVAND_266990B; -.
DR VEuPathDB; ToxoDB:TGVEG_266990; -.
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 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Repeat; Transport.
FT CHAIN 1..1103
FT /note="Coatomer subunit beta"
FT /id="PRO_0000408947"
FT REPEAT 51..89
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 94..129
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 130..166
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 247..284
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 322..359
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 365..404
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 405..441
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1103 AA; 121852 MW; CBC646FBC08B447D CRC64;
MELERNCMLY IYSSRGDAPS TAELQKKIES PNEATKAEGM QDLIIGMTQG EAYTRLLMTV
IRYAMPSKDK RVKKLTQLYL EIVGKCRPDG SLKEEMILIC NALRNDLMSP NEYVRGSTLR
LLSKIRQFKV LEPLVEAILQ NLTHRHSYVR RNAVMCVYSI VKNFGLDAIP ATIDQIEQML
LSEGDLTTKR NAFLVLVHCA SKRAIQFILQ QRSEDGTGGL GFLLSSGDLF QLALLELLRK
VCRQKQQQKA GLLRLIVSIL PNTLPSVAYE GACSLLALSR APVSLKAAAG AFASLLCGNS
DNNVKLIVLD RLQECVQRAS RRTMEEFVID LLRGLQTPSL EVRRKILDLV LQIVGKNSVE
QLLNVLKREL LRTAEPEQLT VPRTMEYRRL LIKAVHSCCT RFPEAAASVV NVLIDFPGDP
DVTTATEVAV VVRELVATCV HLRSRIISRV VDAFPDSAHA RVLRVSLWML GEFCEDSELL
DSFLTAVYAA CSPLPFTSGD SGGAEGEQRS GCQPKLKMTT RTVVLEDGTY GTEDVYESVN
EKGDSSAKAG KTALRKFILG GDFLLASTVA VTCAKLILKT SDEVHAQLAE EFERHREAVQ
EKAGRRTLTG DAQARETLLE RQELEGKVAP VKLRASTEQK TRVLYLVACL LKFLRLSSSG
AGAHSDAAIR VCQSLRALCG LMTGLEKEKA FVRHWVHHGR FALERVLALG PVSDDPFTWN
LKDAEDEKTV SAPDDLAFFR QLRPDRQSLM VASEGVAAVG EDSLEEDEIY YSACAGLARG
AELEEVDETE ADLQLTVGGA GGTSPSLSGG NAKDDAALFQ QRLAKVQPIT GQADPLYVEA
FLQVNQFDLL VEMLVVNRTQ DSLQNVTVEP STHGDLKLVE RPAPVSLAPG QQAVLHAPIK
VRSTEAGIIL GYVTFSRRGS SDKECLVLNE LHIDVLDYIE RRWTCELAFR SMWAEFEWEN
KIHVNTSFTD VSEFLEHLMK MTNLTVVGFR PPASVMRRLK FSAACAGLDE AERAAGDGEE
DEDRYLQSVR KIPTLRKLSE SSSFFAVNLY SRSIFGEDAL VNVSIEKLPG GKLAGSIRIR
SRTQGIALSL GDRITVVQRG LTK
