COPB_DICDI
ID COPB_DICDI Reviewed; 912 AA.
AC Q23924; Q54P83; Q9NGP1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Coatomer subunit beta;
DE AltName: Full=Beta-coat protein;
DE Short=Beta-COP;
GN Name=copb; Synonyms=rcdC, veg125; ORFNames=DDB_G0284735;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=10887966; DOI=10.1078/s0171-9335(04)70039-4;
RA Mohrs M.R., Janssen K.-P., Kreis T., Noegel A.A., Schleicher M.;
RT "Cloning and characterization of beta-COP from Dictyostelium discoideum.";
RL Eur. J. Cell Biol. 79:350-357(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 513-912.
RC STRAIN=AX4;
RX PubMed=8643615; DOI=10.1073/pnas.93.11.5562;
RA Kuspa A., Loomis W.F.;
RT "Ordered yeast artificial chromosome clones representing the Dictyostelium
RT discoideum genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5562-5566(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 (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:0000269|PubMed:10887966}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10887966}; Cytoplasmic side
CC {ECO:0000269|PubMed:10887966}. Cytoplasmic vesicle, COPI-coated vesicle
CC membrane {ECO:0000269|PubMed:10887966}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10887966}; Cytoplasmic side
CC {ECO:0000269|PubMed:10887966}. 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}.
CC -!- MISCELLANEOUS: Brefeldin A does not induce dissociation from the Golgi
CC of the beta-COP and presumably the other coatomer subunits, but DMSO
CC does.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF247143; AAF62179.1; -; mRNA.
DR EMBL; AAFI02000071; EAL65020.1; -; Genomic_DNA.
DR EMBL; U62960; AAB04026.1; -; mRNA.
DR RefSeq; XP_638375.1; XM_633283.1.
DR AlphaFoldDB; Q23924; -.
DR SMR; Q23924; -.
DR STRING; 44689.DDB0191250; -.
DR PaxDb; Q23924; -.
DR EnsemblProtists; EAL65020; EAL65020; DDB_G0284735.
DR GeneID; 8624744; -.
DR KEGG; ddi:DDB_G0284735; -.
DR dictyBase; DDB_G0284735; copB.
DR eggNOG; KOG1058; Eukaryota.
DR HOGENOM; CLU_006949_0_0_1; -.
DR InParanoid; Q23924; -.
DR OMA; QCGFMAA; -.
DR PhylomeDB; Q23924; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DDI-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q23924; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:dictyBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:dictyBase.
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; 2.
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..912
FT /note="Coatomer subunit beta"
FT /id="PRO_0000193836"
FT REPEAT 59..96
FT /note="HEAT 1"
FT REPEAT 100..135
FT /note="HEAT 2"
FT REPEAT 136..172
FT /note="HEAT 3"
FT REPEAT 244..281
FT /note="HEAT 4"
FT REPEAT 300..337
FT /note="HEAT 5"
FT REPEAT 339..375
FT /note="HEAT 6"
FT REPEAT 397..434
FT /note="HEAT 7"
FT REPEAT 441..479
FT /note="HEAT 8"
FT REPEAT 550..575
FT /note="HEAT 9"
FT REPEAT 576..612
FT /note="HEAT 10"
SQ SEQUENCE 912 AA; 102855 MW; 60123AE2DBE98CEE CRC64;
MSALTQSGSI EKPCTILINY DKGDPPQVNE FKQNFEHGTT EQKIETLKKV ILYTINGEPI
PQLLMPIILY VMPSNDHTIK KLLLIYWEVI EKTHLGKLKS EMILVCNSLL NDLNHPNEFV
RGSTLRFLCK LREAEVLEPL VPSVRSNLEN RHAYCRRNAV LAIYNIYSHF DYLIPDAPEL
IYNFLLQEKD ASCKRNAFIM LFNCAPEKAV EYLSSVLDEV PSFGDMLQFI VVELIRKVCK
TSPSERSKYI KCIFTLLNSS SPAVKYESAG TLLSLSSAPT AVRGAASAYI DLLCNESDNN
VKMIVLDKLI EIKKNHSKIM EELVMDILRA LSSPNIDICK KVLNIVLDSV TPKNIDEIIL
FLKKEINKTQ SKEFDKGLEY RHILIRTIHV SSLKYPEVLG NVVPLLMEYL GDSYLPSAVD
VVIFLREVVE TYPSLRELII KKLIENLSSI KVSKVYRVAV WVIAEYVTCL EDLQYAMTSI
TNDLEELLKP KQTEEVILET KAKVKIEKVS IQKLIADGDW YLASCISSSL TKLFFRAEQL
NIDNADSNKL KAQVMMIISV LINLSKASQV STSKSAYERM LSCIQVLIDS NATIKKIWLQ
DCRDSFANYL KYLLIKQSEN KKKTEKEVLV KPNNIINIRQ LKSKKAFGPV DTEDDLIKAV
GNTGEANKDQ NEYSKISQLS GFSDPIYVEA YVRVHQYDIV LDISVFNQTN DTLQNVTLEL
VTLGDLKICE RVPPFTMAPR EKTSAKASIK VSSTDNGVIM GTIAFDIAGS VSSMSDKNCV
ILNELHIDVI DYILPANHQY TDVLFRNHWL EFEWENKIPV NTNITDLVKY VHHISKVTNM
GILTPEVHLS NDTGILSANL CAKSVFGEDA LANICIEKQA DGKISGYIRI RAKVQSIAVT
LGEKIGNMGM KA
