COPB_DANRE
ID COPB_DANRE Reviewed; 953 AA.
AC Q66HV4; Q6JWU8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Coatomer subunit beta {ECO:0000312|EMBL:AAH81657.1};
DE AltName: Full=Beta-coat protein {ECO:0000250|UniProtKB:P23514};
DE Short=Beta-COP {ECO:0000250|UniProtKB:P23514};
GN Name=copb1 {ECO:0000312|EMBL:AAQ63171.1};
GN Synonyms=hap {ECO:0000303|PubMed:15469843},
GN happy {ECO:0000303|PubMed:15469843};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAQ63171.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
RX PubMed=15469843; DOI=10.1016/j.devcel.2004.07.020;
RA Coutinho P., Parsons M.J., Thomas K.A., Hirst E.M., Saude L., Campos I.,
RA Williams P.H., Stemple D.L.;
RT "Differential requirements for COPI transport during vertebrate early
RT development.";
RL Dev. Cell 7:547-558(2004).
RN [2] {ECO:0000312|EMBL:AAH81657.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P23514}. 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}.
CC -!- DISRUPTION PHENOTYPE: From 28 hours post-fertilization (hpf) onward,
CC embryos show an anterior-posterior gradient of pigmentation defects.
CC While the head is fully pigmented, more posterior regions are
CC decreasingly pigmented until midtrunk levels, where pigmentation is not
CC detectable. Melanophores are present at midtrunk levels and migrate
CC correctly, but are not properly pigmented. Embryos show severe
CC reduction in pigmentation and widespread degeneration from 48 hpf
CC onward. Failure to form perinotochordal basement membrane (PBM),
CC without the loss of laminin immunoreactivity. Embryos are significantly
CC shorter, because the notochord cells fail to differentiate and the
CC notochord fails to lengthen properly. Vacuoles fail to inflate fully.
CC Many notochord cells die by apoptosis. In 32 hpf embryos the
CC endoplasmic reticulum is abnormally swollen and filled with a
CC relatively electron dense material and the Golgi complex is fragmented
CC into large vesicles throughout the cytoplasm. PBM is thin, disorganized
CC and essentially lacks the medial layer. However, cells have a
CC distinctive inner layer. {ECO:0000269|PubMed:15469843}.
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DR EMBL; AY294010; AAQ63171.1; -; mRNA.
DR EMBL; BC081657; AAH81657.1; -; mRNA.
DR RefSeq; NP_001002013.1; NM_001002013.1.
DR AlphaFoldDB; Q66HV4; -.
DR SMR; Q66HV4; -.
DR STRING; 7955.ENSDARP00000073498; -.
DR PaxDb; Q66HV4; -.
DR PRIDE; Q66HV4; -.
DR Ensembl; ENSDART00000079042; ENSDARP00000073498; ENSDARG00000056557.
DR Ensembl; ENSDART00000185811; ENSDARP00000147390; ENSDARG00000116045.
DR GeneID; 338138; -.
DR KEGG; dre:338138; -.
DR CTD; 1315; -.
DR ZFIN; ZDB-GENE-030219-38; copb1.
DR eggNOG; KOG1058; Eukaryota.
DR GeneTree; ENSGT00390000005270; -.
DR HOGENOM; CLU_006949_0_0_1; -.
DR InParanoid; Q66HV4; -.
DR OMA; QCGFMAA; -.
DR OrthoDB; 195812at2759; -.
DR PhylomeDB; Q66HV4; -.
DR TreeFam; TF105737; -.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR Reactome; R-DRE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DRE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q66HV4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000056557; Expressed in gastrula and 23 other tissues.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
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 GO; GO:0030903; P:notochord development; IMP:ZFIN.
DR GO; GO:0061053; P:somite development; IMP:ZFIN.
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_0000408944"
FT REPEAT 96..131
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 132..168
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 240..276
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 277..314
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 316..353
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 396..433
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT CONFLICT 146
FT /note="H -> R (in Ref. 1; AAQ63171)"
FT /evidence="ECO:0000305"
FT CONFLICT 935
FT /note="G -> V (in Ref. 1; AAQ63171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 953 AA; 107032 MW; 293B52FD3451C773 CRC64;
MTAAENVCYT LINVTNDSEP PSEVSLKTDL EKGEIKAKTE ALKKVIIMIL NGEKLPGLLM
TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGKLLQEMIL VCDAYRKDLQ HPNEFIRGST
LRFLCKLKES ELLEPLMPAI RACLEHRHSY VRRNAVLAIY TIYRNFEHLI PDAPELIHDF
LVNEKDASCK RNAFMMLIHA DQDRALDYLS TCIDQVHTFG DILQLVIVEL IYKVCHANPS
ERARFIRCIY NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI
VLDRLIELKE HPTHERVLQD LVMDILRVLT TPDLEVRKKT LQLALDLVSS RNVEELVIVL
KKEVIKTNNV TEHEDTDKYR QLLVRTLHSC SVRFPDMAAN VIPVLMEFLS DTNEAAAADV
LEFVREAIQR FDNLRPLIIE KMLEVFHAIK TVKIYRGALW ILGEYCSTKE DIQSVMTEVR
RSLGEIPIVE NELKKEAGEV KPEEEVTAAP APKLVTEMGT YVTQSALSTS RPSKKEEDRP
PLRGFLMDGD FYVAASLATT LTKVALRYVA LAEDKRRQNS FVAEAMLIMA TVLHLGKSSL
PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRRSLS HMLAVRLEEE KLSQKKESEK
RNVTVQADDP ISFMQLTAKN EMASKEDQFQ LSLLAAMGNT QRKEATDPLA SKLNKVTQLT
GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH
DFANIKANVK VASTENGIIF GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPASCTDAEF
RQMWAEFEWE NKVTVNTNIT DLNDYLLHIL KSTNMKCLTP EKALSGICGF MAANLYARSI
FGEDALANVS IEKPIHLGVD APVNGHIRIR AKSQGMALSL GDKINLSQKR TAS
