ID D7G7C5_ECTSI Unreviewed; 967 AA.
AC D7G7C5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN Name=CPC24 {ECO:0000313|EMBL:CBJ27676.1};
GN ORFNames=Esi_0080_0089 {ECO:0000313|EMBL:CBJ27676.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ27676.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ27676.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(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 {ECO:0000256|PIRNR:PIRNR005727}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC {ECO:0000256|PIRNR:PIRNR005727}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR005727}. Golgi
CC apparatus membrane {ECO:0000256|ARBA:ARBA00004255,
CC ECO:0000256|PIRNR:PIRNR005727}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR005727};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255,
CC ECO:0000256|PIRNR:PIRNR005727}. Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000256|PIRNR:PIRNR005727}; Peripheral membrane
CC protein {ECO:0000256|PIRNR:PIRNR005727}; Cytoplasmic side
CC {ECO:0000256|PIRNR:PIRNR005727}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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DR EMBL; FN649036; CBJ27676.1; -; Genomic_DNA.
DR AlphaFoldDB; D7G7C5; -.
DR STRING; 2880.D7G7C5; -.
DR EnsemblProtists; CBJ27676; CBJ27676; Esi_0080_0089.
DR eggNOG; KOG1058; Eukaryota.
DR InParanoid; D7G7C5; -.
DR OMA; MDYIIPA; -.
DR OrthoDB; 151169at2759; -.
DR Proteomes; UP000002630; Chromosome LG28.
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; Leucine-rich Repeat Variant; 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; COATOMER SUBUNIT BETA; 1.
DR PANTHER; PTHR10635:SF0; COATOMER SUBUNIT BETA; 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; ARM repeat; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR005727};
KW Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR005727};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|PIRNR:PIRNR005727};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|PIRNR:PIRNR005727};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005727};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR005727};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT DOMAIN 24..478
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 684..818
FT /note="Coatomer beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07718"
FT DOMAIN 824..953
FT /note="Coatomer beta subunit appendage platform"
FT /evidence="ECO:0000259|Pfam:PF14806"
FT REGION 481..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 105677 MW; ABC6B2EA87CB760C CRC64;
MAVTEQHCTI LFNSDGLQSM QQDDIIKNLE QPNISGKVTG IKQAILLLLS GETMPRLLMS
VIKGCLKDDS KELKKLVMMY WEVVKKYDAE GKLLPEMILV CNALRNDLNH PNEYVRGCTL
RFLCKLREPE LLEPLIPTVK LCLEHRHSYV RRNAALLCYY VHKNFGQQLL PDGPELIERF
IAAEGDTSAR RSAFLFLYNE SEELAIDFLN NHMEDVPKFG DGFALLVLEL CRKVCRRDPS
QKSRFVRVLL SMLQSRSAAV SYEAAWTLVS LSGAPTAIRA AATTYAQLLN TQSDNNVKLI
VLERLAGLKK HHTKVLQEVL MDILRALSSP NVDICRKTLE VAMDLVTPRN IEEVVQVLKR
EVVRTQEAGM EKGTQYRTLL IQAIHGCATK FADVAESVVG VLMDFLNGDG AMDVILFVRS
IVEQYEGLRP SILSKLIFSL RDMVNGPVIA VAIWILGEYC EDADAITSAF TELRESVGPM
PLTEANSSAA NGGADGGPAK EGGAAEEGGG AAAGAGGGGT TVTKNIVLSD GTYATQTTVQ
GGGVAAVASA LKSDARLRQL LVGGEIFLGS ALSASLTKMT LRAMDLLGDS SPAAKEMQIA
TLQILCGLAK VIEARSLTHR GAYADCLERV TMCCRSLLDP AARAVLKPTL LDLCRQSFQQ
LLDKEKAAQA KQAEEMEGRP RSQPDDLINF RQLRSNALQA AELDIYDGDD ISKATGMDAP
DTGRLSHIYQ LSGFADPVYA EACVTVHDYD IVLEMLVINR TPNTLTNLTV ELSTMGDLRL
VERPQSHTIG PLDSRNIRAN IKVSSTETGH IFGTIVYENS STAEKTYINL NDIHMDIMDY
IKPASCSEEA FRSMWAEFEW ENKVAVNTSF TDLNAFLKHL VAKTNTNCLT PLSSLDGSSS
FLAANLYAMS VFGEDALVNV SVEKKSDADG KLSGHVRIRS KTQGIALSLG DRITLVQRGP
GTTKAQP
//
