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Database: UniProt
Entry: E2ADX3_CAMFO
LinkDB: E2ADX3_CAMFO
Original site: E2ADX3_CAMFO 
ID   E2ADX3_CAMFO            Unreviewed;       957 AA.
AC   E2ADX3;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Coatomer subunit beta {ECO:0000256|ARBA:ARBA00017024, ECO:0000256|PIRNR:PIRNR005727};
DE   AltName: Full=Beta-coat protein {ECO:0000256|ARBA:ARBA00030841, ECO:0000256|PIRNR:PIRNR005727};
GN   ORFNames=EAG_13117 {ECO:0000313|EMBL:EFN68206.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN68206.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(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; GL438827; EFN68206.1; -; Genomic_DNA.
DR   RefSeq; XP_011256301.1; XM_011257999.2.
DR   AlphaFoldDB; E2ADX3; -.
DR   STRING; 104421.E2ADX3; -.
DR   EnsemblMetazoa; XM_011257999.3; XP_011256301.1; LOC105251308.
DR   GeneID; 105251308; -.
DR   KEGG; cfo:105251308; -.
DR   InParanoid; E2ADX3; -.
DR   OMA; MDYIIPA; -.
DR   OrthoDB; 151169at2759; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
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:UP000000311};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT   DOMAIN          24..525
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          665..805
FT                   /note="Coatomer beta subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07718"
FT   DOMAIN          812..942
FT                   /note="Coatomer beta subunit appendage platform"
FT                   /evidence="ECO:0000259|Pfam:PF14806"
FT   REGION          493..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   957 AA;  105540 MW;  E6FECCA8350C4646 CRC64;
     MSTITEQPCY TLINIPTDTE PLNELQLKQD LEKGSVQTKI DSLKKTIHMI LSGERLPGLL
     MTIIRFVLPL QNHTIKKLLL IFWEIVPKTS ADGKLLQEMI LVCDAYRKDL QHPNEFVRGS
     TLRFLCKLKE PELLEPLMPA ITACLEHRHS YVRRNAVLAI FTIYRNFEFL IPDAPELIAK
     YLEGEQDMSC RRNAFLMLLH ADQNRALAYL AACLDQVPSF GDILQLVIVE LIYKVCLANP
     SERARFIRCI YSLLNSPSAA VRYEAAGTLV TLSSAPTAIK AAASCYIELV VKESDNNVKL
     IVLDRLIAMK DSSVYERVLQ DLVMDVLRVL GSPALEVRTK TLALAMDLVT TRTIEEMVQL
     LKKEVLRTAG GEHEDAGRYR QLLVRTLHAC SMKFADVAAT VIPVLTDFLS ESNEAAATDV
     LVFVREAIQR FENLRPLIVE KLLEVFPHIR SVKVHRAALW ILGEYATSKE DIEAVMGRVR
     AALGELPLLE AENKRQAGEK SEDGNSQAAP TQLVTSDGTY ATQSAFSATS ARKKEEKRPA
     LVQYMMEGDF FIGASLATTL AKLALRYKTL ETNIQKSNRL QAEAMLIMSS MLQLGRSGLP
     MKAMTHDDAE RISLCLRSLA CPTPIVQKVF TEGCRDALGR MLTAKAEEDS QNQKAKEKPG
     SIVQVDDAIQ FLQLSRGSDL AGGAGDVFEQ SLSAAVAGRP GASGDAPAPS VLSKVTQLTG
     FSDPVYAEAL VHVNQYDIVL DVLIVNQTED TLQNCTLELA TMGDLKLVER PQPIVLAPRD
     FASIKANVKV ASTENGIIFG NIVYDVSGAG SDRSVVVLND IHIDIMDYIV PATCTDAEFR
     QMWAEFEWEN KVSVNTTLSD LREYLAHLLK STNMRCLTPE KALSGQCGFM AANMYAKSIF
     GEDALANLSI EKPLNKPDAP VVGHIRIRAK SQGMALSLGD KINSAQKGPQ TKVVQAA
//
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