ID C3Y7L1_BRAFL Unreviewed; 930 AA.
AC C3Y7L1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=BRAFLDRAFT_275075 {ECO:0000313|EMBL:EEN63839.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN63839.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN63839.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN63839.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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; GG666489; EEN63839.1; -; Genomic_DNA.
DR RefSeq; XP_002607829.1; XM_002607783.1.
DR AlphaFoldDB; C3Y7L1; -.
DR STRING; 7739.C3Y7L1; -.
DR eggNOG; KOG1058; Eukaryota.
DR InParanoid; C3Y7L1; -.
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 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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT DOMAIN 11..503
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 644..783
FT /note="Coatomer beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07718"
FT DOMAIN 790..921
FT /note="Coatomer beta subunit appendage platform"
FT /evidence="ECO:0000259|Pfam:PF14806"
SQ SEQUENCE 930 AA; 104409 MW; 185D930934DF28EC CRC64;
MFHVFPPTEK GDVRTKTEAL KKVIHMILNG EKMPSLLMTI IRFVMPLQDH TIKKLLLIFW
EIVPKTGPDG KMLHEFILVC DAYRKDLQHP NEFIRGSTLR FLCKLKESEL LEPLMPSIRT
CLEHRHSYVR RNAVLAIFTI YKNFDTLIPD GPELIHNFLE QEQDASCKRN AFMMLIHADQ
ERALDYLSTC IDQLHTFGDI LQLVIVELVY KVCHANPNER ARFIRCIYNL LNSSSPAVRY
EAAGTLVTLS SAPTAIKAAA SCYIELIVKE SDNNVKLIVL DRLIALKDNP QHERVLQDLV
MDILRVLSTP DLEVRKKTLN LALDLVSSRN VEELVLVLKK EVIKTNDITE HEDTDKYRQL
LVRTLHSCSI KFPDMAGAVI PVLMEFLSDQ NELAAADVLV FVREAIQRFD QLKHVILEKL
LEVFPSIKSV KIHRAALWIL GEYCTTAEDI QALMHEIRHS LGDIPIVESE MKKAAGEIKD
EDEFTPTQQK LLTAEGTYAT QSALTSTVKK SSEEKRPPLR GFLMDGDFFV GASLATTLTK
LAIRYGEIVP DPKKHNSFNA ECMLIMATII HLGKSGLATK PITDDDLDRI ALCLKVLSDH
TPAVNDIFSR ECRHSLSTML AALHEEEKEN QKTVIEKKTV SVQPDDPISF MQLVNKAEHG
TTEDLFELSL LQAVGTPQKK DAADPQASKL QKVNQLTGFS DPVYAEAYVH VNQYDIVLDV
LIVNQTSDTL QSVTLELATL GDLKLVEKPS PIILAPHDFA NIKANVKVAS TENGIIFGNI
VYDVSGAASD RNCVVLNDIH IDIMDYIVPA QCSDNEFRQM WAEFEWENKV TVNTSITDLG
IYMGHLLKST NMKSLTPEKA LSGECGFMAA NLYARSIFGE DVLANLSIEK MIHLGEDAPV
QGHIRIRAKS QGMALSMGDK VNMCQKNPPK
//
