ID V4BQF1_LOTGI Unreviewed; 962 AA.
AC V4BQF1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Coatomer subunit beta' {ECO:0000256|PIRNR:PIRNR005567};
GN ORFNames=LOTGIDRAFT_182444 {ECO:0000313|EMBL:ESO91109.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO91109.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO91109.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
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:PIRNR005567}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC {ECO:0000256|PIRNR:PIRNR005567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004347, ECO:0000256|PIRNR:PIRNR005567};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004347,
CC ECO:0000256|PIRNR:PIRNR005567}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004347, ECO:0000256|PIRNR:PIRNR005567}. Golgi
CC apparatus membrane {ECO:0000256|PIRNR:PIRNR005567}; Peripheral membrane
CC protein {ECO:0000256|PIRNR:PIRNR005567}; Cytoplasmic side
CC {ECO:0000256|PIRNR:PIRNR005567}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}. 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:0000256|PIRNR:PIRNR005567}.
CC -!- SIMILARITY: Belongs to the WD repeat COPB2 family.
CC {ECO:0000256|ARBA:ARBA00010844, ECO:0000256|PIRNR:PIRNR005567}.
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DR EMBL; KB202283; ESO91109.1; -; Genomic_DNA.
DR RefSeq; XP_009057822.1; XM_009059574.1.
DR AlphaFoldDB; V4BQF1; -.
DR STRING; 225164.V4BQF1; -.
DR EnsemblMetazoa; LotgiT182444; LotgiP182444; LotgiG182444.
DR GeneID; 20244493; -.
DR KEGG; lgi:LOTGIDRAFT_182444; -.
DR CTD; 20244493; -.
DR HOGENOM; CLU_005507_3_0_1; -.
DR OMA; KSYGQCV; -.
DR OrthoDB; 20819at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030117; C:membrane coat; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR CDD; cd22947; Coatomer_WDAD_beta-like; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.25.40.470; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR006692; Coatomer_WD-assoc_reg.
DR InterPro; IPR016453; COPB2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011048; Haem_d1_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19876; COATOMER; 1.
DR PANTHER; PTHR19876:SF2; COATOMER SUBUNIT BETA; 1.
DR Pfam; PF04053; Coatomer_WDAD; 1.
DR Pfam; PF00400; WD40; 6.
DR PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 4.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR005567};
KW Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR005567};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|PIRNR:PIRNR005567};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|PIRNR:PIRNR005567};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005567};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR005567};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005567};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 11..52
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 95..127
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 138..180
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 181..224
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 225..266
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 319..762
FT /note="Coatomer WD associated region"
FT /evidence="ECO:0000259|Pfam:PF04053"
FT REGION 821..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..912
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 108606 MW; 2D74C9D8FE849165 CRC64;
MPLRLDIKRK LSARSDRVKS VDLHPSEPWM LASLYNGNVH IWNYESQQLI KSFEVCDLPV
RAAKFVARKN WVITGSDDMT VRVYNYNTLE RVHQFEAHSD YLRSIAVHPT QPYILTSSDD
MLIKLWDWDK NWTCTQVFEG HSHYVMQIVI NPKDNNQFAS ASLDRTVKVW QLGSNAPNFT
LEGHEKGVNC VDYYSGGDKP YLISGGDDRL VKIWDYQNKT CVQTLEGHAQ NISSVSFHPE
LPIIMTGSED GTVRIWHANT YRLESTLNYG LERVWTISSQ KGSNNVALGY DEGSIIIKLG
REEPAMSMDS NGKIIWAKHS EIQQANIKAM GDQDIKDGER LPLAVKDMGS CEIYPQAIAH
NPNGRFVVVC GDGEYIIYTA MALRNKSYGS AQEFAWSNDA SVYAIREGSS MVKIYKNFKE
LKSFKPDFGA EGIYGGFMLG VRSVSGLAFY DWDTTELIRR IEITPKSIVW SENGELVCIA
TEESFFILRY NPEAVENSKD NKDSVTEDGI EDAFEVIGEI EEVVKTGIWV GDCFIYTNSV
NRLNYYVGGE IVTVAHLDRV MYLLGYIPKE NRMYLGDKEL NVVSYSLLVS VLEYQTAVMR
RDFDTADKVL PTVPREQRTR VAHFLEKQGF KSQALAVTCD PEHKFELAIQ LGDLKIAYTL
AKEAESEQKW KQLSELAIKN CEFGLAQECL HQAQDFGGLM LLASSAGNRD MVERLGHTAE
KAGQNNVAFL SYFTLGRVEE CLDVLIKTGR LPEAAFFART YLPSQISRVV KLWRENLATI
NKKAAESLAD PTEYENLFPG LKEAFKVEQY LEPQRKAVIP AHKYPQVPQN SSRNAVEEMQ
AAEAEGRFDY EPVQRLSESE NLDTEESDKK DTELITPKSP PVSKPQPLLD PIKPEPVLDP
IKPEPVPTPK AAPVTKSQPS EPVSSRTAAE IEQELELDLD NLQIDDDIDT SDVNLDEDLL
ED
//
