ID A0A024V895_PLAFA Unreviewed; 1010 AA.
AC A0A024V895;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Coatomer subunit beta' {ECO:0000256|PIRNR:PIRNR005567};
GN ORFNames=PFFVO_02345 {ECO:0000313|EMBL:ETW18445.1};
OS Plasmodium falciparum Vietnam Oak-Knoll (FVO).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=1036723 {ECO:0000313|EMBL:ETW18445.1, ECO:0000313|Proteomes:UP000030690};
RN [1] {ECO:0000313|EMBL:ETW18445.1, ECO:0000313|Proteomes:UP000030690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vietnam Oak-Knoll (FVO) {ECO:0000313|Proteomes:UP000030690};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Annotation of Plasmodium falciparum Vietnam Oak-Knoll (FVO).";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW18445.1, ECO:0000313|Proteomes:UP000030690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vietnam Oak-Knoll (FVO) {ECO:0000313|Proteomes:UP000030690};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum Vietnam Oak-Knoll (FVO).";
RL Submitted (FEB-2013) 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 {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; KI925078; ETW18445.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024V895; -.
DR EnsemblProtists; ETW18445; ETW18445; PFFVO_02345.
DR Proteomes; UP000030690; 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; 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; 5.
DR PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
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|PIRNR:PIRNR005567};
KW Membrane {ECO:0000256|PIRNR:PIRNR005567};
KW Protein transport {ECO:0000256|PIRNR:PIRNR005567};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|PIRNR:PIRNR005567};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 95..130
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 186..229
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 230..262
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 324..805
FT /note="Coatomer WD associated region"
FT /evidence="ECO:0000259|Pfam:PF04053"
FT REGION 919..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1010 AA; 118230 MW; A1D359107A81A692 CRC64;
MPLNLDIKKK LNSRIGKVKC VDIHESENWI LASLYSGKLV IFDYVNQNTI KNIEVSVFPI
RCAKFIEKKQ WIICGGDDMT IRVYNYNTFE KIKSFEDHTD YIRYIEVHQT LPYILTSSDD
MTIKLYDYEN NFEKLCSFEN HIHYVMMCKF NPKDTYIFAS ASLDKTIKIW GVQNNTSVVT
KPHFTLSGHT KGVNCIDYSC SGETSYIISG SDDKTIRIWD YHTKQCIQVL SGHTQNISCV
IYHSNLPIIL SSSEDCNVKI WNSSMFKLES TLNYNMDRCW SLCAKKTKND LCIGYDEGLV
VIQIGSDVPI YTMFKNKIIY IKNTDIFIIN LQNVQEENYN DGDIYKVNKK ELGNCDFYPT
NVSFHPSGRF ICVNGHHEFN IYTSQVLRNK AYGKSSFFVW SHTGDYAIKD EGNKVSIYKD
FTSHHIFQTP YTITQLFGGY LLGVKSNNFI CFYDWSDYSL IRKIDINVKN VFWNDSGTYV
AISTEDSIYI LNYLNSDGNL SKDNINKNND TINNNNNSNN NGNIELIGVQ NRNINHPQHV
ENKMDEENYF QLESEINESI ESGIWIYDSF LYISKNLRLY IYTKKFIDIY AYIDKYLYIC
GYVYEYDRIF LLDKNFNFYS FFLPITYLQY QKYIMGQDFI AADNIMKNIP ESLYNKLSLF
LEKMGYKNKA LNICNDLEKK FELSLSIGNL QLCVDIINEL ERKENDSFVH NKYKKLGDTA
LVYNDIPMAI YCYKKTNDFS SLLIILSTLG DKIGIEELGQ MCLNHQKFNI AFICYFLLHK
INKCIHILLS NNNFAYAAFF SRVYKPSLLP TILKKWKEHL NKVYPNIPVN LLNPEENPEY
FPDYDKAVEC EKIFDKVNTI GSTKNYNTLK TLIDLNIVEE IKEIGYDKVE DIFIKQFNEE
LEKDIQNFDQ NGKIFLTEES KNKNVNQKED NKEINKENNK DDNKDDNKEN NKEDNKEYNK
EDDKEDDKED DKFCKMEDTE LLSNIQIQED NKNINSYSIN SNQSMDEELL
//