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Database: UniProt
Entry: A0A024V895_PLAFA
LinkDB: A0A024V895_PLAFA
Original site: A0A024V895_PLAFA 
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
//
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