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Database: UniProt
Entry: H2KQU2_CLOSI
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Original site: H2KQU2_CLOSI 
ID   H2KQU2_CLOSI            Unreviewed;      1009 AA.
AC   H2KQU2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Coatomer subunit beta' {ECO:0000256|PIRNR:PIRNR005567};
GN   ORFNames=CLF_104710 {ECO:0000313|EMBL:GAA38251.2}, CSKR_102765
GN   {ECO:0000313|EMBL:KAG5441137.1};
OS   Clonorchis sinensis (Chinese liver fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Clonorchis.
OX   NCBI_TaxID=79923 {ECO:0000313|EMBL:GAA38251.2, ECO:0000313|Proteomes:UP000008909};
RN   [1] {ECO:0000313|EMBL:GAA38251.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Henan {ECO:0000313|EMBL:GAA38251.2};
RX   PubMed=22023798; DOI=10.1186/gb-2011-12-10-r107;
RA   Wang X., Chen W., Huang Y., Sun J., Men J., Liu H., Luo F., Guo L., Lv X.,
RA   Deng C., Zhou C., Fan Y., Li X., Huang L., Hu Y., Liang C., Hu X., Xu J.,
RA   Yu X.;
RT   "The draft genome of the carcinogenic human liver fluke Clonorchis
RT   sinensis.";
RL   Genome Biol. 12:R107-R107(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Henan;
RA   Wang X., Huang Y., Chen W., Liu H., Guo L., Chen Y., Luo F., Zhou W.,
RA   Sun J., Mao Q., Liang P., Zhou C., Tian Y., Men J., Lv X., Huang L.,
RA   Zhou J., Hu Y., Li R., Zhang F., Lei H., Li X., Hu X., Liang C., Xu J.,
RA   Wu Z., Yu X.;
RT   "The genome and transcriptome sequence of Clonorchis sinensis provide
RT   insights into the carcinogenic liver fluke.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAG5441137.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Cs-k2 {ECO:0000313|EMBL:KAG5441137.1};
RX   PubMed=29454982;
RA   Wang D., Korhonen P.K., Gasser R.B., Young N.D.;
RT   "Improved genomic resources and new bioinformatic workflow for the
RT   carcinogenic parasite Clonorchis sinensis: Biotechnological implications.";
RL   Biotechnol. Adv. 36:894-904(2018).
RN   [4] {ECO:0000313|EMBL:KAG5441137.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Cs-k2 {ECO:0000313|EMBL:KAG5441137.1};
RX   PubMed=33677057;
RA   Young N.D., Stroehlein A.J., Kinkar L., Wang T., Sohn W.M., Chang B.C.H.,
RA   Kaur P., Weisz D., Dudchenko O., Aiden E.L., Korhonen P.K., Gasser R.B.;
RT   "High-quality reference genome for Clonorchis sinensis.";
RL   Genomics 0:0-0(2021).
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; DF143056; GAA38251.2; -; Genomic_DNA.
DR   EMBL; NIRI02000077; KAG5441137.1; -; Genomic_DNA.
DR   AlphaFoldDB; H2KQU2; -.
DR   STRING; 79923.H2KQU2; -.
DR   InParanoid; H2KQU2; -.
DR   Proteomes; UP000008909; Unassembled WGS sequence.
DR   Proteomes; UP000286415; Chromosome 7.
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; IPR016024; ARM-type_fold.
DR   InterPro; IPR006692; Coatomer_WD-assoc_reg.
DR   InterPro; IPR016453; COPB2.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
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; 2.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 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:UP000008909};
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          331..774
FT                   /note="Coatomer WD associated region"
FT                   /evidence="ECO:0000259|Pfam:PF04053"
FT   REGION          899..1009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        913..971
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1009 AA;  112979 MW;  AC6C0F38FD66BDE5 CRC64;
     MPLRLDIKRK LLARSDRVKA VDLHPTEPWI CAALYNGNVH VWNIEGQQLI KTLEVCTLPV
     RAVKFVARKN WIVTGSDDLQ LRVFNYNTLE RVQQIEAHSD YIRSIAVHPT QPFLLTASDD
     MLIRLWDWEK NWTCAQVFEG HSHYVMQLVF NPKDNNTFAS ASLDHTVKVW SLGSSSPNFT
     LEGHERGVNC VDYYIFGDKP YLASGADDKT VRIWDYQTKA CVQTLEGHAQ NISAVVFHPE
     LPIILTGSED GTVRVWHSGT YRLESTLNYG LERIWAMACY RGKQTVAIGY DEGTIVISLG
     RDEPAMSMDA SGKVVCARHT ELMQANLRSL TLGPGGVDDI QDGERLPVTF KDMGTSEIYP
     QTIEHNANGR FVAVCGDGEY IIYTAMALRN KTFGQAQEFV WSQADASMYA VRESNAIVKV
     YKQFKEVRTF KLDYGAEQIF GGHLLGVRSL TGLTFYDWNT GRLVRRIDIS PRSVYWNEGG
     QLVSLCTNET AFILRYAADA IPEAEPAPGS IEDTDGFEQA FQVVPNGEVN VAVHTGFWYG
     DAFLFTTTAN RLCYYVGGEL VTLAHLDRPM HLLGYLAKEN RVYLSDRDLQ IASYSLLLSV
     LEYETAVMRG DFSAADTIFP SIPKEQRTKV AQFLEKQGFR SQAMRVTTDV DHKFDLALQL
     GDLELCRDLA ADGDPEVNES KWKQLAEAAC RSCRFDLAEE CLARIKDYAS LLLLASSSGN
     GQMVKWIGDQ ASTESKDNVA FLARFLLSDL EGCLELLVKA DRLPEAAFFA RTYLPSHVPE
     IVELWREWLK KTTKSSSKVA QALANPQEYP NLFPGMENAL AAEKRMKMER AARSRLPAST
     YPSQPAMWER DVLSELHTKP EPLFESVPSH TLLNGGTLGS ESEANVARAS PTIEVMIASQ
     QNNAKPTLEE DNTPEEKDNE EEEEADEEEE EVDDEGDGED EDDDEDEEDE EEEEENGDAE
     EPEDDTLDAE LEQEIATLQL NKMKSKPTTA VAAPPSADAD WGDAGSDFE
//
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