ID A0A2A2KAL7_9BILA Unreviewed; 876 AA.
AC A0A2A2KAL7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=WR25_20924 {ECO:0000313|EMBL:PAV70948.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV70948.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV70948.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV70948.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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|PIRNR:PIRNR005727}; Peripheral membrane
CC protein {ECO:0000256|PIRNR:PIRNR005727}; Cytoplasmic side
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAV70948.1}.
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DR EMBL; LIAE01009154; PAV70948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2KAL7; -.
DR STRING; 2018661.A0A2A2KAL7; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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 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 PIRSF; PIRSF005727; Coatomer_beta_subunit; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 4: Predicted;
KW Cytoplasm {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|PIRNR:PIRNR005727};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Transport {ECO:0000256|PIRNR:PIRNR005727}.
FT DOMAIN 23..529
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 672..811
FT /note="Coatomer beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07718"
FT REGION 493..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 876 AA; 97938 MW; D7C1EB5C59933399 CRC64;
MSSELPCYTL IHTPTDIDLP SEAQLKEKFE KGADKDKIDA LKKLIYTILN GDKVSQGMLM
HVIRFCLPSN DHTLKKLLLI FWETVPKVNA QGKLLQEMIL VCDAYRKDLQ HPNEFVRGST
LRFLCKLKEP ELLEPLMPSI RQCLEHRHSY VRRNAVCAIF TIYKNFEFLI PDAPELVSNF
LEGEQDASCK RNAFMMLLHV DQARALDYLS GCIEQVTQFG DILQLIIVEL IYKVCHTNPA
ERARFIRCIY NLLQSNSAAV RYEAAGTLIT LSSAPAAIKA AATAYIDLIV KESDNNVKLI
VLDRLIDLRQ NSSNERVLQE LVMDILRVLS SPGFEVRQKT LNLALDLVSS RNVEDMVMFL
KKEISKSASE SADEADKYKQ ALVKTLHTAT IKFPDVAPTI IPVLLEFLSD ENETAATYVL
LFIREAIHKL PPLKQSILTS LQEGLLSIHK PKVFMAALWI LGTYCDTEPS ILALLRLIKQ
SLGELPIVES EMRELEGTGE EKKDADAPQD KKQTRQLVTA DGTYAAQSAI SSGPKSTVAE
KPPLRRFLLD GDFFLGASLA TILVKMSEQF TILNTVGAKD NSERANRFRA EAMFILASII
SLGKSGLAKN NVTEDDLDRM GTMIKVLALN MPNAREILLD ECKKSLELML ANQKMDRLED
SASSKKKNTV DVDKTICYSQ LAARTDASTG ENLFDLSLSQ ALGTAPKSHK FDFSSSKLGK
VIQLTGFSDP VYAEAYVNVN QYDIVLDVLI VNQTADTLQN ISLELSTVGD LKLVDKPMPI
TLAPADFTNI KATVKVASTE NGVIFSTISY DVKGSTSDRN CVYLQDIKVE SFIFVEEQIL
LLFEISLKHS SDSFRYFSTM TFSDRYNGLH RPRFGN
//
