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Database: UniProt
Entry: A0A314Y8U5_PRUYE
LinkDB: A0A314Y8U5_PRUYE
Original site: A0A314Y8U5_PRUYE 
ID   A0A314Y8U5_PRUYE        Unreviewed;       951 AA.
AC   A0A314Y8U5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE   AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN   ORFNames=Pyn_22694 {ECO:0000313|EMBL:PQQ01259.1};
OS   Prunus yedoensis var. nudiflora.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=2094558 {ECO:0000313|EMBL:PQQ01259.1, ECO:0000313|Proteomes:UP000250321};
RN   [1] {ECO:0000313|EMBL:PQQ01259.1, ECO:0000313|Proteomes:UP000250321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jeju island {ECO:0000313|Proteomes:UP000250321};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PQQ01259.1};
RA   Baek S., Kim J.-H., Choi K., Kim G.-B., Cho A., Jang H., Shin C.-H.,
RA   Yu H.-J., Mun J.-H.;
RT   "Draft genome of wild Prunus yedoensis var. nudiflora.";
RL   Submitted (FEB-2018) 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: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|ARBA:ARBA00004255,
CC       ECO:0000256|PIRNR:PIRNR005727}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR005727};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255,
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}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
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:PQQ01259.1}.
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DR   EMBL; PJQY01001586; PQQ01259.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A314Y8U5; -.
DR   STRING; 2094558.A0A314Y8U5; -.
DR   Proteomes; UP000250321; 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   InterPro; IPR029446; COPB1_appendage_platform_dom.
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   Pfam; PF14806; Coatomer_b_Cpla; 1.
DR   PIRSF; PIRSF005727; Coatomer_beta_subunit; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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|ARBA:ARBA00022927,
KW   ECO:0000256|PIRNR:PIRNR005727};
KW   Reference proteome {ECO:0000313|Proteomes:UP000250321};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT   DOMAIN          21..524
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          671..809
FT                   /note="Coatomer beta subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07718"
FT   DOMAIN          816..943
FT                   /note="Coatomer beta subunit appendage platform"
FT                   /evidence="ECO:0000259|Pfam:PF14806"
SQ   SEQUENCE   951 AA;  106243 MW;  8E28877F6DE9C623 CRC64;
     MMEKSCTLLV HFDKGTPALA NEIKEALEGN DVELKIEALK KAIMLLLNGD TIPQLFITII
     RYVLPSEDHT VQKLLLLYLE IIEKTDSKGK ILPEMILICQ NLRNNLQHPN EYIRGVTLRF
     LCRLNEAEII EPLIPSILSN LEHRHPFVRR NAVLAIMFVY RLPQGETLLD SAPEIIDRFL
     ASEQDPSSKR NAFLMLFNCA QDRAVNYLFT HIGRIIEWGE QLQMVVLELI KKVCRVNKGE
     KSKYIKIIIS LLDAPSSAVV YECAGTLVSL SSAPTAIKAA ANTYSQLLLS QSDNNVKLIL
     LDRISELKAS HREIMVELVM DVLRALSSPN VDIRRKTLDI VLDLITPRNI NQVVMMLKKE
     VVKTQSGELE KNGEYRQMLV QAIYACAVKF PEVASTVVHP LMDFLGDTNV ASALDVAVFV
     REIIETNPKL RVSIITRLLD TFYQIRNSRV CTHALWIIGE YCLSLSEVES GIETIKQCLG
     ELPFYTASEE KEAQDATKNS QVVSSTTVSS RRPVILADGT YATQSAALET AMSAPVLVQG
     SLASVGNLRS LILSGDFFLE TVVACTLTKL VLRLEEIQPS KAEVNKATTQ ALLIMVSMLQ
     LGQSSVLPHP IDNDSRDRIV LCIRLLCHKG EEVRKIWLES CRQSFVKMLA DKQLLETEET
     KAKAQILSAQ PDDLIDFYHL KSRKGMSQLE LEDAVQDDLK RATGEFTKDR DDANKLNRIL
     QLTGFSDPVY AEAYVTVNHY DIVLDVTVIN RTKETLQNLC LELATMGDLK LVERPQNYTL
     APESSKQIKA NIKVSSTETG VIFGNIVYET SSNVLERTVI VLNDIHIDIM DYISPASCAD
     VSFRTMWAEF EWENKVAVNT VIQDEKEFLN HVVKATNMKC LTPPLALEGE CGVLAANLYA
     KSVFGEDALV NVSVEKQADG KLSGYIRIRS KTQGIALSLG DKITLKQKGG V
//
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