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Database: UniProt
Entry: A0A3D8RR90_9EURO
LinkDB: A0A3D8RR90_9EURO
Original site: A0A3D8RR90_9EURO 
ID   A0A3D8RR90_9EURO        Unreviewed;       949 AA.
AC   A0A3D8RR90;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE   AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN   ORFNames=DSM5745_06472 {ECO:0000313|EMBL:RDW76480.1};
OS   Aspergillus mulundensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW76480.1, ECO:0000313|Proteomes:UP000256690};
RN   [1] {ECO:0000313|EMBL:RDW76480.1, ECO:0000313|Proteomes:UP000256690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW76480.1,
RC   ECO:0000313|Proteomes:UP000256690};
RX   PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA   Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA   Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA   De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA   Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA   Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA   Xiong C., Yue Q., Zhang X.;
RT   "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT   Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT   basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT   Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT   and Morchella septimelata.";
RL   IMA Fungus 9:199-223(2018).
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:RDW76480.1}.
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DR   EMBL; PVWQ01000007; RDW76480.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8RR90; -.
DR   STRING; 1810919.A0A3D8RR90; -.
DR   OrthoDB; 151169at2759; -.
DR   Proteomes; UP000256690; 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:UP000256690};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT   DOMAIN          20..491
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          673..809
FT                   /note="Coatomer beta subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07718"
FT   DOMAIN          814..940
FT                   /note="Coatomer beta subunit appendage platform"
FT                   /evidence="ECO:0000259|Pfam:PF14806"
SQ   SEQUENCE   949 AA;  105706 MW;  66F55D07B6087ED1 CRC64;
     MASFLENSYS LVHLDNTADQ PSQQELKLQL EKGNDETKMD TMRRIITIML NGDPMSGLLM
     HIIRFVMPSK SKPLKKLLYF YYEICPKHDS SGKLKQEMIL VCNGIRNDLQ HPNEYIRGNT
     LRFLCKLREP ELIEPLLSSA RSCLDHRHAY VRKSAVWAIS SIFQHSESLI PDAPELIQAF
     LETESDGTCK RNAFAALMSI SHQAALEYLA STFDSIPNTD ELLQLAELEF IRKDAVQNSQ
     NKARYLRLIF DLLDASTSTV VYEAATSLTA LTSNPVAVKA AAGKLIELSI KEADNNVKLI
     VLDRVDQLRI RNEGVLDELT MEILRVLSSP DIDVRRKALG IALEMVSSKN VEEIVMLLKK
     ELSKTVDEQY EKNSEYRQLL IQSIHNCAIK FSEIAASVVD LLMDFIADFN NNSAVDVISF
     VKEVVEKFPK LRASIVDRLV STLSEVRAGK VYRGVLWVVG EYSLEERDIR EAWKKIRASL
     GEIPILASEQ RLLEEVPEDT LPKEQINGHK SAPKVLADGT YATESALTSQ SAAAARLQAV
     KAAQKPPLRQ LILDGDYYLA TVLSSTLTKL VMRHSEVSED SARTNALRAE AMLIMISIIR
     VGQSPFVAAP IDEDSVDRIM TCVRSLAEFS ERKELETTFL EDTRKAFRAM VQVEDKKRAA
     KEAVEKAKTA VQIDDAIPIR QFTKKSALEG AEEIELDLAK ATGGDSTVET VSSKLSRVVQ
     LTGFSDSVYA EAYVTVHQFD IVLDVLLVNQ TVETLQNLSV EFATLGDLKV VERPTTHNLG
     PRDFLNVQAT VKVSSTDTGV IFGNIVYDGA SSTETHVVIL NDIHADIMDY IQPAHCTETQ
     FRTMWTEFEW ENKVNINSKA KTLREFLKQL MESTNMACLT PEASLTGDCR FLSANLYARS
     VFGEDALANL SIEKEGDDGP VTGFVRIRSR SQGLALSLGS LKGLKASTA
//
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