ID A0A024TD70_9STRA Unreviewed; 963 AA.
AC A0A024TD70;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Coatomer subunit beta {ECO:0000256|PIRNR:PIRNR005727};
DE AltName: Full=Beta-coat protein {ECO:0000256|PIRNR:PIRNR005727};
GN ORFNames=H310_13716 {ECO:0000313|EMBL:ETV91929.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV91929.1};
RN [1] {ECO:0000313|EMBL:ETV91929.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV91929.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-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: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}.
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DR EMBL; KI914006; ETV91929.1; -; Genomic_DNA.
DR RefSeq; XP_008879566.1; XM_008881344.1.
DR AlphaFoldDB; A0A024TD70; -.
DR STRING; 157072.A0A024TD70; -.
DR EnsemblFungi; H310_13716-t26_1; H310_13716-t26_1-p1; H310_13716.
DR EnsemblProtists; ETV91929; ETV91929; H310_13716.
DR GeneID; 20090766; -.
DR VEuPathDB; FungiDB:H310_13716; -.
DR eggNOG; KOG1058; Eukaryota.
DR OrthoDB; 151169at2759; -.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005727}.
FT DOMAIN 26..487
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 677..812
FT /note="Coatomer beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07718"
FT DOMAIN 818..945
FT /note="Coatomer beta subunit appendage platform"
FT /evidence="ECO:0000259|Pfam:PF14806"
SQ SEQUENCE 963 AA; 105753 MW; 5232E8A37B0138FB CRC64;
MATPSEKNCT ILLFSGVEKG GAQPPSQDEI LKGLESAKID DKIRSLKAAI VALLNGEKQP
RVLMQIIRFC STKEDHQLKK LLMIYWEIAT KYDEHGKLLP EMILVCNALL NDLNHANEYV
RGCMLRFLCK IKEKELLEPL KDAVKANLEH RHSYVRKNAV MTVYTMYKNF GDALIPDAPE
LIERFIVTES DSSARRNAYL MLFDCAETVA VNFLMNSMDQ IQKFGDGFSL VILELTRKVC
RVDPAQKARF IRCIFQLLQS SSAAVSYEAA WTLVTLSSAP TAVRAAAKTY AGLLNSQSDN
NVKLIVLDRL ADLKKHHTKV LQEVLMDILR ALSSPNLDIC KKVLDIAMNL VSPRNIDEVV
GHLKREVVKT QEKGRMDKAA GDDYRKLLIR SIHACAVKFP EVAHQVVHLL MDFLNSDGAM
DVVLFVRTMC ETYPDLRPSI VQKLMLSLGD IQSAKVFRVA LWVLGEYASD QPSADTAVHV
VVEAIVEVLG PLPFSNDVKP PVDKSATPAA KPVTKSVVLA DGTYATETSY AVDPAAVAAS
AGLSLRKLIL AGDFFLASTV SSSLTKLAVR AMTHDPASAA NGPVKSLVLT VLRYIVAFLS
YGQDAAASPL IELDEDSKRR MLVCVRILTD PTFFDRMATV LTKDCRAAYR AVLDDQASAA
AAAAAALGDA DAPQIEVDDL ISFRQLRGKK ALGSTDIDID DGADLSRATD GPNEYSGKLR
AVHQLTGFAD PVYAEAYVTV HAYDIVLDIL VMNRTPNTLN NLSVDLTPMG DLKLVERPAS
ITIGPLDSRT IRANIKVSST ETGHIFGTIV YESASGADKT YVNLNDIHLD IMDYIVPADC
GDTHFRSMWA EFEWENRVAV NTDITNVFAF LQHIVDKTNM RCMTPTASLG GDTHFLAANL
YAKSIFGEDA LVNLSVEKLD KGKIAGYIRI RSKTQGIALS LGDRITAVQR GHEEPSKRKK
VAA
//