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Database: UniProt
Entry: A0A1Y1WGI0_9FUNG
LinkDB: A0A1Y1WGI0_9FUNG
Original site: A0A1Y1WGI0_9FUNG 
ID   A0A1Y1WGI0_9FUNG        Unreviewed;      1170 AA.
AC   A0A1Y1WGI0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Coatomer subunit alpha {ECO:0000256|PIRNR:PIRNR003354};
GN   ORFNames=DL89DRAFT_265851 {ECO:0000313|EMBL:ORX72244.1};
OS   Linderina pennispora.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX   NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX72244.1, ECO:0000313|Proteomes:UP000193922};
RN   [1] {ECO:0000313|EMBL:ORX72244.1, ECO:0000313|Proteomes:UP000193922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX72244.1,
RC   ECO:0000313|Proteomes:UP000193922};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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.
CC       {ECO:0000256|PIRNR:PIRNR003354}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits.
CC       {ECO:0000256|PIRNR:PIRNR003354}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR003354}. Golgi
CC       apparatus membrane {ECO:0000256|ARBA:ARBA00004255,
CC       ECO:0000256|PIRNR:PIRNR003354}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR003354};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}. 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:ORX72244.1}.
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DR   EMBL; MCFD01000003; ORX72244.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1WGI0; -.
DR   STRING; 61395.A0A1Y1WGI0; -.
DR   OrthoDB; 20819at2759; -.
DR   Proteomes; UP000193922; Unassembled WGS sequence.
DR   GO; GO:0030126; C:COPI vesicle coat; IEA:UniProtKB-UniRule.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   CDD; cd22948; Coatomer_WDAD_alpha; 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; IPR047312; Coatomer_alpha_WD-assoc_reg.
DR   InterPro; IPR016391; Coatomer_asu.
DR   InterPro; IPR010714; Coatomer_asu_C.
DR   InterPro; IPR006692; Coatomer_WD-assoc_reg.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
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:SF1; COATOMER SUBUNIT ALPHA; 1.
DR   Pfam; PF04053; Coatomer_WDAD; 1.
DR   Pfam; PF06957; COPI_C; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PIRSF; PIRSF003354; Coatomer_alpha_subunit; 2.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF101908; Putative isomerase YbhE; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 4.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR003354};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW   ECO:0000256|PIRNR:PIRNR003354};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|PIRNR:PIRNR003354};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR003354};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|PIRNR:PIRNR003354};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193922};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR003354};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   REPEAT          7..48
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          49..90
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          104..126
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          127..161
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          203..244
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          247..288
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          383..720
FT                   /note="Coatomer WD associated region"
FT                   /evidence="ECO:0000259|Pfam:PF04053"
FT   DOMAIN          770..1168
FT                   /note="Coatomer alpha subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06957"
SQ   SEQUENCE   1170 AA;  130657 MW;  B1AD18530534FD09 CRC64;
     MQMLTKFETK SSRVKGVAFH PKRPWILASL HNGSIQLWDY RMGTLLERFE EHEGPVRGIS
     FHPSQELFVS GGDDYKVKVW NYRTRRCLFT LQGHLDYVRT ARWIITASDD QTIRIWNWQS
     RQCIAVLTGH NHYVMSAEFH PTEDLVVSAC LDQTVRVWDI SGLRQKSAAG AQPVMMADPL
     ASQRMGAQGD FFNATDVVVK FVLEGHTRGV NWATFHPTMP LILSCGDDRQ IKIWRMNDSR
     AWEVDTCRGH YNNVNSALFH PKREFILSDS EDKTIRVWDT TRRTLLATFR REQDRFWCLT
     AHPELNLFAA GHDNGLIVFK LERERPAAAS HHNNLLYVRE SQIRIHDFAN NNDAAMIAIR
     SAPAGQYLPP PRSMSFNPAE KAARRGTGTS AIWTGRNRFA VLDKAQQQIL IKDLTNQTTK
     TIQPPVTVEA IFPAPGSQIL LATATSVVLY DVQTRQMLGE ISAAPVKYVV WSSDMSSVAL
     LCKHTITLAN KHLEQLCQVH ETIRIKSAVW DDSGVLLYTT LNHIKFALPQ GDTGTIRTID
     NPIYLVRVKG GDVHCLDREG KVQVIKVDPT EYRFKLALVH RNYEEVSIIA YLQQKGYPEI
     ALHFVRDDTA RFELALEQPK PSDKPAYWDK FSQEALRRGH VQMVELAYQR NKAYDRLSFL
     YSVTGNITKL GKMQKIAVMR NDLQSRLQNA LYLGDAEERV RVLRESGQLS LAYLTAKTHG
     LAEEAEAIRE AAGIDEASIT GVPTKSSLLQ PATPILPAAD LDWPQLRVSK GIFDGKFNFG
     DKGAAGPQPG KSRVADLATA DGNDVEEDAG AWGIDEDDDV AGDSRAAAAA GRFDDEDLLD
     DDAEEGWGLE DEGELDAELT AEATAAAAAD FVAPQPGTSE LEQWSRNSQL AADQIAAGNF
     EQAMKLLRDQ VGIVSFEALK PAFLEIYSAS RAVLTTTPSS EPMRAEATQA SEYLPVQIYS
     LTTSLELLQQ AYREMTAGKF EDAQTLFRRL LLSLIFVTVD SSEDAKEVKE LLQISREYVL
     ACTVEMERAA LAKQEAGEEN DTRVVELAAY FTHCQMRADH EKLALRSAMN IAYKGKCFIA
     AGEFAQRLLD LVPSPKIADR ARKIIALCDR QSVNTLSIEY DARNPFSLCA ASHKPINRGD
     ASVECPYCQA VYTPEFNGSV CQVCQIAEAA
//
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