ID F2SU57_TRIRC Unreviewed; 1212 AA.
AC F2SU57;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Coatomer subunit alpha {ECO:0000256|PIRNR:PIRNR003354};
GN ORFNames=TERG_06007 {ECO:0000313|EMBL:EGD89769.2};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD89769.2, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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}. Cytoplasmic vesicle,
CC COPI-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004347};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004347};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004347}. 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; GG700654; EGD89769.2; -; Genomic_DNA.
DR AlphaFoldDB; F2SU57; -.
DR STRING; 559305.F2SU57; -.
DR VEuPathDB; FungiDB:TERG_06007; -.
DR InParanoid; F2SU57; -.
DR OMA; EMTYQKQ; -.
DR OrthoDB; 20819at2759; -.
DR Proteomes; UP000008864; 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; IPR011048; Haem_d1_sf.
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; 5.
DR PIRSF; PIRSF003354; Coatomer_alpha_subunit; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
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:UP000008864};
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 33..74
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 75..116
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 117..158
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 192..233
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 236..277
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 331..759
FT /note="Coatomer WD associated region"
FT /evidence="ECO:0000259|Pfam:PF04053"
FT DOMAIN 838..1206
FT /note="Coatomer alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06957"
FT REGION 824..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1212 AA; 135717 MW; 2E0A9776C2DEBAEA CRC64;
MLTDPSRPWL LVALHSSTIQ LWDYRMGTLI DRFEEHDGPV RGVDFHKTQP LFVSAGDDYK
IKVWSLQSRR CLFTLNGHLD YVRTVFFHHE LPWIISSSDD QTIRIWNWQN RSLICTMTGH
NHYTMCAQFH PKDDLVVSAS LDQTVRVWDI SGLRKKHSAP SSTMAFEEQM ARSNPAQADM
FGNTDAVVKF VLEGHDRGVN WVAFHPTLPL IVSAGDDRLI KLWRMSETKA WEVDTCRGHF
QNASACIFHP HQDLILSAGE DKTIRVWDLN KRTAVQSFKR DADRFWMIAA HPEINLFAAG
HDTGVMVFKL ERERPASALY QNQVFYITKD KHLRSYDFTK NTESPAMLSL KKLGSPWVPA
RTLSYNPAER AILVTSPTDN GTYELIHIPR DSTGAVEPTD VKRGHGNSAV FVARNRFAVF
TQSTQQIDIK DLSNSTTKTI KASHGTTDIH FGGTSCLLLL TPTSVVLLDI QQKKQLAELS
VSGVKYVVWS NDGLYVALLS KHNVTIATKS LEHVSTLHET IRIKSACWDD SGVLLYSTLN
HVKYSLLNGD NGIVCTLDQT LYLVRVKARK VYCLDRTAKP TVLAIDPTEY RFKLSLVKRN
YEEMLQIIKT SSLVGQSIIS YLQKKGYPEI ALQFVQDPQT RFELALECGN IDVAIEMAKT
LDRPKLWARL GTEALAHGNN QTVEMTYQRQ RNFDKLSFLY LTTGDQEKLS RMAKIAQHRG
DFTSQFQNAL YLDDVEARIQ MFKEIDLLPL AYLTAKTHGF AEEAQSILKA SGVSEDQITL
PTLGEPKPAP NVVVQTFKSN WPVKAPSHSS FEKALLGEVG GADDEGVNGF EDQDGERENG
GVEIGLGDEQ EEEDVAGWDM GDDIQIEEET DLLGTENVES GPSSSEAELW SRNSPLAADH
VAAGSFESAM QLLNRQVGAV NFEPLKPRFL EIYQASKTYL PATPALPPII NYVRRTVDET
DTRRLLPIIP RSLETIASVD LQEGYAAMRS NKLQDGIVIF QRILHSILVN TVSSEAHVTE
AKKIISTARE YILAMSMELE RRALPTDTPE NLKRSLELSA YFTIPKLEVA HRQLALMAAM
KFAYTNQNFS SALSFANRMI ANGGSAKLLD QVSPFFIPSL YLLLTSKQAK KIKAQCERNP
QDAIEIEFDQ FAEFDICAAS HTPIYGGSPS VTCPYTGTKY HEQHKGSVCT VCKVSAVGAP
ASGLRLFVPG QH
//
