(data stored in ACNUC7421 zone)

SWISSPROT: Q758F5_ASHGO

ID   Q758F5_ASHGO            Unreviewed;       932 AA.
AC   Q758F5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 115.
DE   RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN   ORFNames=AGOS_AEL193W {ECO:0000313|EMBL:AAS52492.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52492.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52492.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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:PIRNR037093}.
CC   -!- SUBUNIT: Oligomeric complex. {ECO:0000256|PIRNR:PIRNR037093}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037093}. Golgi
CC       apparatus membrane {ECO:0000256|PIRNR:PIRNR037093}; Peripheral membrane
CC       protein {ECO:0000256|PIRNR:PIRNR037093}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR037093}. Cytoplasmic vesicle, COPI-coated
CC       vesicle membrane {ECO:0000256|PIRNR:PIRNR037093}; Peripheral membrane
CC       protein {ECO:0000256|PIRNR:PIRNR037093}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR037093}.
CC   -!- SIMILARITY: Belongs to the COPG family.
CC       {ECO:0000256|PIRNR:PIRNR037093}.
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DR   EMBL; AE016818; AAS52492.1; -; Genomic_DNA.
DR   RefSeq; NP_984668.1; NM_210021.1.
DR   STRING; 33169.AAS52492; -.
DR   EnsemblFungi; AAS52492; AAS52492; AGOS_AEL193W.
DR   GeneID; 4620851; -.
DR   KEGG; ago:AGOS_AEL193W; -.
DR   HOGENOM; HOG000184434; -.
DR   InParanoid; Q758F5; -.
DR   KO; K17267; -.
DR   OMA; PVNARKC; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IEA:EnsemblFungi.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:EnsemblFungi.
DR   Gene3D; 1.25.10.10; -; 2.
DR   Gene3D; 2.60.40.1480; -; 1.
DR   Gene3D; 3.30.310.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR   InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR   InterPro; IPR032154; Coatomer_g_Cpla.
DR   InterPro; IPR017106; Coatomer_gsu.
DR   InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
DR   InterPro; IPR037067; Coatomer_gsu_app_sf.
DR   InterPro; IPR012295; TBP_dom_sf.
DR   PANTHER; PTHR10261; PTHR10261; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF16381; Coatomer_g_Cpla; 1.
DR   Pfam; PF08752; COP-gamma_platf; 1.
DR   PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF49348; SSF49348; 1.
DR   SUPFAM; SSF55711; SSF55711; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q758F5.
DR   SWISS-2DPAGE; Q758F5.
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR037093};
KW   Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR037093};
KW   ER-Golgi transport {ECO:0000256|PIRNR:PIRNR037093};
KW   Golgi apparatus {ECO:0000256|PIRNR:PIRNR037093};
KW   Membrane {ECO:0000256|PIRNR:PIRNR037093, ECO:0000256|SAAS:SAAS00468874};
KW   Protein transport {ECO:0000256|PIRNR:PIRNR037093,
KW   ECO:0000256|SAAS:SAAS00299732};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transport {ECO:0000256|PIRNR:PIRNR037093, ECO:0000256|SAAS:SAAS00468876}.
FT   DOMAIN          30..565
FT                   /note="Adaptin_N"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          669..814
FT                   /note="COP-gamma_platf"
FT                   /evidence="ECO:0000259|Pfam:PF08752"
FT   DOMAIN          817..929
FT                   /note="Coatomer_g_Cpla"
FT                   /evidence="ECO:0000259|Pfam:PF16381"
FT   REGION          633..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..652
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   932 AA;  103513 MW;  528B50D6D111E9C8 CRC64;
     MSTHTYKSGF RVTVSNKAPE EAQAGHLPDK MTVYQDCLNE FNESPVKPAR CRMLIGKLLK
     LLSHGETFPA NESTALFFSI SKLFQHPNNS LRQAVYLALK ELCRNSEDVL MATSSVMKDV
     QNGTDLVKPN AIRALTRVLD ASTAFSAERL YKSAVVSKDP SISSAALVSS YHMLPIAEST
     VKRYANETQE AVSDLKTYPH SAGPTDFYRV SSYISQYHAL GLLYKLKSHD KIAMMKLIQQ
     FSANNVLRNQ LAQVQMVRLV HELLRMDNQL VPQFVPQLQS WLTSRYDAVK LEACKLISSL
     NSYMPSDIHT AMIHTLQGML SVPQVCSRFA AVRLLNSISM TAPEKVIICN PELESLINDS
     NRNISTYAIT TLLKTGTSKN ISSLIKTITK FIHEVSDDFK VIIIDAIRTL SLKFPDEWKN
     ILSFLIDTLK SAEGGYTFKN NIVDALFDLI QHVPQSREQA LEHLCDFIED CEFNEISVRI
     IYLLGKEGPS TEKPSLYVRH HYNRVVLENS IIRSAAVSAL SKFSSPKKDP SLAYSIEKLL
     KGIQTDEDDE VRDRATILVK LLEENKEKPG VADEFIQPKH SYDLHALESK LTNYLHHNED
     GFATPFDASS IPKYTEEELK AINLKQKQQQ FFANAEPSNS GKKTSGSDPK LSASATDIAA
     EAVQPSSIDY AEQLSSIEEF ASYGAIIHSS KPIPLTEPEA EFTVAGVKHL FQDHLVLQFN
     ITNTLTDVAL DKVTVICTPE EDAEMTELCA IPLDRLLPGD TGSCFISYEK PTATTVGFFN
     NLNFTTLELD PATNAPFEGD EGFQDEYEID ALYLQPGDYI KSVFVGDFAA TFEELPHEEV
     AVYNLSQSGA SLQDIVNKLV LSTNCLPLEN SQFVSTESNS AVVKLFGKHI TSEDRVALLV
     RLIKSTKGIA LKVQCKSDSA ELCGDLANGL VL
//

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