(data stored in SCRATCH zone)

SWISSPROT: Q6FJU5_CANGA

ID   Q6FJU5_CANGA            Unreviewed;       932 AA.
AC   Q6FJU5;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 91.
DE   RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN   OrderedLocusNames=CAGL0M03531g {ECO:0000313|CGD:CAL0136665,
GN   ECO:0000313|EMBL:CAG62475.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62475.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: The coatomer is a cytosolic protein complex that binds
CC       to dilysine motifs and reversibly associates with Golgi non-
CC       clathrin-coated vesicles, which further mediate biosynthetic
CC       protein transport from the ER, via the Golgi up to the trans Golgi
CC       network. Coatomer complex is required for budding from Golgi
CC       membranes, and is essential for the retrograde Golgi-to-ER
CC       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}.
CC       Golgi apparatus membrane {ECO:0000256|PIRNR:PIRNR037093};
CC       Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR037093};
CC       Cytoplasmic side {ECO:0000256|PIRNR:PIRNR037093}. Cytoplasmic
CC       vesicle, COPI-coated vesicle membrane
CC       {ECO:0000256|PIRNR:PIRNR037093}; Peripheral membrane protein
CC       {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; CR380959; CAG62475.1; -; Genomic_DNA.
DR   RefSeq; XP_449499.1; XM_449499.1.
DR   ProteinModelPortal; Q6FJU5; -.
DR   STRING; 284593.XP_449499.1; -.
DR   EnsemblFungi; CAG62475; CAG62475; CAGL0M03531g.
DR   KEGG; cgr:CAGL0M03531g; -.
DR   CGD; CAL0136665; CAGL0M03531g.
DR   EuPathDB; FungiDB:CAGL0M03531g; -.
DR   eggNOG; KOG1078; Eukaryota.
DR   eggNOG; COG5240; LUCA.
DR   HOGENOM; HOG000184434; -.
DR   InParanoid; Q6FJU5; -.
DR   KO; K17267; -.
DR   OMA; SPYAVCM; -.
DR   OrthoDB; EOG092C0K4D; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0030126; C:COPI vesicle coat; IEA:EnsemblFungi.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005768; C:endosome; IEA:EnsemblFungi.
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:ER to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IEA:EnsemblFungi.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 2.60.40.1480; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR   InterPro; IPR013041; Coatomer/clathrin_app_Ig-like.
DR   InterPro; IPR032154; Coatomer_g_Cpla.
DR   InterPro; IPR017106; Coatomer_gsu.
DR   InterPro; IPR013040; Coatomer_gsu_app_Ig-like-sub.
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; Q6FJU5.
DR   SWISS-2DPAGE; Q6FJU5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
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,
KW   ECO:0000256|SAAS:SAAS00101884};
KW   Protein transport {ECO:0000256|PIRNR:PIRNR037093,
KW   ECO:0000256|SAAS:SAAS00468902};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Transport {ECO:0000256|PIRNR:PIRNR037093,
KW   ECO:0000256|SAAS:SAAS00299740}.
FT   DOMAIN       20    559       Adaptin_N. {ECO:0000259|Pfam:PF01602}.
FT   DOMAIN      668    816       COP-gamma_platf. {ECO:0000259|Pfam:
FT                                PF08752}.
FT   DOMAIN      819    931       Coatomer_g_Cpla. {ECO:0000259|Pfam:
FT                                PF16381}.
SQ   SEQUENCE   932 AA;  103694 MW;  8AEB960FB2319E1D CRC64;
     MSTSTYKKFE QAGSSDLPDK MTIYQDCMNT FNETPVNPKR CRLLISRLLR LLAQGETFPR
     NEATALFFSI SKLFQYPNDS LRQLVYLAIK EFSGISEDVL MATSSIMKDV QNGSDLVKPN
     AIRSLTNVLD ESTAFSAERL LKSALVSKHP SISSAALCTS YHLLPISEVT VKRFTNETQE
     AVVDLKQFPS SSMNGEYYPN STYITQYHAL GLLYQLKKND KMALLKLVRQ FSEGNVLKNQ
     LAKVELVRIV SELIQKDPQL FTQFKPLLNN WLSNKFESVQ LETAKMITSF AIHNPRLVSP
     ELYAAAISAL QSLLSVPRVS TRFATLRILN RISMISPEKI AICNPELESL VNDSNRNIST
     YAITTLLKTG TAKNISSLIH TITRFIHDVS DDFKIIIVDA VRTLSLNFPQ EWKSIVTFLI
     DVLKNSEGGF KYKNSIVEAL IDIVSFVPQS KELALENLCD FIEDCEYNEI LVRILHLLGK
     EGPSTTNPSL YVRHIYNRVV LENSIIRSAA VVALSKFALT KNDSTLCESI ISLLKRIVHD
     KDDEVRDRAS IALKFIEAAK EKNDKVANDL IQSSSAYDLS SLESKLSAYL SSNTDSFQTP
     FDSQSIPKYA EDELKAMELK KKQEKIFENK GDKTRDSSKT ESTSNSAGEN FNAEAEYDDG
     KDDLLAAKYA EEMAAIPEIN AFGSIVNTTK AVPLTEPEAE FVVTGIKHLF ADHVVIQFNI
     RNTLTDVILD NVSVSCVPEE SGDVTLEEQF TIPIDRLLPS AESSCYVAFK KPEAIVTETF
     MNSINFTTRE VNPDTNEPFE GDEGFEDEYE IDPITLSGGD YVKSSFVGNF TSAFDELPHE
     EIAVYNIQED ISIQEVVDKV IQNTSCLPLG STQYVGGDSN SHTLKLFGKS ALTGSKIGML
     VKFIKSSKGV ALKVQGKAED ATLCADLVNS VI
//

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