COPG_SCHPO
ID COPG_SCHPO Reviewed; 905 AA.
AC P87140;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Probable coatomer subunit gamma;
DE AltName: Full=Gamma-coat protein;
DE Short=Gamma-COP;
GN Name=sec21; ORFNames=SPAC57A7.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC originating from it. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
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DR EMBL; CU329670; CAB08768.1; -; Genomic_DNA.
DR PIR; T38944; T38944.
DR RefSeq; NP_593371.1; NM_001018803.2.
DR AlphaFoldDB; P87140; -.
DR SMR; P87140; -.
DR BioGRID; 278717; 4.
DR STRING; 4896.SPAC57A7.10c.1; -.
DR iPTMnet; P87140; -.
DR MaxQB; P87140; -.
DR PaxDb; P87140; -.
DR PRIDE; P87140; -.
DR EnsemblFungi; SPAC57A7.10c.1; SPAC57A7.10c.1:pep; SPAC57A7.10c.
DR GeneID; 2542247; -.
DR KEGG; spo:SPAC57A7.10c; -.
DR PomBase; SPAC57A7.10c; sec21.
DR VEuPathDB; FungiDB:SPAC57A7.10c; -.
DR eggNOG; KOG1078; Eukaryota.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; P87140; -.
DR OMA; YMTQYHA; -.
DR PhylomeDB; P87140; -.
DR Reactome; R-SPO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SPO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:P87140; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030126; C:COPI vesicle coat; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
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: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; ISO:PomBase.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISO:PomBase.
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 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..905
FT /note="Probable coatomer subunit gamma"
FT /id="PRO_0000193860"
FT REPEAT 265..302
FT /note="HEAT 1"
FT REPEAT 303..340
FT /note="HEAT 2"
FT REPEAT 374..412
FT /note="HEAT 3"
FT REPEAT 414..450
FT /note="HEAT 4"
FT REPEAT 525..563
FT /note="HEAT 5"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 905 AA; 100936 MW; 1E2802CC76819573 CRC64;
MSYSKKDDDG DESIFANVNQ VTVTQDARAF NSSSISPRKS RRLLSKIAYL IYTGEHFQEK
QATELFFGIT KLFQHKDPSL RQFVYIIIKE LSVVAEDVIM ITSSIMKDTA TGRETIYRPN
AIRSLIRVID ANTVPAIERI LTTGIVDPIS AVASAALVSA YHLYPVAKDI VSRWNNEVQD
AVTSHNVGRK VASSPFFTST LGYTPNASGI SQYHALGLLY RIRRHDSIAM NKLLQLLVSN
LGTVSNSHAF VMLIRYISSL MDQNTQFRDQ MVPFLHGWLK SKGDMVNLEV ARNMVRLKNI
SDDDLQPVVS VLKIFLSSHR SATRFSAIRT LNELAMTRPH LVHSCNLNIE SLITDVNRSI
ATYAITTLLK TGNDESVDRL MKQIVTFMSD ISDNFKIIVV DAIRSLCLKF PRKQDSMLTF
LSNILCDEGG YEFKRAAVDA ISDMIKYIPE SKERALAELC EFIEDCEYPK IAVRILSILG
EEGPKASEPT RFIRYIYNRI MLENAIVRSA AVSALTKFGL NAEDKFVQRS VKVILTRCLE
DADDEVRDRA AFSVKALEDR DAFLPVVKSD KIPSLPALER SLVIYISERK FGQGFDIKSV
PVLSQEEIDA ENLRIKKATT EVEFTEVTPA EDQNALASSN IETEFLNALE SVSEFNEYGP
VLKSSPSPIE LTEQETEFVV KVVKHVFKDH LVVQFQLHNT LSEVILENAV VVSTPSTDDL
VEECVVPAAI VSGEPVSIFV SFKFNDSVPY PLTTLTNTLQ FTTKEIDIHT GEPEEEGYED
EYKIDDLDVS AGDFISPAYE SNFDGLFDSL EHEASEVYVL SLLDSFRSTC SRVAELLQMQ
PLEGTENPTD KPVHVMKLSG KLVNGEKVLA LVKMAHSKDG EGITIKVIAR GESDSSVELV
VGGIA
