ID K3WPR6_GLOUD Unreviewed; 916 AA.
AC K3WPR6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
OS Globisporangium ultimum (strain ATCC 200006 / CBS 805.95 / DAOM BR144)
OS (Pythium ultimum).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Pythiales; Pythiaceae;
OC Globisporangium.
OX NCBI_TaxID=431595 {ECO:0000313|EnsemblProtists:PYU1_T006958, ECO:0000313|Proteomes:UP000019132};
RN [1] {ECO:0000313|Proteomes:UP000019132}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DAOM:BR144 {ECO:0000313|Proteomes:UP000019132};
RX PubMed=20626842; DOI=10.1186/gb-2010-11-7-r73;
RA Levesque C.A., Brouwer H., Cano L., Hamilton J.P., Holt C., Huitema E.,
RA Raffaele S., Robideau G.P., Thines M., Win J., Zerillo M.M., Beakes G.W.,
RA Boore J.L., Busam D., Dumas B., Ferriera S., Fuerstenberg S.I.,
RA Gachon C.M., Gaulin E., Govers F., Grenville-Briggs L., Horner N.,
RA Hostetler J., Jiang R.H., Johnson J., Krajaejun T., Lin H., Meijer H.J.,
RA Moore B., Morris P., Phuntmart V., Puiu D., Shetty J., Stajich J.E.,
RA Tripathy S., Wawra S., van West P., Whitty B.R., Coutinho P.M.,
RA Henrissat B., Martin F., Thomas P.D., Tyler B.M., De Vries R.P., Kamoun S.,
RA Yandell M., Tisserat N., Buell C.R.;
RT "Genome sequence of the necrotrophic plant pathogen Pythium ultimum reveals
RT original pathogenicity mechanisms and effector repertoire.";
RL Genome Biol. 11:R73-R73(2010).
RN [2] {ECO:0000313|Proteomes:UP000019132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM:BR144 {ECO:0000313|Proteomes:UP000019132};
RA Buell R., Hamilton J., Hostetler J.;
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblProtists:PYU1_T006958}
RP IDENTIFICATION.
RC STRAIN=DAOM BR144 {ECO:0000313|EnsemblProtists:PYU1_T006958};
RG EnsemblProtists;
RL Submitted (FEB-2015) to UniProtKB.
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|ARBA:ARBA00004255,
CC ECO:0000256|PIRNR:PIRNR037093}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR037093};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255,
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the COPG family. {ECO:0000256|ARBA:ARBA00010720,
CC ECO:0000256|PIRNR:PIRNR037093}.
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DR EMBL; GL376560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K3WPR6; -.
DR STRING; 431595.K3WPR6; -.
DR EnsemblFungi; PYU1_T006958; PYU1_T006958-p1; PYU1_G006943.
DR EnsemblProtists; PYU1_T006958; PYU1_T006958; PYU1_G006943.
DR VEuPathDB; FungiDB:PYU1_G006943; -.
DR eggNOG; KOG1078; Eukaryota.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; K3WPR6; -.
DR OMA; IEDCEYN; -.
DR Proteomes; UP000019132; Unassembled WGS sequence.
DR GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1480; Coatomer, gamma subunit, appendage domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.30.310.10; TATA-Binding Protein; 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; COATOMER SUBUNIT GAMMA; 1.
DR PANTHER; PTHR10261:SF0; COATOMER SUBUNIT GAMMA-2; 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; ARM repeat; 1.
DR SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1.
DR SUPFAM; SSF55711; Subdomain of clathrin and coatomer appendage domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR037093};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW ECO:0000256|PIRNR:PIRNR037093};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|PIRNR:PIRNR037093};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|PIRNR:PIRNR037093};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037093};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR037093};
KW Reference proteome {ECO:0000313|Proteomes:UP000019132};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT DOMAIN 61..575
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 652..798
FT /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT /evidence="ECO:0000259|Pfam:PF08752"
FT DOMAIN 802..915
FT /note="Coatomer subunit gamma C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16381"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 101262 MW; B566228E0AB7AE2B CRC64;
MKLGSHSDAH STGGGSEGGR SGSGGGSLSI SAVMQDLKEK FKNDEDSDHS SPFQGLDKAT
VLQETKIFSD ATMVTKHPKK CCQLITKLLH ILTQGEPFTS AETTAVFFGV TKLFQSKDSN
LRRMMYLFIK EVAEATAADE VIIVTQSLTK DMSSDVDLYR ANAIRVLCRI IDGSMLNAIE
RFMKQAIVDR NALVSSSALV SGMHLIKQNP EVVRRWVNEV QEAVNSQHDM VQYHAVGLLY
QIRQHDKLAV SKFINQLQKT NLRSNLATCL LIRYTAGLLR EDLGAQDPRP LYQFLQKMLR
QKNEMVIYEA AKALCSLPVD ARDLSQAIVV LQLFLSSSKP TLRFAAVRTL NQVALTQPLL
VTRCNDDMES LISDPNRSIA TLAITTLLKT GAESSVDRLM KQISTFMGDI ADEFKIVVVE
AIKNLCIKYP QKHRVLLNFL ANFLREEGGY EFKKTITDSI LFLIDRIPDC KEGGLLHLCE
FIEDCEFTQL STKILRVLGQ KGPTTSAPSR YIRYIRNRVI LENAAVRASA VSALAQFAIR
VDSLRLSVSS LLQSCKLDDD DEVRDRATMY LSVLHGDEGV SKTLLVDDFP MSVAALQKSI
EQYQLRPTDG PVTLDVLPHV EIVEEVKVAA ADADDSANDT PQAVAAPVQP QDVAKELYKI
PEFADLGPIF RSSKPVELTE AEVEYVVSCT KHVFSEHLVL QFKIMNTVND QLLTNVSVGF
AMDPDDVWQI HSVVPLKELA YGKTGSCYVC LKHIGDGMYP VVQIANELKF KVHEVNPSTG
EAEDDGFDEE YPMEDFEIGP NDLIAKVPVG DFRSAWEHIG DSAEAKGSYA LKYKSLVEGV
AAVIDNLGMQ PCENTAVPQP KANAHILLLS GVFVGGVKVL VKSRIVLDEQ SGGMILQMAV
RSESEDISQT IMDCIR
//
