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Database: UniProt
Entry: A0A4Y7ICZ1_PAPSO
LinkDB: A0A4Y7ICZ1_PAPSO
Original site: A0A4Y7ICZ1_PAPSO 
ID   A0A4Y7ICZ1_PAPSO        Unreviewed;       886 AA.
AC   A0A4Y7ICZ1;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN   ORFNames=C5167_038195 {ECO:0000313|EMBL:RZC45259.1};
OS   Papaver somniferum (Opium poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Papaver.
OX   NCBI_TaxID=3469 {ECO:0000313|EMBL:RZC45259.1, ECO:0000313|Proteomes:UP000316621};
RN   [1] {ECO:0000313|EMBL:RZC45259.1, ECO:0000313|Proteomes:UP000316621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HN1 {ECO:0000313|Proteomes:UP000316621};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RZC45259.1};
RX   PubMed=30166436; DOI=.1126/science.aat4096;
RA   Guo L., Winzer T., Yang X., Li Y., Ning Z., He Z., Teodor R., Lu Y.,
RA   Bowser T.A., Graham I.A., Ye K.;
RT   "The opium poppy genome and morphinan production.";
RL   Science 362:343-347(2018).
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; CM010715; RZC45259.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Y7ICZ1; -.
DR   STRING; 3469.A0A4Y7ICZ1; -.
DR   EnsemblPlants; RZC45259; RZC45259; C5167_038195.
DR   Gramene; RZC45259; RZC45259; C5167_038195.
DR   OMA; IEDCEYN; -.
DR   OrthoDB; 5260816at2759; -.
DR   Proteomes; UP000316621; Chromosome 1.
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:UP000316621};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT   DOMAIN          27..541
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          622..766
FT                   /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT                   /evidence="ECO:0000259|Pfam:PF08752"
FT   DOMAIN          769..883
FT                   /note="Coatomer subunit gamma C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16381"
FT   REGION          593..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   886 AA;  98276 MW;  ED92ACB08EEC63ED CRC64;
     MAQPLIKKDD DRDDEAEYSP FLGIEKGAVL QEARVFHDPQ LDPRRCSQVI TKLLYLLNQG
     ESFTKVEATE VFFAVTKLFQ SKDIGLRRMV YLIIKELSPS SDEVIIVTSS LMKDMNSKSD
     MYRANAIRVL CRIIDGTLLT QIERYLKQAI VDKNPVVASA ALVSGIHLLQ TNPEIVKRWG
     NEVQEAVQSR AALVQFHALA LLHQIRQNDR LAVSKLVTSL TKGTVRSPLA QCLLIRYTCQ
     VIRETGVNTP TGDRPFYDYL EGCLRHKAEM VIFEAARAIT ELSGVTNREL TPAITVLQLF
     LSSSKPVLRF AAVRTLNKVA MTHPLAVTNC NIDMESLISD QNRSIATLAI TTLLKTGNES
     SVDRLMKQIT NFMSDIADEF KIVVVDAIRS LCLKFPLKYR SLMNFLSNIL REEGGFEYKK
     AIVDSIVILI RDIPDAKESG LFHLCEFIED CEFTYLSTQI LHFLGDEGPK TSDPSKYIRY
     IYNRVILENA TVRSSAVSTL AKYGALVESL KPRVFILLNR CLFDSDDEVR DRATLYLNTL
     RGDGSEAETN SEAKEFLFGS LDVPLVNLEK SLKNYEPSEE AFDIDSVPKE VKSQPLAEKK
     ATGKKQTGLG APPAGPKPVV DAYEKTLSSI PEFSSFGKLF KSSAPFELTE AETEYAVNVV
     KHIFDDHVVF QYNCTNTIPE QQLENVTVIV DASEAEGFAK LAVKPLTALP YDSPGQTYVA
     FEKPEGLAFG KFSNTLRFIV KEVDTSTGDV EDDGVEDEYQ LEDVEIVAAD YMLKIGVSNF
     RNAWEGMGPE CEKVDEYGLG VRESLAEAVS AVISILGMQP CEGTEVVPSN SRSHTCLLSG
     VFVGNVKVLV RLSFGIDGPK QVAMKLAVRS EDEAVSDAIH DIVASG
//
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