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Database: UniProt
Entry: A0A1Q2YD02_9ASCO
LinkDB: A0A1Q2YD02_9ASCO
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ID   A0A1Q2YD02_9ASCO        Unreviewed;       905 AA.
AC   A0A1Q2YD02;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN   ORFNames=PMKS-000905 {ECO:0000313|EMBL:GAV27437.1};
OS   Pichia membranifaciens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=4926 {ECO:0000313|EMBL:GAV27437.1, ECO:0000313|Proteomes:UP000186136};
RN   [1] {ECO:0000313|EMBL:GAV27437.1, ECO:0000313|Proteomes:UP000186136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KS47-1 {ECO:0000313|EMBL:GAV27437.1,
RC   ECO:0000313|Proteomes:UP000186136};
RA   Konishi M., Ishida M., Arakawa T., Kato Y., Horiuchi J.;
RT   "Whole genome shotgun sequence of Pichia membranifaciens KS47-1.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAV27437.1}.
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DR   EMBL; BDGI01000034; GAV27437.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2YD02; -.
DR   Proteomes; UP000186136; 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; 2.
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:UP000186136};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT   DOMAIN          2..539
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          644..790
FT                   /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT                   /evidence="ECO:0000259|Pfam:PF08752"
FT   DOMAIN          792..903
FT                   /note="Coatomer subunit gamma C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16381"
SQ   SEQUENCE   905 AA;  102132 MW;  C95EFB1FDD9151B2 CRC64;
     MTVYQECLQA CNASPIQAKK CRKLLSRLLR LFYAGETFPT VESTNLFFSI SKLFHNDDPS
     LRQIAYLAIK ELCSMSNDIL MITASIMKDI QNGDAVYKPD AVRTLSRVLD GSTIHAAERL
     FKNCIVDSNQ SISSAALVSS YHLLPVAKDV VKRWTTEVQE SITANKVFPT SPYTQHEFTG
     YNKTPNSTFI HQYHALSLIY QFRNNDKMSL IKMIQQLTER KTLTNSLAQI QMIRFVEKLI
     LDDPNFVHSL WPLFVNWLNN KSDMVELEAA KLILNNTSKF NSEQQMHAIT TLQSLLGVPR
     TVTRFAAVRV LNKVAIKDAD KVGVCNLELE RLISDQSRSI STYAITTLLK TGNIESVDRL
     VQAISNFMDE ISDEFKIIVI DAIRTLSLKF PAKYKSMLTF LNDVLREEGG FNFKNSIVEA
     IFDIIKFIPE SKEIALEMLC EFIEDCEYTE LSVRILHLLG NEGPKTANPS TYVRYIYNRV
     VLENSIVRSS AVIALSKFAL INDKDLNKSI KILLKRSLQD VDDEVRDRAV LSLKLLESKD
     LVEAKSYLLP QFKYSLPILE QELTKYVQNP DKSSFKSSFS IESIPKISEE EYMAVQYKEK
     LTGGIDDVIV DGSDDLNSKG NESNDDVKGL DKISDVTKYT LLQQQYQNEL SALPEIGDYG
     TLLHSSAPVE LTEKETEFVV TAIKHIFPKH VVVEFSIENT LDDIILENVN VVTQLDTEEY
     TEELTLPIEL LNPHSKGKAY SSFTRPEDDD EKFMLTTMNN TLAYLTKDVD AEADEEGFPD
     EYQIEDLSLT PGDFVIPTYI SNFTNVWDEL SNEESAVYNL GDEESVDLQQ VVTKLIVTMS
     MMPIEGTEVV TSGKNHSLKL FGKSIAGGRL AAVIKFAVSS KGVMMKNVVK GEEAELVELV
     ANYLE
//
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