ID   COG4_BOVIN              Reviewed;         785 AA.
AC   Q3MHG0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Conserved oligomeric Golgi complex subunit 4;
DE            Short=COG complex subunit 4;
DE   AltName: Full=Component of oligomeric Golgi complex 4;
GN   Name=COG4;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for normal Golgi function. Plays a role in SNARE-pin
CC       assembly and Golgi-to-ER retrograde transport via its interaction with
CC       SCFD1. {ECO:0000250|UniProtKB:Q9H9E3}.
CC   -!- SUBUNIT: Monomer. Component of the conserved oligomeric Golgi (COG)
CC       complex which is composed of eight different subunits and is required
CC       for normal Golgi morphology and localization. Mediates interaction of
CC       SCFD1 with the COG complex. Interacts with STX5.
CC       {ECO:0000250|UniProtKB:Q9H9E3}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9H9E3}. Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q9H9E3}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9H9E3}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q9H9E3}.
CC   -!- SIMILARITY: Belongs to the COG4 family. {ECO:0000305}.
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DR   EMBL; BC105251; AAI05252.1; -; mRNA.
DR   RefSeq; NP_001029755.1; NM_001034583.1.
DR   AlphaFoldDB; Q3MHG0; -.
DR   STRING; 9913.ENSBTAP00000017269; -.
DR   PaxDb; Q3MHG0; -.
DR   PRIDE; Q3MHG0; -.
DR   Ensembl; ENSBTAT00000017269; ENSBTAP00000017269; ENSBTAG00000012988.
DR   GeneID; 533007; -.
DR   KEGG; bta:533007; -.
DR   CTD; 25839; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012988; -.
DR   VGNC; VGNC:27549; COG4.
DR   eggNOG; KOG0412; Eukaryota.
DR   GeneTree; ENSGT00940000154065; -.
DR   HOGENOM; CLU_014853_2_0_1; -.
DR   InParanoid; Q3MHG0; -.
DR   OMA; SECQQRV; -.
DR   OrthoDB; 376278at2759; -.
DR   TreeFam; TF105835; -.
DR   Reactome; R-BTA-6811438; Intra-Golgi traffic.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000012988; Expressed in retina and 109 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017119; C:Golgi transport complex; IBA:GO_Central.
DR   GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR   GO; GO:0048213; P:Golgi vesicle prefusion complex stabilization; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR   InterPro; IPR013167; COG_su4.
DR   Pfam; PF08318; COG4; 1.
DR   SMART; SM00762; Cog4; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Golgi apparatus; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9E3"
FT   CHAIN           2..785
FT                   /note="Conserved oligomeric Golgi complex subunit 4"
FT                   /id="PRO_0000282883"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..84
FT                   /note="Interaction with SCFD1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9E3"
FT   REGION          85..153
FT                   /note="Interaction with STX5"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9E3"
FT   REGION          618..740
FT                   /note="D domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9E3"
FT   REGION          741..785
FT                   /note="E domain; essential for proper cell surface
FT                   glycosylation"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9E3"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9E3"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9E3"
SQ   SEQUENCE   785 AA;  88856 MW;  5E6BE25D3C170110 CRC64;
     MADLDSPQKL SGVPRPPDGV GGGSCSEIST ELIRSLTDLQ ELEAVYERLC GEEKVVEREL
     DALLEQQNTI ESKMVTLHRM GPNLQLIEGD AKQLAGMITF TCNLAENVSS KVRQLDLAKN
     RLYQAIQRAD DILDLKFCMD GVQTALRNED YEQAAAHIHR YLCLDKSVIE LSRQGKEGSM
     IDANLKLLQE AEQRLKAIVT EKFAVATKEG DLPQVERFFK IFPLLGLHEE GLSKFSEYLC
     KQVASKAEEN LLLVLGTDMS DRRAAVIFAD TLTLLFEGIA RIVETHQPIV ETYYGPGRLY
     TLIKYLQVEC DRQVEKVVDK FIKQRDYRQQ FRHVQSNLMR NSTSEKIEPR ELDPILTEVT
     LMNARSELYL RFLRKRISSD FEVGDSMASE EVKQEHQKCL DKLLNNCLLS CTMQELIGLY
     ITMEEYFMRE TVNKAVALDT YEKGQLTSSM VDDVFYIVKK CIGRALSSSS IDCLCAMINL
     ATTELESDFR DVLCHKLRMG FPATTLQDIQ RGVTSAVSIM HSSLQQGKFD TKGIESTDEA
     KLSFLVTLNN VEVCSENIST LKKTLESDCT KLFSQGIGGE QAQAKFDSCL SDLAAVSGKF
     RDLLQEGLTE LNSTAIKPQV QPWINTFLSV SHNIEEEEFS DYEANDPWVQ QFILNLEQQM
     AEFKAGLSPV IYDSLTSLMT SLVAVELEKV VLKSTFNRLG GLQFDKELRS LIAYLTTVTT
     WTIRDKFARL SQMATILNLE RVTEILDYWG ANSGPLTWRL TPAEVRQVLA LRIDFRSEDI
     KRLRL