ID   GOGA5_XENLA             Reviewed;         722 AA.
AC   Q6GNT7;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Golgin subfamily A member 5;
DE   AltName: Full=Golgin-84;
GN   Name=golga5;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in maintaining Golgi structure. Stimulates the
CC       formation of Golgi stacks and ribbons. Involved in intra-Golgi
CC       retrograde transport (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type IV membrane protein {ECO:0000250}.
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DR   EMBL; BC073415; AAH73415.1; -; mRNA.
DR   RefSeq; NP_001085841.1; NM_001092372.1.
DR   AlphaFoldDB; Q6GNT7; -.
DR   SMR; Q6GNT7; -.
DR   GeneID; 444268; -.
DR   KEGG; xla:444268; -.
DR   CTD; 444268; -.
DR   Xenbase; XB-GENE-1014830; golga5.L.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 444268; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR   GO; GO:0048193; P:Golgi vesicle transport; ISS:UniProtKB.
DR   InterPro; IPR019177; Golgin_subfamily_A_member_5.
DR   PANTHER; PTHR13815; PTHR13815; 2.
DR   Pfam; PF09787; Golgin_A5; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..722
FT                   /note="Golgin subfamily A member 5"
FT                   /id="PRO_0000190065"
FT   TOPO_DOM        1..689
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        690..710
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        711..722
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          90..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          211..622
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        90..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   722 AA;  82044 MW;  E7C075D69915D298 CRC64;
     MSWFTDLAGR AEDFLNLVDQ GAATALKTKD GNDLIMDSIT DYSGNFEEKQ KTTEKYQSQA
     KSSFISSAAD NIKHQKATML AGTANIKTGT RSSIESSHNS SVNVSSHRST TQFVRQKKSE
     PDDEQLFDFL NSSDKVHSSS QKETRKESAS VNQAVKPISQ SVTMAEDFHN TTEDAGVPLL
     PELGITEPVV KAETLSDSGS SASLSTTGDP KSHELSNLRL ENQLLRNEVQ SLNQEMASLI
     QRSKETQEEL NEARTRMEKW NGDNSKNDRT ARELRAQVDD LSEAMAAKDS QLAVLKVRLQ
     EADQLLKSRT ETLESLQIEK SRILQDQSEG SSIHNQALQT MQERLREAES TLIREQESYK
     QIQNEFATRL SKIEAERQNL AEAVILAEKK HMEEKRKSDD LQQQLKTSKV GLDSLKQEMA
     DYKQKATRIL QSKEKLINSL KEGSGIEGLD SHSASTMELE EMRHERDMQR EEIQKLMGQI
     QQLKAELQDV ETQQVSEAES AREQLQDVHE QFATQQRAKQ ELEAELERQK QEFQYIQEDL
     YKTKNTLQGR IRDREDEIQK LRNQLTNKAL SSSSQTELEN RLHQLTETLI QKQTMLENLS
     TEKNSLVYQL ERLEHQLKNV QGSSLNGTSI NMSVIESNEG ARMRNVPVLF SDSDPNVAGM
     YGRVRKAATS IDQFSIRLGI FLRRYPIARV FIIIYMALLH LWVMIVLLTY TPEMHHDTPS
     GK