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Database: UniProt
Entry: TVP38_PICGU
LinkDB: TVP38_PICGU
Original site: TVP38_PICGU 
ID   TVP38_PICGU             Reviewed;         349 AA.
AC   A5DH87;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Golgi apparatus membrane protein TVP38;
GN   Name=TVP38; ORFNames=PGUG_02638;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: Golgi membrane protein involved in vesicular trafficking and
CC       spindle migration.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC       protein.
CC   -!- DOMAIN: The VTT domain was previously called the SNARE-assoc domain. As
CC       there is no evidence that this domain associates with SNARE proteins,
CC       it was renamed as VMP1, TMEM41, and TVP38 (VTT) domain.
CC       {ECO:0000250|UniProtKB:P36164}.
CC   -!- SIMILARITY: Belongs to the TVP38/TMEM64 family. {ECO:0000305}.
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DR   EMBL; CH408157; EDK38540.2; -; Genomic_DNA.
DR   RefSeq; XP_001484909.1; XM_001484859.1.
DR   AlphaFoldDB; A5DH87; -.
DR   STRING; 294746.A5DH87; -.
DR   GlyCosmos; A5DH87; 1 site, No reported glycans.
DR   GeneID; 5126612; -.
DR   KEGG; pgu:PGUG_02638; -.
DR   VEuPathDB; FungiDB:PGUG_02638; -.
DR   eggNOG; KOG3140; Eukaryota.
DR   HOGENOM; CLU_041954_1_0_1; -.
DR   InParanoid; A5DH87; -.
DR   OMA; KWQALET; -.
DR   OrthoDB; 2385736at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR032816; VTT_dom.
DR   PANTHER; PTHR47549:SF1; GOLGI APPARATUS MEMBRANE PROTEIN TVP38; 1.
DR   PANTHER; PTHR47549; GOLGI APPARATUS MEMBRANE PROTEIN TVP38-RELATED; 1.
DR   Pfam; PF09335; SNARE_assoc; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..349
FT                   /note="Golgi apparatus membrane protein TVP38"
FT                   /id="PRO_0000343072"
FT   TOPO_DOM        1..49
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..91
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..123
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..240
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..349
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          117..227
FT                   /note="VTT domain"
FT                   /evidence="ECO:0000250|UniProtKB:P36164"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   349 AA;  38715 MW;  F64E6B6D5503051F CRC64;
     MPRLHSASEP PATGFFARVR NELGNRTEGL HQINNQALDW YRSQSQIRQI LIQIGGVVAI
     VIGVLVLIFH KYLIELLVII SDDWAKLPGG RLILFLLVFF VGFPPLIGYS ALSLLAGMVY
     GFPYGWPLLA SASVSGSFVA FLVFRYFLRS QGERLVNSNE KFRAFAEILR EDSSLFLLVL
     IRLCPLPYSL SNGALAAIPE LSAWVYLGAS VITSPKMLIH LFVGHKIKEF GDAKTDTSTK
     IIDVISILVT GAAASLTTFI IYRKMQQKLH HNRAGANYDA FVFGNFDDLE SGTNVELNSA
     DFDQDNFIIT DDELEEEEPN GSHTATATQV QVARRNCSKA MTICTLMFV
//
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