ID   TVP38_DEBHA             Reviewed;         383 AA.
AC   Q6BQJ1;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Golgi apparatus membrane protein TVP38;
GN   Name=TVP38; OrderedLocusNames=DEHA2E04840g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382137; CAG87756.1; -; Genomic_DNA.
DR   RefSeq; XP_459529.1; XM_459529.1.
DR   AlphaFoldDB; Q6BQJ1; -.
DR   STRING; 4959.XP_459529.1; -.
DR   EnsemblFungi; CAG87756; CAG87756; DEHA2E04840g.
DR   GeneID; 2901842; -.
DR   KEGG; dha:DEHA2E04840g; -.
DR   VEuPathDB; FungiDB:DEHA2E04840g; -.
DR   eggNOG; KOG3140; Eukaryota.
DR   HOGENOM; CLU_041954_1_0_1; -.
DR   InParanoid; Q6BQJ1; -.
DR   OMA; IAVHKLI; -.
DR   OrthoDB; 1327131at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR032816; SNARE_assoc.
DR   Pfam; PF09335; SNARE_assoc; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..383
FT                   /note="Golgi apparatus membrane protein TVP38"
FT                   /id="PRO_0000343068"
FT   TOPO_DOM        1..57
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..99
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..133
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        234..248
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        270..383
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..235
FT                   /note="VTT domain"
FT                   /evidence="ECO:0000250|UniProtKB:P36164"
FT   REGION          345..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   383 AA;  43234 MW;  E13A1103C8ABD89B CRC64;
     MPRLPSSSDP FQGHNELPQS NNFMSRTNSI IQDKLFLVRN VGQQTLDWYQ SQPLWKRTLL
     QVLFVFNAIV VVLIMIFHKS IIQAIVVISD KWHGLKFGQG LLFTLVFMVG FPPLLGFSAL
     SMLAGMVYGF VHGWILLACA SISGSFCSFL VFRYLLHSRA ERLMNSNKKF RAFSEILRED
     SSLFILVLLR LCPLPYSLSN GALAAIPELP ATTYFLASLI TSPKLMIHIF VGHKLKELGD
     DTKGKSTHLI DILSIIITGA AASLTTYIIY NKMQRKLEFY HQRGIIPRDD AIIFGNFEDI
     ESANNVELNS ADYDEDNFII EDEDDENATD PDYVASKKNI QVHAEDQNKN GEFEIDENDG
     VDDLGLGEIS KNSKQNTNGY RDY