ID   TVP38_ASPCL             Reviewed;         419 AA.
AC   A1CIM4;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Golgi apparatus membrane protein tvp38;
GN   Name=tvp38; ORFNames=ACLA_052010;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027054; EAW10729.1; -; Genomic_DNA.
DR   RefSeq; XP_001272155.1; XM_001272154.1.
DR   AlphaFoldDB; A1CIM4; -.
DR   STRING; 5057.CADACLAP00004897; -.
DR   EnsemblFungi; EAW10729; EAW10729; ACLA_052010.
DR   GeneID; 4703631; -.
DR   KEGG; act:ACLA_052010; -.
DR   VEuPathDB; FungiDB:ACLA_052010; -.
DR   eggNOG; KOG3140; Eukaryota.
DR   HOGENOM; CLU_041954_0_0_1; -.
DR   OMA; YHDEFTD; -.
DR   OrthoDB; 1327131at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
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..419
FT                   /note="Golgi apparatus membrane protein tvp38"
FT                   /id="PRO_0000343060"
FT   TOPO_DOM        1..82
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..158
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        182..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..274
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..419
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..259
FT                   /note="VTT domain"
FT                   /evidence="ECO:0000250|UniProtKB:P36164"
FT   REGION          365..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..419
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   419 AA;  46644 MW;  A525ABB50E9444F6 CRC64;
     MPAGYASTAR ALSLPMSPSG TPSPADDDIQ SPPWGHLIPN RQNTPSPSIR EATSFRDQIT
     SQATRLLYRM KKTWRRLNFW QRVGAIGAVI LAILLGLGFM IFTGQVFLWL EPVAETWEQS
     KLAFFVLWLC VFFVSFPPLV GWSTFGTVAG FIFGIWKGWL LYATATVLGS TCSFIVSRTV
     LSKFVNRMME RDKRFAALAL TLKYDGLKLL CMIRLCPLPY SVCNGAVSTF PTVHPLMYGL
     ATAIITPKLL VPAFIGSRIR ILSEQKGEMS AGSKAVNICS IVLTISIGVF TGWYIYKRTL
     ARAKELEAKE RADIRRSLQA DHAAHRPHGS FSEDPDVNTA ASILARDEEE RIGFNDFDDD
     NVDLVIDDES GSDNSSGQTR KHLQGSYRDE FTDNDSDVFR DGDGADSETY HLHTHVRPN