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Database: UniProt
Entry: G3XRH4_ASPNA
LinkDB: G3XRH4_ASPNA
Original site: G3XRH4_ASPNA 
ID   G3XRH4_ASPNA            Unreviewed;       212 AA.
AC   G3XRH4;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Endoplasmic reticulum transmembrane protein {ECO:0000256|RuleBase:RU367026};
GN   ORFNames=ASPNIDRAFT_205494 {ECO:0000313|EMBL:EHA27030.1};
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA27030.1, ECO:0000313|Proteomes:UP000009038};
RN   [1] {ECO:0000313|EMBL:EHA27030.1, ECO:0000313|Proteomes:UP000009038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC   NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
CC   -!- FUNCTION: May play a role in anterograde transport of membrane proteins
CC       from the endoplasmic reticulum to the Golgi.
CC       {ECO:0000256|RuleBase:RU367026}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367026}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU367026}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the BCAP29/BCAP31 family.
CC       {ECO:0000256|ARBA:ARBA00007956, ECO:0000256|RuleBase:RU367026}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHA27030.1}.
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DR   EMBL; ACJE01000004; EHA27030.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3XRH4; -.
DR   STRING; 380704.G3XRH4; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1142721; -.
DR   HOGENOM; CLU_087648_0_1_1; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.5.110; -; 1.
DR   InterPro; IPR008417; BAP29/BAP31.
DR   InterPro; IPR040463; BAP29/BAP31_N.
DR   InterPro; IPR041672; Bap31/Bap29_C.
DR   PANTHER; PTHR12701; BCR-ASSOCIATED PROTEIN, BAP; 1.
DR   PANTHER; PTHR12701:SF18; ENDOPLASMIC RETICULUM TRANSMEMBRANE PROTEIN; 1.
DR   Pfam; PF05529; Bap31; 1.
DR   Pfam; PF18035; Bap31_Bap29_C; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU367026};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW   ECO:0000256|RuleBase:RU367026};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367026};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU367026};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU367026};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU367026};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367026}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367026"
FT   TRANSMEM        49..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367026"
FT   TRANSMEM        108..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367026"
FT   DOMAIN          1..140
FT                   /note="BAP29/BAP31 transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF05529"
FT   DOMAIN          163..212
FT                   /note="Bap31/Bap29 cytoplasmic coiled-coil"
FT                   /evidence="ECO:0000259|Pfam:PF18035"
FT   COILED          165..199
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   212 AA;  24053 MW;  8F27EA098A30AC05 CRC64;
     MTLYYSLVFC LLVFEMAVFM GLIIPLPFTV KRKLFAFISQ SPIVAKLQYG LKITFIFILI
     LFIDSVNRVY RVQLELASFG KEGGTMGAAA LGTDRMEVQA RKFYSQRNMY LCGFTLFLSL
     ILNRTYTMIL DVLRLEDRVR LLEGDKKAGG KDSARLAQAG EIGEIGRLKE ELAAKDRDIE
     TLKKQCEGLT REYHKLGDQV SGEKDEAPKK DQ
//
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