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Database: UniProt
Entry: A0A1L9VRS0_ASPGL
LinkDB: A0A1L9VRS0_ASPGL
Original site: A0A1L9VRS0_ASPGL 
ID   A0A1L9VRS0_ASPGL        Unreviewed;       438 AA.
AC   A0A1L9VRS0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Endoplasmic reticulum-Golgi intermediate compartment protein {ECO:0000256|RuleBase:RU369013};
GN   ORFNames=ASPGLDRAFT_44429 {ECO:0000313|EMBL:OJJ86596.1};
OS   Aspergillus glaucus CBS 516.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Aspergillus.
OX   NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ86596.1, ECO:0000313|Proteomes:UP000184300};
RN   [1] {ECO:0000313|Proteomes:UP000184300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC   -!- FUNCTION: Plays a role in transport between endoplasmic reticulum and
CC       Golgi. {ECO:0000256|RuleBase:RU369013}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU369013}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU369013}. Endoplasmic reticulum-Golgi
CC       intermediate compartment membrane {ECO:0000256|RuleBase:RU369013};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU369013}. Golgi
CC       apparatus membrane {ECO:0000256|RuleBase:RU369013}; Multi-pass membrane
CC       protein {ECO:0000256|RuleBase:RU369013}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ERGIC family.
CC       {ECO:0000256|RuleBase:RU369013}.
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DR   EMBL; KV878892; OJJ86596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9VRS0; -.
DR   STRING; 1160497.A0A1L9VRS0; -.
DR   VEuPathDB; FungiDB:ASPGLDRAFT_44429; -.
DR   OrthoDB; 506854at2759; -.
DR   Proteomes; UP000184300; Unassembled WGS sequence.
DR   GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IEA:UniProtKB-UniRule.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:UniProtKB-UniRule.
DR   InterPro; IPR045888; Erv.
DR   InterPro; IPR012936; Erv_C.
DR   InterPro; IPR039542; Erv_N.
DR   PANTHER; PTHR10984; ENDOPLASMIC RETICULUM-GOLGI INTERMEDIATE COMPARTMENT PROTEIN; 1.
DR   PANTHER; PTHR10984:SF25; ENDOPLASMIC RETICULUM-GOLGI INTERMEDIATE COMPARTMENT PROTEIN 3; 1.
DR   Pfam; PF07970; COPIIcoated_ERV; 1.
DR   Pfam; PF13850; ERGIC_N; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU369013};
KW   ER-Golgi transport {ECO:0000256|RuleBase:RU369013};
KW   Golgi apparatus {ECO:0000256|RuleBase:RU369013};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369013};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184300};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU369013};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU369013}; Transport {ECO:0000256|RuleBase:RU369013}.
FT   TRANSMEM        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369013"
FT   TRANSMEM        400..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369013"
FT   DOMAIN          8..96
FT                   /note="Endoplasmic reticulum vesicle transporter N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13850"
FT   DOMAIN          144..422
FT                   /note="Endoplasmic reticulum vesicle transporter C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07970"
SQ   SEQUENCE   438 AA;  48618 MW;  E4E244CB7A6170C2 CRC64;
     MPAKSRFTRL DAFAKTVEDA RIRTTSGGIV TIASLLIILW LVWGEWVDYR HVSVLPELVV
     DKSRGEKMEI HLNVTFPRLP CELLTLDVMD VSGEQQVGVA HGVNKVRLSP QAEGGRVLDI
     QALDLHSQEE IAKHLAPDYC GECGGAPAPD GVIKPGCCNT CDEVREAYAQ KSWAFGKGEN
     IEQCDREGYA ERLNAQRREG CRLEGVVRVN KVIGNFHIAP GRSFTSGNIH AHDLENFFEK
     DLSENERHTM THEIHQLRFG PQLPDELSDR WQWTDHHHTN PLDNTQQSTD EPAYNFMYFV
     KVVSTSYLPL GWDPLLSSAI HNTYDKSPLG AHGFAYGSQG SIETHQYSVT SHKRTLMGGN
     DAAEGHKERI HAQGGIPGVF FNYDISPMKV INREARTKTF SGFLTGVCAI IGGTLTVAAA
     VDRGLYEGAM KVKKIHSS
//
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