ID A0A165G4J1_EXIGL Unreviewed; 194 AA.
AC A0A165G4J1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE RecName: Full=Protein RER1 {ECO:0000256|PIRNR:PIRNR016013};
GN ORFNames=EXIGLDRAFT_771257 {ECO:0000313|EMBL:KZV89973.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV89973.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV89973.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV89973.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- FUNCTION: Involved in the retrieval of endoplasmic reticulum membrane
CC proteins from the early Golgi compartment.
CC {ECO:0000256|PIRNR:PIRNR016013}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the RER1 family. {ECO:0000256|ARBA:ARBA00006070,
CC ECO:0000256|PIRNR:PIRNR016013}.
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DR EMBL; KV426059; KZV89973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165G4J1; -.
DR STRING; 1314781.A0A165G4J1; -.
DR InParanoid; A0A165G4J1; -.
DR OrthoDB; 415184at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR InterPro; IPR004932; Rer1.
DR PANTHER; PTHR10743; PROTEIN RER1; 1.
DR PANTHER; PTHR10743:SF0; PROTEIN RER1; 1.
DR Pfam; PF03248; Rer1; 1.
DR PIRSF; PIRSF016013; AtER_Rer1p; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR016013};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 194 AA; 22498 MW; 02E0A6811EA68733 CRC64;
MMNAEDPSPF AGGPMAQYTL LKRRYQQLLD RSAPHTVNRW LATAGLIAVF ILRIVFAQGW
YIDAHAIYLL NLLLAFLQPK FDPSLEADLM ADEIEEGGAE EREPQLPSNS KDDEFRPFIR
RLPEWQFWLS VTRATVVALV CSLFSAFDVP VYWPILVVYF FILFALTMRR QIQHMVKYKY
VPWDFGKAKY GGKK
//
