ID A0A0F0I0H9_ASPPU Unreviewed; 79 AA.
AC A0A0F0I0H9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Stress-associated endoplasmic reticulum protein {ECO:0000256|RuleBase:RU364120};
GN ORFNames=P875_00053682 {ECO:0000313|EMBL:KJK60137.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK60137.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK60137.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Interacts with target proteins during translocation into the
CC lumen of the endoplasmic reticulum. Protects unfolded target proteins
CC against degradation and facilitate correct glycosylation.
CC {ECO:0000256|RuleBase:RU364120}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU364120}; Single-
CC pass membrane protein {ECO:0000256|RuleBase:RU364120}. Endoplasmic
CC reticulum membrane {ECO:0000256|RuleBase:RU364120}; Single-pass
CC membrane protein {ECO:0000256|RuleBase:RU364120}.
CC -!- SIMILARITY: Belongs to the RAMP4 family.
CC {ECO:0000256|ARBA:ARBA00005500, ECO:0000256|RuleBase:RU364120}.
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:KJK60137.1}.
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DR EMBL; JZEE01000753; KJK60137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0I0H9; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR010580; ER_stress-assoc.
DR Pfam; PF06624; RAMP4; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU364120};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364120};
KW Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU364120};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU364120}.
FT TRANSMEM 39..57
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364120"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 79 AA; 8551 MW; E31A435517356EE3 CRC64;
MAQTPQQRKA NEKYAKSEAA KRGKGKTATK QKQNSKSPVS TGWVVVLAFA VCGGLAFEAL
RIVPELWSAA VAMFNRKLA
//
