ID G8BXS8_TETPH Unreviewed; 66 AA.
AC G8BXS8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Stress-associated endoplasmic reticulum protein {ECO:0000256|RuleBase:RU364120};
GN Name=TPHA0I02020 {ECO:0000313|EMBL:CCE64706.1};
GN OrderedLocusNames=TPHA_0I02020 {ECO:0000313|EMBL:CCE64706.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE64706.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE64706.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE612864; CCE64706.1; -; Genomic_DNA.
DR RefSeq; XP_003687140.1; XM_003687092.1.
DR AlphaFoldDB; G8BXS8; -.
DR GeneID; 11534507; -.
DR KEGG; tpf:TPHA_0I02020; -.
DR eggNOG; ENOG502SDGZ; Eukaryota.
DR HOGENOM; CLU_182424_0_1_1; -.
DR OMA; ANEKFYK; -.
DR OrthoDB; 5604459at2759; -.
DR Proteomes; UP000005666; Chromosome 9.
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:UP000005666};
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 44..65
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364120"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 66 AA; 7586 MW; B99732EF3995A25F CRC64;
MASNALKQKL GNEKFKKRNE HHRKLGKKKI ELSKKKDQPP ISKVWIYILA FLIVGGGILE
IISLLF
//