SOP4_VANPO
ID SOP4_VANPO Reviewed; 230 AA.
AC A7TFH0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Protein SOP4;
DE Flags: Precursor;
GN Name=SOP4; ORFNames=Kpol_2002p55;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC -!- FUNCTION: Involved in the export of PMA1, possibly through the
CC monitoring or assisting of PMA1 folding and acquisition of competence
CC to enter vesicles. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SOP4 family. {ECO:0000305}.
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DR EMBL; DS480383; EDO18984.1; -; Genomic_DNA.
DR RefSeq; XP_001646842.1; XM_001646792.1.
DR AlphaFoldDB; A7TFH0; -.
DR SMR; A7TFH0; -.
DR STRING; 436907.A7TFH0; -.
DR EnsemblFungi; EDO18984; EDO18984; Kpol_2002p55.
DR GeneID; 5547310; -.
DR KEGG; vpo:Kpol_2002p55; -.
DR eggNOG; ENOG502RXGD; Eukaryota.
DR HOGENOM; CLU_102669_0_0_1; -.
DR InParanoid; A7TFH0; -.
DR OMA; PYITVEL; -.
DR OrthoDB; 1591902at2759; -.
DR PhylomeDB; A7TFH0; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR031395; Sop4.
DR Pfam; PF17081; SOP4; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..230
FT /note="Protein SOP4"
FT /id="PRO_0000324498"
FT TOPO_DOM 18..187
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 230 AA; 26951 MW; C9E4C97E3F3FC36E CRC64;
MKLLILCLLY YTQLVICNVV SFTGKYSLHP KNLTIDDISR VDFRIYQIGN YTNKPFSQST
KVNSIDGLFT FNNLPLNRGN NVTTDFVIYS TSLDYNLKPV RILLTYTSWD DEANNHTVKA
YSNFVGREYF PDKDIIFPDK LEELSMDPYL EVTYFNKAPY RLYYQERNEG ILSTGIIGNI
LSSRWKTAGV ITMILLIIFP YVVERLDPET SQLLREEVQR KQREKYQIQQ