SOP4_KLULA
ID SOP4_KLULA Reviewed; 234 AA.
AC Q6CW19;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Protein SOP4;
DE Flags: Precursor;
GN Name=SOP4; OrderedLocusNames=KLLA0B07645g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382122; CAH02263.1; -; Genomic_DNA.
DR RefSeq; XP_451870.1; XM_451870.1.
DR AlphaFoldDB; Q6CW19; -.
DR SMR; Q6CW19; -.
DR STRING; 28985.XP_451870.1; -.
DR PRIDE; Q6CW19; -.
DR EnsemblFungi; CAH02263; CAH02263; KLLA0_B07645g.
DR GeneID; 2897048; -.
DR KEGG; kla:KLLA0_B07645g; -.
DR eggNOG; ENOG502RXGD; Eukaryota.
DR HOGENOM; CLU_102669_0_0_1; -.
DR InParanoid; Q6CW19; -.
DR OMA; PYITVEL; -.
DR Proteomes; UP000000598; Chromosome B.
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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..234
FT /note="Protein SOP4"
FT /id="PRO_0000324497"
FT TOPO_DOM 20..191
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 234 AA; 27120 MW; DC4B7D951E15F95A CRC64;
MNFVLFCFLV WQFVNPGAAF DIKGRLDLKV RNVSRHDISR TYFNLYRIRN PNDDSEWDSY
SQSSKLENIN GEFTFSDVPI DTGINRTTYF TLHSHSNEFN LKPNRILIQI VGNGQDQEPN
LSAFENRFGR EYFPSPDITY PETLNPLPLD SANRLTITTM NKQPYRKYIK IRNPGILESG
PIASVLRSKF KLAGVVTVIF LVLFPILLEK FDPETAKAMR QEKMHRENAK YVSK