SVP26_YEAST
ID SVP26_YEAST Reviewed; 228 AA.
AC P38869; D3DLC9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein SVP26;
DE AltName: Full=Sed5 compartment vesicle protein of 26 kDa;
GN Name=SVP26; OrderedLocusNames=YHR181W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
RP SUBUNIT, AND INTERACTION WITH KTR3.
RX PubMed=16107716; DOI=10.1128/mcb.25.17.7696-7710.2005;
RA Inadome H., Noda Y., Adachi H., Yoda K.;
RT "Immunoisolation of the yeast Golgi subcompartments and characterization of
RT a novel membrane protein, Svp26, discovered in the Sed5-containing
RT compartments.";
RL Mol. Cell. Biol. 25:7696-7710(2005).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MNN2 AND MNN5.
RX PubMed=20236934; DOI=10.1074/jbc.m109.086272;
RA Noda Y., Yoda K.;
RT "Svp26 facilitates endoplasmic reticulum to Golgi transport of a set of
RT mannosyltransferases in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 285:15420-15429(2010).
CC -!- FUNCTION: Plays a role in retention of a subset of membrane proteins in
CC the early Golgi compartments. Facilitates endoplasmic reticulum to
CC Golgi transport of mannosyltransferases MNN2 and MNN5.
CC {ECO:0000269|PubMed:16107716, ECO:0000269|PubMed:20236934}.
CC -!- SUBUNIT: Interacts with itself. Interacts with KTR3, MNN2 and MNN5.
CC {ECO:0000269|PubMed:16107716, ECO:0000269|PubMed:20236934}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16107716,
CC ECO:0000269|PubMed:20236934}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16107716,
CC ECO:0000269|PubMed:20236934}. Note=Early Golgi.
CC -!- PTM: N-glycosylated.
CC -!- MISCELLANEOUS: Present with 1810 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SVP26 family. {ECO:0000305}.
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DR EMBL; U00028; AAB68454.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06873.1; -; Genomic_DNA.
DR PIR; S46673; S46673.
DR RefSeq; NP_012051.3; NM_001179312.3.
DR AlphaFoldDB; P38869; -.
DR BioGRID; 36614; 137.
DR IntAct; P38869; 3.
DR STRING; 4932.YHR181W; -.
DR MaxQB; P38869; -.
DR PaxDb; P38869; -.
DR PRIDE; P38869; -.
DR EnsemblFungi; YHR181W_mRNA; YHR181W; YHR181W.
DR GeneID; 856587; -.
DR KEGG; sce:YHR181W; -.
DR SGD; S000001224; SVP26.
DR VEuPathDB; FungiDB:YHR181W; -.
DR eggNOG; KOG4136; Eukaryota.
DR GeneTree; ENSGT00390000010888; -.
DR HOGENOM; CLU_058268_0_0_1; -.
DR InParanoid; P38869; -.
DR OMA; FEDLPWS; -.
DR BioCyc; YEAST:G3O-31212-MON; -.
DR PRO; PR:P38869; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38869; protein.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:SGD.
DR GO; GO:0097020; F:COPII receptor activity; IMP:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR007277; Svp26/Tex261.
DR PANTHER; PTHR13144; PTHR13144; 1.
DR Pfam; PF04148; Erv26; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..228
FT /note="Protein SVP26"
FT /id="PRO_0000202934"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..42
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..142
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 228 AA; 26284 MW; C86FD804BC4EEAFD CRC64;
MLLELISYAG TVSGFLFLTL SIASGLYYIS ELVEEHTEPT RRFLTRAIYG IILILILLLL
LDGFPFKLTL FSIACYIVYY QNLKSFPFIS LTSPTFLLSC VCVVLNHYFW FKYFNDTEVP
PQFKFDPNYI PRRRASFAEV ASFFGICVWF IPFALFVSLS AGDYVLPTTS EQHMAKKNDD
ITTNNQPKFR KRAVGLARVV INSVRKYIYS LARVFGYEIE PDFDRLAV
