ENV10_YEAST
ID ENV10_YEAST Reviewed; 181 AA.
AC Q99382; D6VY66; Q6Q5C1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=SRP-independent targeting protein 2 {ECO:0000303|PubMed:27905431};
DE AltName: Full=Late endosome and vacuole interface protein 10 {ECO:0000303|PubMed:21912603};
GN Name=ENV10 {ECO:0000303|PubMed:21912603};
GN Synonyms=SND2 {ECO:0000303|PubMed:27905431};
GN OrderedLocusNames=YLR065C {ECO:0000312|SGD:S000004055}; ORFNames=L2180;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
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 [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21912603; DOI=10.1371/journal.pone.0023696;
RA Ricarte F., Menjivar R., Chhun S., Soreta T., Oliveira L., Hsueh T.,
RA Serranilla M., Gharakhanian E.;
RT "A genome-wide immunodetection screen in S. cerevisiae uncovers novel genes
RT involved in lysosomal vacuole function and morphology.";
RL PLoS ONE 6:E23696-E23696(2011).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SND1; PHO88 AND SEC61.
RX PubMed=27905431; DOI=10.1038/nature20169;
RA Aviram N., Ast T., Costa E.A., Arakel E.C., Chuartzman S.G., Jan C.H.,
RA Hassdenteufel S., Dudek J., Jung M., Schorr S., Zimmermann R.,
RA Schwappach B., Weissman J.S., Schuldiner M.;
RT "The SND proteins constitute an alternative targeting route to the
RT endoplasmic reticulum.";
RL Nature 540:134-138(2016).
CC -!- FUNCTION: Functions in the SND pathway, a SRP (signal recognition
CC particle) and GET (guided entry of tail-anchored proteins) independent
CC pathway for targeting a broad range of substrate proteins to the
CC endoplasmic reticulum. SND functions in parallel to GET in targeting
CC proteins with downstream hydrophobic motifs (PubMed:27905431). Involved
CC in vacuolar processing and morphology (PubMed:21912603).
CC {ECO:0000269|PubMed:21912603, ECO:0000269|PubMed:27905431}.
CC -!- SUBUNIT: Interacts with SND1, PHO88/SND3 and the translocon complex
CC subunit SEC61. ENV10/SND2 and PHO88/SND3 form a complex with the
CC translocon in the endoplasmic reticulum membrane.
CC {ECO:0000269|PubMed:27905431}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27905431}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Exhibits cold sensitivity and leads to internal
CC accumulation of precursor CPY. {ECO:0000269|PubMed:21912603}.
CC -!- SIMILARITY: Belongs to the TMEM208 family. {ECO:0000305}.
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DR EMBL; X94607; CAA64311.1; -; Genomic_DNA.
DR EMBL; Z73237; CAA97621.1; -; Genomic_DNA.
DR EMBL; AY558207; AAS56533.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09382.1; -; Genomic_DNA.
DR PIR; S61638; S61638.
DR RefSeq; NP_013166.1; NM_001181952.1.
DR AlphaFoldDB; Q99382; -.
DR BioGRID; 31339; 514.
DR DIP; DIP-1937N; -.
DR IntAct; Q99382; 1.
DR MINT; Q99382; -.
DR STRING; 4932.YLR065C; -.
DR TCDB; 9.A.64.1.1; the srp-independent targeting (snd) family.
DR MaxQB; Q99382; -.
DR PaxDb; Q99382; -.
DR PRIDE; Q99382; -.
DR TopDownProteomics; Q99382; -.
DR EnsemblFungi; YLR065C_mRNA; YLR065C; YLR065C.
DR GeneID; 850754; -.
DR KEGG; sce:YLR065C; -.
DR SGD; S000004055; ENV10.
DR VEuPathDB; FungiDB:YLR065C; -.
DR eggNOG; KOG3269; Eukaryota.
DR GeneTree; ENSGT00390000008139; -.
DR HOGENOM; CLU_094308_1_1_1; -.
DR InParanoid; Q99382; -.
DR OMA; GLKNQFF; -.
DR BioCyc; YEAST:G3O-32218-MON; -.
DR PRO; PR:Q99382; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q99382; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
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:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006624; P:vacuolar protein processing; IMP:SGD.
DR InterPro; IPR008506; SND2/TMEM208.
DR PANTHER; PTHR13505; PTHR13505; 1.
DR Pfam; PF05620; TMEM208_SND2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..181
FT /note="SRP-independent targeting protein 2"
FT /id="PRO_0000247246"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..45
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..112
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT REGION 144..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 181 AA; 20742 MW; F001EE144370D4B3 CRC64;
MAGKAGRKQA SSNAKIIQGL YKQVSLFLGM AIVRLFISRK VTIGQWIKLV ALNVPMFVAL
YIIVLSGKPK YDGNRVVKQG IDLNDNTNLI SYFFDLIYLS LFGNIGIIAF RTFKFWWCLL
LCPIYAGYKL YGLKNMFMPG AQQTQADNRS KNANEGQSKS KRQMKRERRG ETDSKIKYKY
R
