NCE2_YEAST
ID NCE2_YEAST Reviewed; 173 AA.
AC Q12207; D6W4E6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Non-classical export protein 2;
GN Name=NCE102; Synonyms=NCE2, RTG2S2; OrderedLocusNames=YPR149W;
GN ORFNames=P9659.2;
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 [MRNA], AND FUNCTION.
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=8655575; DOI=10.1083/jcb.133.5.1017;
RA Cleves A.E., Cooper D.N.W., Barondes S.H., Kelly R.B.;
RT "A new pathway for protein export in Saccharomyces cerevisiae.";
RL J. Cell Biol. 133:1017-1026(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=COP161U7;
RA Jia Y., Li J.-P., Butow R.A.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10716729; DOI=10.1073/pnas.97.7.3254;
RA Bagnat M., Keranen S., Shevchenko A., Shevchenko A., Simons K.;
RT "Lipid rafts function in biosynthetic delivery of proteins to the cell
RT surface in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3254-3259(2000).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12469340;
RX DOI=10.1002/1615-9861(200212)2:12<1706::aid-prot1706>3.0.co;2-k;
RA Navarre C., Degand H., Bennett K.L., Crawford J.S., Moertz E., Boutry M.;
RT "Subproteomics: identification of plasma membrane proteins from the yeast
RT Saccharomyces cerevisiae.";
RL Proteomics 2:1706-1714(2002).
RN [8]
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 [9]
RP FUNCTION.
RX PubMed=17415679; DOI=10.1007/s10522-007-9095-5;
RA Desmyter L., Verstraelen J., Dewaele S., Libert C., Contreras R., Chen C.;
RT "Nonclassical export pathway: overexpression of NCE102 reduces protein and
RT DNA damage and prolongs lifespan in an SGS1 deficient Saccharomyces
RT cerevisiae.";
RL Biogerontology 8:527-535(2007).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19064668; DOI=10.1083/jcb.200806035;
RA Grossmann G., Malinsky J., Stahlschmidt W., Loibl M., Weig-Meckl I.,
RA Frommer W.B., Opekarova M., Tanner W.;
RT "Plasma membrane microdomains regulate turnover of transport proteins in
RT yeast.";
RL J. Cell Biol. 183:1075-1088(2008).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19564405; DOI=10.1083/jcb.200811081;
RA Frohlich F., Moreira K., Aguilar P.S., Hubner N.C., Mann M., Walter P.,
RA Walther T.C.;
RT "A genome-wide screen for genes affecting eisosomes reveals Nce102 function
RT in sphingolipid signaling.";
RL J. Cell Biol. 185:1227-1242(2009).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND DOMAIN.
RX PubMed=20581291; DOI=10.1128/ec.00006-10;
RA Loibl M., Grossmann G., Stradalova V., Klingl A., Rachel R., Tanner W.,
RA Malinsky J., Opekarova M.;
RT "C terminus of Nce102 determines the structure and function of microdomains
RT in the Saccharomyces cerevisiae plasma membrane.";
RL Eukaryot. Cell 9:1184-1192(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in membrane organization. Required for the formation
CC of membrane compartments of CAN1 (MCCs), localization of CAN1 at the
CC MCCs and subsequent invagination of the plasma membrane at the MCCs
CC sites. Involved in eisosome organization and might act as a sensor of
CC sphingolipids that regulates plasma membrane function. Involved in a
CC novel pathway of export of proteins that lack a cleavable signal
CC sequence. It may be an accessory subunit to an essential core component
CC of the non-classical export machinery. Non-classical export pathway
CC functions also as an alternative clearance/detoxification pathway to
CC eliminate damaged material, when the basic repair pathway is not
CC sufficient. {ECO:0000269|PubMed:10716729, ECO:0000269|PubMed:17415679,
CC ECO:0000269|PubMed:19064668, ECO:0000269|PubMed:19564405,
CC ECO:0000269|PubMed:20581291, ECO:0000269|PubMed:8655575}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10716729,
CC ECO:0000269|PubMed:12469340, ECO:0000269|PubMed:19064668,
CC ECO:0000269|PubMed:19564405, ECO:0000269|PubMed:20581291}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10716729,
CC ECO:0000269|PubMed:12469340, ECO:0000269|PubMed:19064668,
CC ECO:0000269|PubMed:19564405, ECO:0000269|PubMed:20581291}.
CC Note=Associates with the ergosterol-rich membrane compartment of CAN1
CC (MCC). Accumulates in membrane domains at eisosomes.
CC -!- DOMAIN: The C terminus is necessary to target MCC-specific transporters
CC into MCC and for the formation of the plasma membrane invaginations.
CC {ECO:0000269|PubMed:20581291}.
CC -!- SIMILARITY: Belongs to the NCE102 family. {ECO:0000305}.
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; U41659; AAB05589.1; -; mRNA.
DR EMBL; U65683; AAB06618.1; -; Genomic_DNA.
DR EMBL; U40829; AAB68287.1; -; Genomic_DNA.
DR EMBL; AY558523; AAS56849.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11562.1; -; Genomic_DNA.
DR PIR; S69036; S69036.
DR RefSeq; NP_015475.1; NM_001184246.1.
DR AlphaFoldDB; Q12207; -.
DR BioGRID; 36317; 68.
DR DIP; DIP-5397N; -.
DR IntAct; Q12207; 31.
DR STRING; 4932.YPR149W; -.
DR TCDB; 8.A.148.1.1; the plasma membrane organizing center, eisosome (eisosome) family.
DR TCDB; 9.A.27.1.1; the non-classical protein exporter (ncpe) family.
DR iPTMnet; Q12207; -.
DR MaxQB; Q12207; -.
DR PaxDb; Q12207; -.
DR PRIDE; Q12207; -.
DR TopDownProteomics; Q12207; -.
DR EnsemblFungi; YPR149W_mRNA; YPR149W; YPR149W.
DR GeneID; 856272; -.
DR KEGG; sce:YPR149W; -.
DR SGD; S000006353; NCE102.
DR VEuPathDB; FungiDB:YPR149W; -.
DR eggNOG; ENOG502RZW2; Eukaryota.
DR GeneTree; ENSGT00940000176512; -.
DR HOGENOM; CLU_098356_1_0_1; -.
DR InParanoid; Q12207; -.
DR OMA; QGSGKRC; -.
DR BioCyc; YEAST:G3O-34281-MON; -.
DR ChiTaRS; NCE102; yeast.
DR PRO; PR:Q12207; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12207; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0033101; C:cellular bud membrane; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; ISM:SGD.
DR GO; GO:0070250; C:mating projection membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0070941; P:eisosome assembly; IMP:SGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:SGD.
DR GO; GO:0007009; P:plasma membrane organization; IMP:SGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:SGD.
DR GO; GO:0009306; P:protein secretion; IMP:SGD.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0061091; P:regulation of phospholipid translocation; IGI:SGD.
DR InterPro; IPR008253; Marvel.
DR Pfam; PF01284; MARVEL; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..173
FT /note="Non-classical export protein 2"
FT /id="PRO_0000096760"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..37
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 173 AA; 18967 MW; DA7630E5B516160E CRC64;
MLALADNILR IINFLFLVIS IGLISSLLNT QHRHSSRVNY CMFACAYGIF TDSLYGVFAN
FIEPLAWPLV LFTLDFLNFV FTFTAGTVLA VGIRAHSCNN SSYVDSNKIT QGSGTRCRQA
QAAVAFLYFS CAIFLAKTLM SVFNMISNGA FGSGSFSKRR RTGQVGVPTI SQV
