FHN1_YEAST
ID FHN1_YEAST Reviewed; 174 AA.
AC P53279; D6VUR3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Non-classical export protein 2 homolog 1;
DE AltName: Full=Functional homolog of NCE102;
GN Name=FHN1; OrderedLocusNames=YGR131W;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 INDUCTION.
RX PubMed=12824174; DOI=10.1074/jbc.m306291200;
RA Agarwal A.K., Rogers P.D., Baerson S.R., Jacob M.R., Barker K.S.,
RA Cleary J.D., Walker L.A., Nagle D.G., Clark A.M.;
RT "Genome-wide expression profiling of the response to polyene, pyrimidine,
RT azole, and echinocandin antifungal agents in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:34998-35015(2003).
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 FUNCTION.
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).
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. Non-classical export pathway functions also as an alternative
CC clearance/detoxification pathway to eliminate damaged material, when
CC the basic repair pathway is not sufficient.
CC {ECO:0000269|PubMed:20581291}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Associates with the ergosterol-rich
CC membrane compartment of CAN1 (MCC). Accumulates in membrane domains at
CC eisosomes. {ECO:0000250}.
CC -!- INDUCTION: By ketoconazole. the promoter contains a sterol regulatory
CC element motif, which has been identified as a UPC2-binding site.
CC {ECO:0000269|PubMed:12824174}.
CC -!- SIMILARITY: Belongs to the NCE102 family. {ECO:0000305}.
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DR EMBL; Z72916; CAA97144.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08224.1; -; Genomic_DNA.
DR PIR; S64440; S64440.
DR RefSeq; NP_011647.1; NM_001181260.1.
DR AlphaFoldDB; P53279; -.
DR BioGRID; 33379; 49.
DR IntAct; P53279; 3.
DR MINT; P53279; -.
DR STRING; 4932.YGR131W; -.
DR TCDB; 9.A.27.1.2; the non-classical protein exporter (ncpe) family.
DR PaxDb; P53279; -.
DR PRIDE; P53279; -.
DR EnsemblFungi; YGR131W_mRNA; YGR131W; YGR131W.
DR GeneID; 853032; -.
DR KEGG; sce:YGR131W; -.
DR SGD; S000003363; FHN1.
DR VEuPathDB; FungiDB:YGR131W; -.
DR eggNOG; ENOG502RZW2; Eukaryota.
DR GeneTree; ENSGT00940000176512; -.
DR HOGENOM; CLU_098356_1_0_1; -.
DR InParanoid; P53279; -.
DR OMA; GFLANFW; -.
DR BioCyc; YEAST:G3O-30837-MON; -.
DR PRO; PR:P53279; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53279; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0070941; P:eisosome assembly; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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..174
FT /note="Non-classical export protein 2 homolog 1"
FT /id="PRO_0000202823"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 174 AA; 19152 MW; E5610CAF65323432 CRC64;
MLSAADNLVR IINAVFLIIS IGLISGLIGT QTKHSSRVNF CMFAAVYGLV TDSLYGFLAN
FWTSLTYPAI LLVLDFLNFI FTFVAATALA VGIRCHSCKN KTYLEQNKII QGSSSRCHQS
QAAVAFFYFS CFLFLIKVTV ATMGMMQNGG FGSNTGFSRR RARRQMGIPT ISQV
