ARV1_YEAST
ID ARV1_YEAST Reviewed; 321 AA.
AC Q06541; D6VYP0; Q2VQX3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein ARV1;
GN Name=ARV1; OrderedLocusNames=YLR242C;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-81.
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16012843; DOI=10.1007/s00294-005-0001-x;
RA Zhang Z., Dietrich F.S.;
RT "Identification and characterization of upstream open reading frames (uORF)
RT in the 5' untranslated regions (UTR) of genes in Saccharomyces
RT cerevisiae.";
RL Curr. Genet. 48:77-87(2005).
RN [5]
RP FUNCTION.
RX PubMed=11063737; DOI=10.1074/jbc.c000710200;
RA Tinkelenberg A.H., Liu Y., Alcantara F., Khan S., Guo Z., Bard M.,
RA Sturley S.L.;
RT "Mutations in yeast ARV1 alter intracellular sterol distribution and are
RT complemented by human ARV1.";
RL J. Biol. Chem. 275:40667-40670(2000).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12145310; DOI=10.1074/jbc.m206624200;
RA Swain E., Stukey J., McDonough V., Germann M., Liu Y., Sturley S.L.,
RA Nickels J.T. Jr.;
RT "Yeast cells lacking the ARV1 gene harbor defects in sphingolipid
RT metabolism. Complementation by human ARV1.";
RL J. Biol. Chem. 277:36152-36160(2002).
CC -!- FUNCTION: Mediator of sterol homeostasis involved in sterol uptake,
CC trafficking and distribution into membranes. Regulates also the
CC sphingolipid metabolism. Required for growth during anaerobiosis and
CC sterol uptake. {ECO:0000269|PubMed:11063737,
CC ECO:0000269|PubMed:12145310}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12145310}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12145310}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:12145310}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12145310}.
CC -!- SIMILARITY: Belongs to the ARV1 family. {ECO:0000305}.
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DR EMBL; U20865; AAB67397.1; -; Genomic_DNA.
DR EMBL; AY692846; AAT92865.1; -; Genomic_DNA.
DR EMBL; AY899245; AAX83930.1; -; mRNA.
DR EMBL; BK006945; DAA09556.1; -; Genomic_DNA.
DR PIR; S59388; S59388.
DR RefSeq; NP_013343.1; NM_001182129.1.
DR AlphaFoldDB; Q06541; -.
DR BioGRID; 31509; 516.
DR DIP; DIP-5171N; -.
DR IntAct; Q06541; 2.
DR MINT; Q06541; -.
DR STRING; 4932.YLR242C; -.
DR TCDB; 9.A.19.1.1; the lipid intermediate transporter (arv1) family.
DR PaxDb; Q06541; -.
DR PRIDE; Q06541; -.
DR EnsemblFungi; YLR242C_mRNA; YLR242C; YLR242C.
DR GeneID; 850943; -.
DR KEGG; sce:YLR242C; -.
DR SGD; S000004232; ARV1.
DR VEuPathDB; FungiDB:YLR242C; -.
DR eggNOG; KOG3134; Eukaryota.
DR GeneTree; ENSGT00390000002675; -.
DR HOGENOM; CLU_057366_2_0_1; -.
DR InParanoid; Q06541; -.
DR OMA; KITICDS; -.
DR BioCyc; YEAST:G3O-32349-MON; -.
DR Reactome; R-SCE-191273; Cholesterol biosynthesis.
DR PRO; PR:Q06541; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06541; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; IMP:SGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR GO; GO:0032366; P:intracellular sterol transport; IMP:SGD.
DR GO; GO:0097036; P:regulation of plasma membrane sterol distribution; IMP:SGD.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:SGD.
DR GO; GO:0006665; P:sphingolipid metabolic process; IBA:GO_Central.
DR GO; GO:0035376; P:sterol import; IMP:SGD.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR InterPro; IPR007290; Arv1.
DR PANTHER; PTHR14467; PTHR14467; 1.
DR Pfam; PF04161; Arv1; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Lipid metabolism;
KW Lipid transport; Membrane; Reference proteome; Sphingolipid metabolism;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..321
FT /note="Protein ARV1"
FT /id="PRO_0000228135"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 321 AA; 38194 MW; 2898F797A5805433 CRC64;
MICITCMRPV DSLYTVYSND HIQLTDCPYC QETVDKYVEI DNVLLFIDLL LLKAGAYRHL
VFNALELHLS KYPKRKALND CQCLRDYTQA LLFNVKNWFC KYDRLNRLWL LLLSFEIYLT
WVTEESKYIY YLNRNNNDGK LIMLSKKLPE SFKWDSAIMR NTITSKVFTW SPPIQYLYFA
SYCILDVSLF HTFTQYFILK KLHWKHYSVS SKDVISYTIL LSYGAKIFPI LMLIWPYDTL
ISMSIIKWVA NLYIIESLKI VTNLSYWNII KIFISVSLLR YFMVKPILIV FVAKFNFSVI
KNLIHQEFIL LLQKSGTYLL L
