AFB1_YEAST
ID AFB1_YEAST Reviewed; 224 AA.
AC Q07988; D6VY43;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=A-factor barrier protein 1 {ECO:0000303|PubMed:24121774};
DE Flags: Precursor;
GN Name=AFB1 {ECO:0000303|PubMed:24121774}; OrderedLocusNames=YLR040C;
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 SUBCELLULAR LOCATION.
RX PubMed=10383953; DOI=10.1128/jb.181.13.3886-3889.1999;
RA Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K.;
RT "Amino acid residues in the omega-minus region participate in cellular
RT localization of yeast glycosylphosphatidylinositol-attached proteins.";
RL J. Bacteriol. 181:3886-3889(1999).
RN [5]
RP INDUCTION.
RX PubMed=15604142; DOI=10.1073/pnas.0407611102;
RA Galgoczy D.J., Cassidy-Stone A., Llinas M., O'Rourke S.M., Herskowitz I.,
RA DeRisi J.L., Johnson A.D.;
RT "Genomic dissection of the cell-type-specification circuit in Saccharomyces
RT cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18069-18074(2004).
RN [6]
RP FUNCTION.
RX PubMed=24121774; DOI=10.1534/genetics.113.155846;
RA Huberman L.B., Murray A.W.;
RT "Genetically engineered transvestites reveal novel mating genes in budding
RT yeast.";
RL Genetics 195:1277-1290(2013).
CC -!- FUNCTION: MATalpha-specific protein that interferes with a-factor, the
CC pheromone secreted by MATa cells (PubMed:24121774). Contributes to
CC mating efficiency (PubMed:24121774). Acts to bind and sequester a-
CC factor rather than to degrade it, and promotes the efficient mating of
CC MATalpha cells by keeping the a-factor concentration at the plasma
CC membrane within the narrow range needed for accurate pheromone gradient
CC detection (Probable). {ECO:0000269|PubMed:24121774,
CC ECO:0000305|PubMed:24121774}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000305|PubMed:10383953}. Membrane {ECO:0000305}; Lipid-anchor,
CC GPI-anchor {ECO:0000305}.
CC -!- INDUCTION: Expression is up-regulated by the MCM1 alpha cell-type-
CC specific transcription factor. {ECO:0000269|PubMed:15604142}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SRP1/TIP1 family. {ECO:0000305}.
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DR EMBL; Z73212; CAA97568.1; -; Genomic_DNA.
DR EMBL; AY557938; AAS56264.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09359.1; -; Genomic_DNA.
DR PIR; S64867; S64867.
DR RefSeq; NP_013141.1; NM_001181927.1.
DR AlphaFoldDB; Q07988; -.
DR BioGRID; 31316; 27.
DR DIP; DIP-5030N; -.
DR IntAct; Q07988; 1.
DR STRING; 4932.YLR040C; -.
DR PaxDb; Q07988; -.
DR EnsemblFungi; YLR040C_mRNA; YLR040C; YLR040C.
DR GeneID; 850730; -.
DR KEGG; sce:YLR040C; -.
DR SGD; S000004030; AFB1.
DR VEuPathDB; FungiDB:YLR040C; -.
DR eggNOG; ENOG502S3Y9; Eukaryota.
DR HOGENOM; CLU_092872_0_0_1; -.
DR InParanoid; Q07988; -.
DR OMA; AFPWYSS; -.
DR BioCyc; YEAST:G3O-32198-MON; -.
DR PRO; PR:Q07988; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07988; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0000749; P:response to pheromone triggering conjugation with cellular fusion; IMP:SGD.
DR InterPro; IPR000992; SRP1_TIP1.
DR Pfam; PF00660; SRP1_TIP1; 1.
PE 2: Evidence at transcript level;
KW Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..203
FT /note="A-factor barrier protein 1"
FT /id="PRO_0000247442"
FT PROPEP 204..224
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000247443"
FT LIPID 203
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 224 AA; 24462 MW; 015A176232B737C3 CRC64;
MIFAPSFSLI KNILLVSFLI SHSFAAKTLT SSSNDDTLAR SAAADADMAF FMEFLNDFDT
AFPQYTSYMM QNHLTLPQPV ADYYYHMVDL ASTADLQSDI AQSFPFTQFQ TFITAFPWYT
SLLNKASATT IYLPQHFITG ETEATMTNSS YASQKNSVSN SVPFSTANAG QSMISMANEE
NSTTALISAS NSSSTSRTSQ SQNGAHAKSL YFPMALFGIF AVAL
