FIT3_YEAST
ID FIT3_YEAST Reviewed; 204 AA.
AC Q08907; D6W376;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Facilitator of iron transport 3;
DE Flags: Precursor;
GN Name=FIT3; OrderedLocusNames=YOR383C;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=11673473; DOI=10.1074/jbc.m109220200;
RA Protchenko O., Ferea T., Rashford J., Tiedeman J., Brown P.O., Botstein D.,
RA Philpott C.C.;
RT "Three cell wall mannoproteins facilitate the uptake of iron in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 276:49244-49250(2001).
CC -!- FUNCTION: Involved in the uptake of non-siderophore and siderophore
CC sources of iron. Has a role in the retention of iron in the cell wall
CC and periplasmic space. {ECO:0000269|PubMed:11673473}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000305|PubMed:10383953}. Membrane {ECO:0000305}; Lipid-anchor,
CC GPI-anchor {ECO:0000305}.
CC -!- INDUCTION: By iron. {ECO:0000269|PubMed:11673473}.
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}.
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DR EMBL; Z75291; CAA99715.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11142.1; -; Genomic_DNA.
DR PIR; S67295; S67295.
DR RefSeq; NP_015028.3; NM_001183803.3.
DR AlphaFoldDB; Q08907; -.
DR BioGRID; 34764; 34.
DR DIP; DIP-4048N; -.
DR IntAct; Q08907; 1.
DR MINT; Q08907; -.
DR STRING; 4932.YOR383C; -.
DR PaxDb; Q08907; -.
DR PRIDE; Q08907; -.
DR EnsemblFungi; YOR383C_mRNA; YOR383C; YOR383C.
DR GeneID; 854565; -.
DR KEGG; sce:YOR383C; -.
DR SGD; S000005910; FIT3.
DR VEuPathDB; FungiDB:YOR383C; -.
DR eggNOG; ENOG502SP38; Eukaryota.
DR GeneTree; ENSGT00940000176726; -.
DR HOGENOM; CLU_113009_0_0_1; -.
DR InParanoid; Q08907; -.
DR OMA; TFVWEGE; -.
DR BioCyc; YEAST:G3O-33845-MON; -.
DR PRO; PR:Q08907; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08907; 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:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0015891; P:siderophore transport; IDA:SGD.
PE 2: Evidence at transcript level;
KW Cell wall; Glycoprotein; GPI-anchor; Ion transport; Iron; Iron transport;
KW Lipoprotein; Membrane; Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..182
FT /note="Facilitator of iron transport 3"
FT /id="PRO_0000021269"
FT PROPEP 183..204
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000372453"
FT REGION 84..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 182
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 204 AA; 19836 MW; AE79394A15B8F8A3 CRC64;
MKFSSALVLS AVAATALAES ITTTITATKN GHVYTKTVTQ DATFVWGGED SYASSTSAAE
SSAAETSAAE TSAAATTSAA ATTSAAETSS AAETSSADEG SGSSITTTIT ATKNGHVYTK
TVTQDATFVW TGEGSSNTWS PSSTSTSSEA ATSSASTTAT TTAETSSSAT SSSTAELSSY
TGAADAITAG TGLMGAALAA VMLL
