FIT2_YEAST
ID FIT2_YEAST Reviewed; 153 AA.
AC Q08906; D6W375;
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 2;
DE Flags: Precursor;
GN Name=FIT2; OrderedLocusNames=YOR382W;
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:0000269|PubMed:10383953}. Membrane {ECO:0000269|PubMed:10383953};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10383953}.
CC Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
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.
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DR EMBL; Z75290; CAA99714.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11141.1; -; Genomic_DNA.
DR PIR; S67294; S67294.
DR RefSeq; NP_015027.1; NM_001183802.1.
DR AlphaFoldDB; Q08906; -.
DR BioGRID; 34763; 126.
DR DIP; DIP-5254N; -.
DR IntAct; Q08906; 2.
DR STRING; 4932.YOR382W; -.
DR iPTMnet; Q08906; -.
DR PaxDb; Q08906; -.
DR EnsemblFungi; YOR382W_mRNA; YOR382W; YOR382W.
DR GeneID; 854564; -.
DR KEGG; sce:YOR382W; -.
DR SGD; S000005909; FIT2.
DR VEuPathDB; FungiDB:YOR382W; -.
DR eggNOG; ENOG502SAAE; Eukaryota.
DR HOGENOM; CLU_1714345_0_0_1; -.
DR InParanoid; Q08906; -.
DR OMA; TYTEGPD; -.
DR BioCyc; YEAST:G3O-33844-MON; -.
DR PRO; PR:Q08906; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08906; 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.
DR InterPro; IPR035323; Fit1_2.
DR Pfam; PF17357; FIT1_2; 1.
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..130
FT /note="Facilitator of iron transport 2"
FT /id="PRO_0000021267"
FT PROPEP 131..153
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021268"
FT REGION 73..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 130
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 153 AA; 15302 MW; 74121DFF9325C211 CRC64;
MKFSTIFGAT TVMTAVSAAA VSSVMTTKTI TATNGNNVYT KVVTDTADPI ISYSTTRTVV
VSNSDATYTK VVTEGPDTTS EKSTTKTLTL TNGSGSSTNL YTKTVTQAVE SSTSSSSSSS
SSSSSASSSG AAPAAFQGAS VGALALGLIS YLL
