FIT1_YEAST
ID FIT1_YEAST Reviewed; 528 AA.
AC Q04433; D6VTF5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Facilitator of iron transport 1;
DE Flags: Precursor;
GN Name=FIT1; OrderedLocusNames=YDR534C; ORFNames=D9719.37;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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=9613572; DOI=10.1007/s004380050706;
RA Hamada K., Fukuchi S., Arisawa M., Baba M., Kitada K.;
RT "Screening for glycosylphosphatidylinositol (GPI)-dependent cell wall
RT proteins in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 258:53-59(1998).
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 FUNCTION, SUBCELLULAR LOCATION, 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).
RN [6]
RP REPEATS.
RX PubMed=16086015; DOI=10.1038/ng1618;
RA Verstrepen K.J., Jansen A., Lewitter F., Fink G.R.;
RT "Intragenic tandem repeats generate functional variability.";
RL Nat. Genet. 37:986-990(2005).
CC -!- FUNCTION: Involved in the uptake of non-siderophore sources of iron and
CC the siderophores ferrioxamine B and ferrichrome. Has a role in the
CC retention of iron in the cell wall and periplasmic space.
CC {ECO:0000269|PubMed:11673473}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-
CC anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-
CC CWP).
CC -!- INDUCTION: By iron. {ECO:0000269|PubMed:11673473}.
CC -!- DOMAIN: The number of the intragenic tandem repeats varies between
CC different S.cerevisiae strains.
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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U33057; AAB64973.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12365.1; -; Genomic_DNA.
DR PIR; S69589; S69589.
DR RefSeq; NP_010823.1; NM_001180842.1.
DR AlphaFoldDB; Q04433; -.
DR BioGRID; 32583; 64.
DR DIP; DIP-5274N; -.
DR IntAct; Q04433; 1.
DR STRING; 4932.YDR534C; -.
DR PaxDb; Q04433; -.
DR PRIDE; Q04433; -.
DR EnsemblFungi; YDR534C_mRNA; YDR534C; YDR534C.
DR GeneID; 852147; -.
DR KEGG; sce:YDR534C; -.
DR SGD; S000002942; FIT1.
DR VEuPathDB; FungiDB:YDR534C; -.
DR eggNOG; ENOG502T53S; Eukaryota.
DR GeneTree; ENSGT00940000176726; -.
DR HOGENOM; CLU_597455_0_0_1; -.
DR InParanoid; Q04433; -.
DR OMA; TTEYETK; -.
DR BioCyc; YEAST:G3O-30045-MON; -.
DR PRO; PR:Q04433; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04433; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 ATP-binding; Cell wall; Glycoprotein; GPI-anchor; Ion transport; Iron;
KW Iron transport; Lipoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..506
FT /note="Facilitator of iron transport 1"
FT /id="PRO_0000021265"
FT PROPEP 507..528
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021266"
FT REPEAT 20..98
FT /note="1-1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 99..168
FT /note="1-2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 169..233
FT /note="1-3"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 234..274
FT /note="1-4; truncated"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 289..294
FT /note="2-1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 295..300
FT /note="2-2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 301..306
FT /note="2-3"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 307..312
FT /note="2-4"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 313..318
FT /note="2-5"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 319..324
FT /note="2-6"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 325..330
FT /note="2-7"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 331..336
FT /note="2-8"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 337..342
FT /note="2-9"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 343..348
FT /note="2-10"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 349..353
FT /note="2-11"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 354..359
FT /note="2-12"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REGION 20..274
FT /note="4 X approximate tandem repeats"
FT REGION 79..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..359
FT /note="12 X 6 AA approximate tandem repeats, Ser/Thr-rich"
FT REGION 298..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 488..495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT LIPID 506
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 528 AA; 52490 MW; 42A31EF67E416E0D CRC64;
MKLSSAFVLS AITVAALGES ITTTITATKN GHVYTKTVTQ DATFVWAGEG AAVTSAVTEA
STVAATSAAA ETSVAAETSI VEPSTSAQGT SADEGSGSSI TTTITATKNG HVYTKTVTQD
ATFVWTGEGE RAPASTVATV ETSVAAETSV AEPSTSAQGT SADEGSGSSI TTTITATKNG
HVYTKTVTQD ATFVWTGEGE RAPVSTVATV ETAASPVTSV AEPSASTDEG SGSSITTTIT
ATKNGHVYTK TVTQDATFVW TGEGERAPAS TVATSSISAI EIPSTTEASI VEASSAVETS
SAAETSSAVE TSSAVETSSA VETSSAAETS SAAETSSAVE TSSAVEISSA VETSAVETSS
SSSTIETTSV KSLSPTQTSL SSSVQASSPI ETSSAAKTSS VVPTFSSTTT ENSSNSKSTS
AVVASTTTSS ESSATIVTPT RIGQAYTESS SRDAQSVRTH ESNNWSSSSS ASTKMVSSIT
RVQTTTAGIF TNGKSSTTPQ IVNYTGAADS IAAGTGLMGA ALAAVIFL
