TIR4_YEAST
ID TIR4_YEAST Reviewed; 487 AA.
AC Q12218; D6W276;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cell wall protein TIR4;
DE AltName: Full=TIP1-related protein 4;
DE Flags: Precursor;
GN Name=TIR4; OrderedLocusNames=YOR009W; ORFNames=UNB487;
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 [GENOMIC DNA].
RX PubMed=8896276;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1091::aid-yea22>3.0.co;2-i;
RA Sterky F., Holmberg A., Pettersson B., Uhlen M.;
RT "The sequence of a 30 kb fragment on the left arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 15 open reading frames, five of which
RT correspond to previously identified genes.";
RL Yeast 12:1091-1095(1996).
RN [2]
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 [3]
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 [4]
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 [5]
RP GPI-ANCHOR, AND 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 [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=11292809; DOI=10.1128/jb.183.9.2881-2887.2001;
RA Abramova N.E., Sertil O., Mehta S., Lowry C.V.;
RT "Reciprocal regulation of anaerobic and aerobic cell wall mannoprotein gene
RT expression in Saccharomyces cerevisiae.";
RL J. Bacteriol. 183:2881-2887(2001).
RN [7]
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: Component of the cell wall. Required for anaerobic growth.
CC {ECO:0000269|PubMed:11292809}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305|PubMed:10383953,
CC ECO:0000305|PubMed:9613572}. Membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- INDUCTION: Induced during anaerobic growth. Induced by cold shock.
CC {ECO:0000269|PubMed:11292809}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SRP1/TIP1 family. {ECO:0000305}.
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; U43491; AAC49489.1; -; Genomic_DNA.
DR EMBL; Z74917; CAA99197.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10792.1; -; Genomic_DNA.
DR PIR; S61993; S61993.
DR RefSeq; NP_014652.1; NM_001183428.1.
DR AlphaFoldDB; Q12218; -.
DR BioGRID; 34414; 82.
DR DIP; DIP-5194N; -.
DR IntAct; Q12218; 2.
DR MINT; Q12218; -.
DR STRING; 4932.YOR009W; -.
DR PaxDb; Q12218; -.
DR TopDownProteomics; Q12218; -.
DR EnsemblFungi; YOR009W_mRNA; YOR009W; YOR009W.
DR GeneID; 854173; -.
DR KEGG; sce:YOR009W; -.
DR SGD; S000005535; TIR4.
DR VEuPathDB; FungiDB:YOR009W; -.
DR eggNOG; ENOG502S6R6; Eukaryota.
DR GeneTree; ENSGT00940000176276; -.
DR HOGENOM; CLU_580257_0_0_1; -.
DR InParanoid; Q12218; -.
DR OMA; ITITYPQ; -.
DR BioCyc; YEAST:G3O-33559-MON; -.
DR PRO; PR:Q12218; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12218; 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:0005199; F:structural constituent of cell wall; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR InterPro; IPR000992; SRP1_TIP1.
DR Pfam; PF00660; SRP1_TIP1; 1.
DR PROSITE; PS00724; SRP1_TIP1; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..465
FT /note="Cell wall protein TIR4"
FT /id="PRO_0000267640"
FT PROPEP 466..487
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000267641"
FT REPEAT 137..148
FT /note="1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 149..160
FT /note="2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 161..172
FT /note="3"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 173..184
FT /note="4"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 185..196
FT /note="5"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 197..208
FT /note="6"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 209..220
FT /note="7"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 221..232
FT /note="8"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 233..244
FT /note="9"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 245..256
FT /note="10"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 257..268
FT /note="11"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REGION 137..268
FT /note="11 X 12 AA approximate tandem repeats, Ser-rich"
FT REGION 205..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 465
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 487 AA; 47849 MW; BA12415C400FAD65 CRC64;
MAYSKITLLA ALAAIAYAQT QAQINELNVV LDDVKTNIAD YITLSYTPNS GFSLDQMPAG
IMDIAAQLVA NPSDDSYTTL YSEVDFSAVE HMLTMVPWYS SRLLPELEAM DASLTTSSSA
ATSSSEVASS SIASSTSSSV APSSSEVVSS SVAPSSSEVV SSSVAPSSSE VVSSSVASSS
SEVASSSVAP SSSEVVSSSV ASSSSEVASS SVAPSSSEVV SSSVAPSSSE VVSSSVASSS
SEVASSSVAP SSSEVVSSSV ASSTSEATSS SAVTSSSAVS SSTESVSSSS VSSSSAVSSS
EAVSSSPVSS VVSSSAGPAS SSVAPYNSTI ASSSSTAQTS ISTIAPYNST TTTTPASSAS
SVIISTRNGT TVTETDNTLV TKETTVCDYS STSAVPASTT GYNNSTKVST ATICSTCKEG
TSTATDFSTL KTTVTVCDSA CQAKKSATVV SVQSKTTGIV EQTENGAAKA VIGMGAGALA
AVAAMLL