PIR5_YEAST
ID PIR5_YEAST Reviewed; 287 AA.
AC P46999; D6VW27; Q86ZS0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cell wall protein PIR5;
DE AltName: Full=Protein with internal repeats 5;
DE Flags: Precursor;
GN Name=PIR5; OrderedLocusNames=YJL160C; ORFNames=J0555;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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] OF 144-223.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [4]
RP FUNCTION.
RX PubMed=12586695; DOI=10.1093/genetics/163.1.47;
RA Enyenihi A.H., Saunders W.S.;
RT "Large-scale functional genomic analysis of sporulation and meiosis in
RT Saccharomyces cerevisiae.";
RL Genetics 163:47-54(2003).
RN [5]
RP IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [6]
RP INDUCTION.
RX PubMed=16278933; DOI=10.1002/yea.1302;
RA de Lichtenberg U., Wernersson R., Jensen T.S., Nielsen H.B., Fausboell A.,
RA Schmidt P., Hansen F.B., Knudsen S., Brunak S.;
RT "New weakly expressed cell cycle-regulated genes in yeast.";
RL Yeast 22:1191-1201(2005).
CC -!- FUNCTION: Component of the outer cell wall layer (By similarity). May
CC be involved in meiosis and sporulation. {ECO:0000250,
CC ECO:0000269|PubMed:12586695}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CC Note=Covalently attached to the cell wall. {ECO:0000250}.
CC -!- INDUCTION: Cell cycle-regulated. Expression peaks during mitosis.
CC {ECO:0000269|PubMed:16278933}.
CC -!- DOMAIN: The PIR1/2/3 repeats are required for the covalent linkage to
CC the cell wall (By similarity). Their number varies among different
CC strains of S.cerevisiae. {ECO:0000250}.
CC -!- PTM: Covalently linked to beta-1,3-glucan of the inner cell wall layer
CC via an alkali-sensitive ester linkage between the gamma-carboxyl group
CC of glutamic acids, arising from specific glutamines within the PIR1/2/3
CC repeats, and hydroxyl groups of glucoses of beta-1,3-glucan chains.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIR protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA89455.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z49435; CAA89455.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY260893; AAP21761.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08643.1; -; Genomic_DNA.
DR PIR; S56943; S56943.
DR RefSeq; NP_012375.2; NM_001181593.1.
DR AlphaFoldDB; P46999; -.
DR BioGRID; 33600; 311.
DR DIP; DIP-1909N; -.
DR IntAct; P46999; 2.
DR MINT; P46999; -.
DR STRING; 4932.YJL160C; -.
DR PaxDb; P46999; -.
DR EnsemblFungi; YJL160C_mRNA; YJL160C; YJL160C.
DR GeneID; 853280; -.
DR KEGG; sce:YJL160C; -.
DR SGD; S000003696; PIR5.
DR VEuPathDB; FungiDB:YJL160C; -.
DR eggNOG; ENOG502QQD8; Eukaryota.
DR GeneTree; ENSGT00940000176741; -.
DR HOGENOM; CLU_039662_0_0_1; -.
DR InParanoid; P46999; -.
DR OMA; YEGTLEM; -.
DR BioCyc; YEAST:G3O-31600-MON; -.
DR PRO; PR:P46999; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P46999; protein.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
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; IPR000420; Yeast_PIR.
DR Pfam; PF00399; PIR; 3.
DR PROSITE; PS00929; PIR_REPEAT_1; 4.
DR PROSITE; PS50256; PIR_REPEAT_2; 4.
PE 2: Evidence at transcript level;
KW Cell wall; Cleavage on pair of basic residues; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..62
FT /evidence="ECO:0000250"
FT /id="PRO_0000377623"
FT CHAIN 63..287
FT /note="Cell wall protein PIR5"
FT /id="PRO_0000014333"
FT REPEAT 62..80
FT /note="PIR1/2/3 1"
FT REPEAT 81..99
FT /note="PIR1/2/3 2"
FT REPEAT 104..122
FT /note="PIR1/2/3 3"
FT REPEAT 144..162
FT /note="PIR1/2/3 4"
FT SITE 62..63
FT /note="Cleavage; by KEX2"
FT /evidence="ECO:0000255"
FT SITE 72
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 91
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 114
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 154
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
SQ SEQUENCE 287 AA; 30215 MW; 3E02845EA0DD7F33 CRC64;
MHYKKAFLAS LLSSIALTAY APPEPWATLT PSSKMDGGTT EYRTSFGLAV IPFTVTESKV
KRNVISQIND GQVQVTTQKL PHPVSQIGDG QIQVTTQKVP PVVSHIVSQI GDGQLQITTA
KNVVTKSTIA VPSKTVTATA TSTATAVSQI HDGQVQVTIS SASSSSVLSK SKLEPTKKPN
NEKVIKVQAC KSSGTLAITL QGGVLIDSSG RIGSIVANRQ FQFDGPPPQA GAIYAGGWSI
TKHGTLAIGD NDVFYQCLSG TFYNLYDQSI GGQCNPVHLQ TVGLVDC
