YGP1_YEAST
ID YGP1_YEAST Reviewed; 354 AA.
AC P38616; D6W123;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein YGP1;
DE AltName: Full=GP38;
DE Flags: Precursor;
GN Name=YGP1; OrderedLocusNames=YNL160W; ORFNames=N1731;
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], PROTEIN SEQUENCE OF 38-57; 186-216;
RP 319-330 AND 347-353, AND INDUCTION.
RX PubMed=8139573; DOI=10.1128/mcb.14.4.2740-2754.1994;
RA Destruelle M., Holzer H., Klionsky D.J.;
RT "Identification and characterization of a novel yeast gene: the YGP1 gene
RT product is a highly glycosylated secreted protein that is synthesized in
RT response to nutrient limitation.";
RL Mol. Cell. Biol. 14:2740-2754(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 145-156, AND SUBCELLULAR LOCATION.
RX PubMed=10234784;
RX DOI=10.1002/(sici)1097-0061(199904)15:6<459::aid-yea387>3.0.co;2-l;
RA Pardo M., Monteoliva L., Pla J., Sanchez M., Gil C., Nombela C.;
RT "Two-dimensional analysis of proteins secreted by Saccharomyces cerevisiae
RT regenerating protoplasts: a novel approach to study the cell wall.";
RL Yeast 15:459-472(1999).
RN [6]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18434410; DOI=10.1128/jvi.00412-08;
RA Luallen R.J., Lin J., Fu H., Cai K.K., Agrawal C., Mboudjeka I., Lee F.-H.,
RA Montefiori D., Smith D.F., Doms R.W., Geng Y.;
RT "An engineered Saccharomyces cerevisiae strain binds the broadly
RT neutralizing human immunodeficiency virus type 1 antibody 2G12 and elicits
RT mannose-specific gp120-binding antibodies.";
RL J. Virol. 82:6447-6457(2008).
CC -!- FUNCTION: May be involved in cellular adaptations prior to stationary
CC phase.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10234784,
CC ECO:0000269|PubMed:18434410}.
CC -!- INDUCTION: In response to nutrient limitation. Repressed by high
CC glucose concentrations. {ECO:0000269|PubMed:8139573}.
CC -!- PTM: Extensively N-glycosylated. {ECO:0000269|PubMed:18434410}.
CC -!- SIMILARITY: To yeast sporulation-specific protein SPS100.
CC {ECO:0000305}.
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DR EMBL; X73030; CAA51513.1; -; Genomic_DNA.
DR EMBL; X92517; CAA63279.1; -; Genomic_DNA.
DR EMBL; Z71436; CAA96047.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10389.1; -; Genomic_DNA.
DR PIR; S60967; S60967.
DR RefSeq; NP_014239.1; NM_001182998.1.
DR AlphaFoldDB; P38616; -.
DR SMR; P38616; -.
DR BioGRID; 35669; 80.
DR DIP; DIP-5199N; -.
DR IntAct; P38616; 4.
DR STRING; 4932.YNL160W; -.
DR CarbonylDB; P38616; -.
DR iPTMnet; P38616; -.
DR COMPLUYEAST-2DPAGE; P38616; -.
DR MaxQB; P38616; -.
DR PaxDb; P38616; -.
DR PRIDE; P38616; -.
DR EnsemblFungi; YNL160W_mRNA; YNL160W; YNL160W.
DR GeneID; 855562; -.
DR KEGG; sce:YNL160W; -.
DR SGD; S000005104; YGP1.
DR VEuPathDB; FungiDB:YNL160W; -.
DR eggNOG; KOG0503; Eukaryota.
DR GeneTree; ENSGT00940000176754; -.
DR HOGENOM; CLU_046466_0_0_1; -.
DR InParanoid; P38616; -.
DR OMA; TNYTRLF; -.
DR BioCyc; YEAST:G3O-33176-MON; -.
DR PRO; PR:P38616; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P38616; protein.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0070726; P:cell wall assembly; IDA:SGD.
DR InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR InterPro; IPR006034; Asparaginase/glutaminase-like.
DR PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR SMART; SM00870; Asparaginase; 1.
DR SUPFAM; SSF53774; SSF53774; 1.
DR PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..37
FT /evidence="ECO:0000269|PubMed:8139573"
FT /id="PRO_0000022705"
FT CHAIN 38..354
FT /note="Protein YGP1"
FT /id="PRO_0000022706"
FT DOMAIN 50..354
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 47
FT /note="N -> D (in Ref. 1; CAA51513)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="T -> R (in Ref. 1; CAA51513)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 37328 MW; 5A084DA27C1BA895 CRC64;
MKFQVVLSAL LACSSAVVAS PIENLFKYRA VKASHSKNIN STLPAWNGSN SSNVTYANGT
NSTTNTTTAE SSQLQIIVTG GQVPITNSSL THTNYTRLFN SSSALNITEL YNVARVVNET
IQDKSSAGAV VVANAKSLEA VSFFFSIIFD TEKPIVVTED SAYAIPVANN KNATKRGVLS
VTSDKLVYSG VFTPPTACSY GAGLPVAIVD DQDEVKWFFD ASKPTLISSD SIIRKEYSNF
TTPYGLLENG VPIVPIVYDG GYSSSLIDSL SSAVQGLVVV SSGSTNSTSS TIESTEIPVV
YAQANTPLNF IDNKDVPKNA VGAGYLSPIK AQILLSIAAV NGVTSKSALE SIFP
