YN8B_YEAST
ID YN8B_YEAST Reviewed; 404 AA.
AC P53723; D6W1J6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=UPF0674 endoplasmic reticulum membrane protein YNR021W;
GN OrderedLocusNames=YNR021W; ORFNames=N3216;
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=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 [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 PROTEIN SEQUENCE OF 2-32; 93-101 AND 193-200, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:14562095}; Single-pass membrane protein
CC {ECO:0000305|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 34906 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UPF0674 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; Z71636; CAA96300.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10562.1; -; Genomic_DNA.
DR PIR; S63352; S63352.
DR RefSeq; NP_014418.3; NM_001183198.3.
DR AlphaFoldDB; P53723; -.
DR BioGRID; 35846; 100.
DR IntAct; P53723; 1.
DR MINT; P53723; -.
DR STRING; 4932.YNR021W; -.
DR iPTMnet; P53723; -.
DR MaxQB; P53723; -.
DR PaxDb; P53723; -.
DR PRIDE; P53723; -.
DR EnsemblFungi; YNR021W_mRNA; YNR021W; YNR021W.
DR GeneID; 855755; -.
DR KEGG; sce:YNR021W; -.
DR SGD; S000005304; YNR021W.
DR VEuPathDB; FungiDB:YNR021W; -.
DR eggNOG; KOG2357; Eukaryota.
DR GeneTree; ENSGT00390000013997; -.
DR HOGENOM; CLU_672638_0_0_1; -.
DR InParanoid; P53723; -.
DR OMA; AYNWTFE; -.
DR BioCyc; YEAST:G3O-33335-MON; -.
DR PRO; PR:P53723; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53723; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IEA:InterPro.
DR InterPro; IPR012879; CCDC47.
DR PANTHER; PTHR12883; PTHR12883; 1.
DR Pfam; PF07946; DUF1682; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT CHAIN 2..404
FT /note="UPF0674 endoplasmic reticulum membrane protein
FT YNR021W"
FT /id="PRO_0000203473"
FT TRANSMEM 49..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 369..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 404 AA; 47093 MW; F2A46081DF567929 CRC64;
MSSSIFGPLT GFLERVNSLN APYQALSYDE QKAMTIWQRV KFYNWTFELC ALGVLFLVYA
FYKFGNSVNL KRGNQIFQSL HSFLANDLKF SRVGFNINDS KIFTVEHQNT WFSSFATGRS
AIKSINLNLH LVARSNPFSM CLEYLLGFFF ASLKSKQLEE FMEIVIRPNG ILVTSESAHP
NKNAHEILTK FRFVTSIVNK EFMNQARTEN YFLSIAHTSE NDKLPNNFVY MSDVNQLSGF
MFHYSKPYEV LSQAGNLLKY ISFTDLPVNP PRDDKEWESS IEPKAIIRCA VPQNENELKL
LNQIISLVVE IYDGFTQDLV QQSPNLFITN DILKRTTNLR QQELNKIKKF MKETELELAK
EKKLELEKAK RRQLKASGQQ EKVDQKMKEK RERRLKNKQR TRFQ