DFG16_YEAST
ID DFG16_YEAST Reviewed; 619 AA.
AC Q99234; D6W295;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein DFG16;
DE AltName: Full=Extracellular mutant protein 41;
DE AltName: Full=Zinc-regulated gene 11 protein;
GN Name=DFG16; Synonyms=ECM41, ZRG11; OrderedLocusNames=YOR030W;
GN ORFNames=OR26.20;
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=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 [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 IDENTIFICATION.
RX PubMed=9335584; DOI=10.1093/genetics/147.2.435;
RA Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J.,
RA Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C.,
RA Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M.,
RA Davies J., Klis F.M., Robbins P.W., Bussey H.;
RT "Large scale identification of genes involved in cell surface biosynthesis
RT and architecture in Saccharomyces cerevisiae.";
RL Genetics 147:435-450(1997).
RN [4]
RP IDENTIFICATION.
RX PubMed=9055077; DOI=10.1093/genetics/145.3.671;
RA Moesch H.-U., Fink G.R.;
RT "Dissection of filamentous growth by transposon mutagenesis in
RT Saccharomyces cerevisiae.";
RL Genetics 145:671-684(1997).
RN [5]
RP INDUCTION.
RX PubMed=10978274; DOI=10.1093/genetics/156.1.45;
RA Yuan D.S.;
RT "Zinc-regulated genes in Saccharomyces cerevisiae revealed by transposon
RT tagging.";
RL Genetics 156:45-58(2000).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Involved in invasion during filamentous growth.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Repressed by zinc. {ECO:0000269|PubMed:10978274}.
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DR EMBL; X87331; CAA60746.1; -; Genomic_DNA.
DR EMBL; Z74938; CAA99220.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10811.1; -; Genomic_DNA.
DR PIR; S54636; S54636.
DR RefSeq; NP_014673.1; NM_001183449.1.
DR AlphaFoldDB; Q99234; -.
DR SMR; Q99234; -.
DR BioGRID; 34432; 263.
DR STRING; 4932.YOR030W; -.
DR iPTMnet; Q99234; -.
DR PaxDb; Q99234; -.
DR PRIDE; Q99234; -.
DR EnsemblFungi; YOR030W_mRNA; YOR030W; YOR030W.
DR GeneID; 854195; -.
DR KEGG; sce:YOR030W; -.
DR SGD; S000005556; DFG16.
DR VEuPathDB; FungiDB:YOR030W; -.
DR eggNOG; ENOG502RJKI; Eukaryota.
DR HOGENOM; CLU_031414_0_0_1; -.
DR InParanoid; Q99234; -.
DR OMA; WNDYHET; -.
DR BioCyc; YEAST:G3O-33576-MON; -.
DR PRO; PR:Q99234; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q99234; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0071467; P:cellular response to pH; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR InterPro; IPR014844; PalH.
DR PANTHER; PTHR35779; PTHR35779; 1.
DR Pfam; PF08733; PalH; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..619
FT /note="Protein DFG16"
FT /id="PRO_0000079873"
FT TOPO_DOM 1
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..410
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..619
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 33..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 619 AA; 71730 MW; 129097C9C9C3B817 CRC64;
MIIRLHFYYL LTLVYHLGLV GAYEKAARKR IQPPDLIPGP PGHKLGDERP PHYDHRPPYK
KHIDNIPAYN LTDLIDDKLL NKYENSCTVN VLTGGFISLA SNSWHLRAYN YTLNYPSFLI
RCDNGSANPN FSHVLQDFVY DINNKFNVQD DSSKYIGKDP FPLGMIMITF ASGCICVATW
MLFLVVLLLP SDNHNRRNKV VHVYVLFSAI IRTVFLNETI AVIFDSQYHD DYQDASQFES
FIVETAPYKI CELVANILSD INWIYIVHYL QSNYGKPTWN WIPFKMKKGT HIIITVGCFL
SLADNILFAN LLWRKNLVVL KVFYKLIELL IYTIFISIIC YFTWHNFAYI LLPKTAEINT
DGKCKTKLRI LWENYHETIP LLAYNILIFI LFYFTTIFFA AFTKHVRGWT FNFVHLLKVL
ITVNVWGLIG VLEKRELHIS KKTVLGRKIN NRDKFFANPT VNYYGEDLGK HLSAITLNRD
LNTTKSNTTS HDSSSLVGSP SPTWKSPIER IRDRRRRHKI MKSENKFGQN PSFGSKSNGK
PNTKTTLSKY RQLLRKPRRK TNSYEPKNGI GQNKEGSTVR PGADKHIRDS NYLATDISDN
ESMETELRTN HIYNYENSD
