ZRG8_YEAS7
ID ZRG8_YEAS7 Reviewed; 1076 AA.
AC A6ZQY2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Zinc-regulated protein 8;
GN Name=ZRG8; ORFNames=SCY_1529;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Involved in the integrity functions of RAM, a conserved
CC signaling network that regulates maintenance of polarized growth and
CC daughter-cell-specific transcription. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BUD27, GIS1 and SSD1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Bud {ECO:0000250}. Bud
CC neck {ECO:0000250}. Bud tip {ECO:0000250}. Note=Localized to the cortex
CC of small and large buds during bud growth, to the bud neck during
CC mitotic exit and to the tips of mating projections in pheromone-treated
CC cells. {ECO:0000250}.
CC -!- INDUCTION: Repressed by zinc. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ZRG8 family. {ECO:0000305}.
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DR EMBL; AAFW02000048; EDN63002.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZQY2; -.
DR SMR; A6ZQY2; -.
DR PRIDE; A6ZQY2; -.
DR EnsemblFungi; EDN63002; EDN63002; SCY_1529.
DR HOGENOM; CLU_301677_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0005934; C:cellular bud tip; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
PE 3: Inferred from homology;
KW Cytoplasm; Phosphoprotein; Zinc.
FT CHAIN 1..1076
FT /note="Zinc-regulated protein 8"
FT /id="PRO_0000333505"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..450
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40021"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40021"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40021"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40021"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40021"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40021"
SQ SEQUENCE 1076 AA; 119393 MW; 5F383AA330417BBC CRC64;
MRSFIKAHKK STSFDESPKR HSNFSGNTNN SSQRSSDDSL DFLPSTPSQM NYDSIPPPAK
HSPGFESFHR LANKTSKLFK KTSNSNLNSH LASTPTTSTN QTTSNSFVLQ NPPTKNTGPP
PPLPPPLFPS SSTSSFSRHD NESEYTAYKK TSPAKDFNRT TDSLPAIKGT ITHSWGDSKV
ESHVIILNDP ASPASNTSEA TSSKQFKTPI IGNENLTSTT SPSNLEPAIR ILNKNKGKQQ
ENIDDAEDGS SKKEHHVYKA LALAKNRNRQ ARIHSHDDII NLGKASQMDM SLLAAAFSGN
STTTINNDQS SNEQTDEKIL DIERVTTTST LTSSETTSPI NKSPCFYSQT LSLSPKIRHG
DLQSSPSKVN KNDSQNETLN KKKVRISLNR KEEEKVYSLN NNSDEYSVNE KETHKANDCN
DESSENGDGD NDHDDDYDDD DDDDDDDDES EFSFEYAGIN VRTSSVKYYS KPEPAANVYI
DDLYEDENFD DDMNCIEDDE SGNEGNEICG LSTRFEETSL KSNKVKKFND LFNLSDDDEE
EDGKDNSNNG DENESDNLYQ KRLENGKETF NGNHGGHHDD ASLGETVDNK EQFLINDNVK
KPIQKYNDLF DLSDEDDNDD KEMSEAESYM FSDEAPSIES GPANAKSTRG IYSQSNKNII
RDGKPNYSFS LKRNNSDDET EHTSAIKASL TGTTGSTKPT VKSFSDIFNV DDSASDAESD
SGTGGNNSNG LVSNDSERQV SLQSSLYETK SESHPPNHPH SQILQTPAKI VITPSVSDAQ
SQALAITDDD GEDDDDDTSS ILRTPFQLID SSHSQQPHYA SPQYTAVLNS PPLPPPARSQ
SLKYHDLNCD LDSEVPRPMS NLFFIDEAEE DEYNQKSKFF DFDHYDIDEI NGIPEDFNFS
DSERDDLNRR TLKSPLRGGS KNREVSPFSS VSSSFRSTHS FNGKLTINQG AKELAPMKNK
IELTNKTVTF FNSNNWNTYD CNSLSRKTSS QMRDSKYQNH NVGQNVEPSS VRSPQHQISN
GLDGKCNDNY VISPNLPTTI TPTNSFTKPT PEFSNDYSLS PIQETPSSVQ SSPKRA
