SIP5_YEAS7
ID SIP5_YEAS7 Reviewed; 489 AA.
AC A6ZMK0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Protein SIP5;
DE AltName: Full=SNF1-interacting protein 5;
GN Name=SIP5; ORFNames=SCY_4316;
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: May negatively regulate the SNF1 kinase by promoting the
CC interaction of the REG1/GLC7 phosphatase complex with the kinase.
CC Deletion of SIP5 promotes resistance to artimisin, which is probably an
CC indirect effect of an action on the electron transport chain (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SNF1 and REG1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SIP5 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; AAFW02000021; EDN64074.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZMK0; -.
DR PRIDE; A6ZMK0; -.
DR EnsemblFungi; EDN64074; EDN64074; SCY_4316.
DR HOGENOM; CLU_009068_2_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR InterPro; IPR039301; Sip5/DA2.
DR PANTHER; PTHR31315; PTHR31315; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Phosphoprotein.
FT CHAIN 1..489
FT /note="Protein SIP5"
FT /id="PRO_0000333446"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40210"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P40210"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P40210"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40210"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P40210"
SQ SEQUENCE 489 AA; 55814 MW; BCF7C4D78A4B1854 CRC64;
MGNVPGKIDQ EDSFNDVRPD SSYNTTSSNS VIKQYDEEAS SRVRTRRTTS LVNNILNGNN
ARTKTGSHLS STSRRKTSRE KELAKEAHAK QLVVRCSETV DGGFLAPFGC YSFEKLDYDA
TVVKNLIIKR KLAPFYTPLQ DFDESWTRDE LIKIVDGLPL HDTFDENLEE FEDVPIGNLR
KSTFNELIDK SLSKKEQRRM HAKIFRARLY KKRILWQENE NETFLERKLE MKRIGSKSSN
VEDNTSSQPR KNYHLPSDDL KYTLYKNGSE CPICFLYFPG PFNYSKCCQQ PICTECFVQI
KRADPHFPHD EVDPTEPQTN DSEKDPNLLT SEPANCPYCA TASFSITYQP PTNRETGIGG
MPADSYVYKD AAISRADGGQ PNIPAITSDT IRPDWEIKLN KERARLMRRS ANATAIHISN
RLIDPSHSTR RNTSHSITPI HDESTSASRS PEPTINELED QMVREAIRLS LEDQDNRKKS
KNRNTSLRP