RMD5/YDR255C Protein Information

Standard Name	Rmd5p 1
Systematic Name	Ydr255cp
Alias	Gid2p 2, 3
ORF Classification	Verified
Description	Component of GID Complex that confers ubiquitin ligase (U3) activity; necessary for polyubiquitination and degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase; forms dimer with Fyv10p that is then recruited to GID Complex by Gid8p; also required for sporulation; conserved protein that has a degenerate RING finger domain (1, 3, 4, 5)
Name Description	Required for Meiotic nuclear Division 1

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	421
Molecular Weight (Da)	49,168
Isoelectric Point (pI)	8.26

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Rmd5p (InterPro)
Transmembrane Domains	There are 1 total predicted transmembrane domains (TMHMM)
Physical Interactions	There are 17 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000006C771 \| Q12508 MIPS: YDR255C NCBI: 1136210 \| 1226031 \| 398366289 \| 45269483 \| 59800204 \| NP_010541.3 GenBank/EMBL/DDBJ: DAA12095.1 \| AY557796 \| Z68329 \| Z70202

Amino Acid Sequence (or in FASTA format)
1 MSELLDSFET EFAKFYTDSN LEETNLQKCL DHTHEFKSQL KKLKAHLNKH 51 IQESKPEVYN KLSDKEKQKF KRKRELIIEK LSKSQRQWDH SVKKQIKYVS 101 QQSNRFNKST LNKLKEFDID SVYVNKLPKE TMENVNEAIG YHILRYSIDN 151 MPLGNKNEAF QYLKDVYGIT NKESTEFIEM GQIVHDLKKG DTESCLKWCS 201 NEMESLSSNH TALSSLKFDL YTLSAMQIVK HGNPVELYYQ ITQNAPLDCF 251 RHREKELMQN VVPLLTKSLI GQPIEDIDSK VNKELKECTS LFIKEYCAAK 301 HIFFDSPLFL IVLSGLISFQ FFIKYKTIRE LAHVDWTTKD ELPFDVKLPD 351 FLTHFHPIFI CPVLKEETTT ENPPYSLACH HIISKKALDR LSKNGTITFK 401 CPYCPVNTSM SSTKKVRFVM L*

Amino Acid Sequence (or in FASTA format)

       1  MSELLDSFET EFAKFYTDSN LEETNLQKCL DHTHEFKSQL KKLKAHLNKH
      51  IQESKPEVYN KLSDKEKQKF KRKRELIIEK LSKSQRQWDH SVKKQIKYVS
     101  QQSNRFNKST LNKLKEFDID SVYVNKLPKE TMENVNEAIG YHILRYSIDN
     151  MPLGNKNEAF QYLKDVYGIT NKESTEFIEM GQIVHDLKKG DTESCLKWCS
     201  NEMESLSSNH TALSSLKFDL YTLSAMQIVK HGNPVELYYQ ITQNAPLDCF
     251  RHREKELMQN VVPLLTKSLI GQPIEDIDSK VNKELKECTS LFIKEYCAAK
     301  HIFFDSPLFL IVLSGLISFQ FFIKYKTIRE LAHVDWTTKD ELPFDVKLPD
     351  FLTHFHPIFI CPVLKEETTT ENPPYSLACH HIISKKALDR LSKNGTITFK
     401  CPYCPVNTSM SSTKKVRFVM L*

external links for Rmd5p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Candida (CGD)	BioPIXIE	MIPS	YeastGFP
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	DIP
	GeneMANIA

References cited on this page View Complete Literature Guide for Rmd5p

1)	Enyenihi AH and Saunders WS (2003) Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae. Genetics 163(1):47-54
2)	Hammerle M, et al. (1998) Proteins of newly isolated mutants and the amino-terminal proline are essential for ubiquitin-proteasome-catalyzed catabolite degradation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae. J Biol Chem 273(39):25000-5
3)	Regelmann J, et al. (2003) Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell 14(4):1652-63
4)	Santt O, et al. (2008) The Yeast GID Complex, a Novel Ubiquitin Ligase (E3) Involved in the Regulation of Carbohydrate Metabolism. Mol Biol Cell 19(8):3323-33
5)	Menssen R, et al. (2012) Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite-induced degradation of gluconeogenic enzymes. J Biol Chem 287(30):25602-14