Q8BX10 (PGAM5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PGAM5, mitochondrial
EC=3.1.3.16

Alternative name(s):
Phosphoglycerate mutase family member 5

Gene names

Name:

Pgam5

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex. Contributes to the repression of NFE2L2-dependent gene expression By similarity. Acts as a central mediator for programmed necrosis induced by TNF, by reactive oxygen species and by calcium ionophore. Ref.3
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Subunit structure	Dimer. Forms a ternary complex with NFE2L2 and KEAP1. Interacts with BCL2L1 and MAP3K5 By similarity. Upon TNF-induced necrosis, forms in complex with RIPK1, RIPK3 and MLKL; the formation of this complex leads to PGAM5 phosphorylation By similarity. Interacts with DNM1L; this interaction leads to DNM1L dephosphorylation and activation and eventually to mitochondria fragmentation By similarity.
Subcellular location	Mitochondrion outer membrane; Single-pass membrane protein By similarity.
Domain	The N-terminal 35 amino acids, including the potential transmembrane alpha-helix, function as a non-cleaved mitochondrial targeting sequence that targets the protein to the cytosolic side of the outer mitochondrial membrane By similarity.
Post-translational modification	Phosphorylated by the RIPK1/RIPK3 complex under necrotic conditions. This phosphorylation increases PGAM5 phosphatase activity By similarity.
Sequence similarities	Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.
Sequence caution	The sequence BAB28067.1 differs from that shown. Reason: Frameshift at positions 52 and 66.

Ontologies

Keywords
Biological process	Necrosis
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phosphoprotein phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8BX10-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8BX10-2)

The sequence of this isoform differs from the canonical sequence as follows:
     195-195: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 288	288	Serine/threonine-protein phosphatase PGAM5, mitochondrial		PRO_0000288783
Regions
	Transmembrane	7 – 29	23	Helical; Potential
	Region	76 – 81	6	Interaction with KEAP1 By similarity
Amino acid modifications
	Modified residue	79	1	Phosphoserine By similarity
	Modified residue	115	1	N6-acetyllysine By similarity
	Modified residue	143	1	N6-acetyllysine By similarity
	Modified residue	190	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	195	1	Missing in isoform 2.		VSP_025762
Experimental info
	Sequence conflict	46	1	A → V in BAE26984. Ref.1
	Sequence conflict	102	1	I → M in BAC28763. Ref.1
	Sequence conflict	144	1	I → V in BAB28067. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: B704CDF4E640F888	FASTA	288	31,994
	10 20 30 40 50 60 MAFRQALQLA ACGLAGGSAA VLFSAVAVGK PRGGGDADTR ATEPPAWTGA RAGRGVWDTN 70 80 90 100 110 120 WDRREPLSLI NLKKRNVESG EDELTSRLDH YKAKATRHIF LIRHSQYHVD GSLEKDRTLT 130 140 150 160 170 180 PLGREQAELT GLRLASLGLK FNKIVHSSMT RAVETTDIIS KHLPGVSRVS TDLLREGAPI 190 200 210 220 230 240 EPDPPVSHWK PEAVQYYEDG ARIEAAFRNY IHRADARQEE DSYEIFICHA NVIRYIVCRA 250 260 270 280 LQFPPEGWLR LSLNNGSITH LVIRPNGRVA LRTLGDTGFM PPDKITRS
	Isoform 2 [UniParc]. Checksum: EF709F19D24DBBD6	FASTA	287	31,866
	10 20 30 40 50 60 MAFRQALQLA ACGLAGGSAA VLFSAVAVGK PRGGGDADTR ATEPPAWTGA RAGRGVWDTN 70 80 90 100 110 120 WDRREPLSLI NLKKRNVESG EDELTSRLDH YKAKATRHIF LIRHSQYHVD GSLEKDRTLT 130 140 150 160 170 180 PLGREQAELT GLRLASLGLK FNKIVHSSMT RAVETTDIIS KHLPGVSRVS TDLLREGAPI 190 200 210 220 230 240 EPDPPVSHWK PEAVYYEDGA RIEAAFRNYI HRADARQEED SYEIFICHAN VIRYIVCRAL 250 260 270 280 QFPPEGWLRL SLNNGSITHL VIRPNGRVAL RTLGDTGFMP PDKITRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6J, DBA/2 and NOD. Tissue: Thymus.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-288 (ISOFORM 1). Tissue: Brain and Embryo.
[3]	"The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways." Wang Z., Jiang H., Chen S., Du F., Wang X. Cell 148:228-243(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK012159 mRNA. Translation: BAB28067.1. Frameshift. AK034588 mRNA. Translation: BAC28763.1. AK049246 mRNA. Translation: BAC33634.1. AK146216 mRNA. Translation: BAE26984.1. AK169643 mRNA. Translation: BAE41272.1. BC052179 mRNA. Translation: AAH52179.1. BC138924 mRNA. Translation: AAI38925.1. BC138925 mRNA. Translation: AAI38926.1.
IPI	IPI00226387. IPI00848970.
RefSeq	NP_001157010.1. NM_001163538.1. NP_082549.2. NM_028273.3.
UniGene	Mm.61682.
3D structure databases
ProteinModelPortal	Q8BX10.
SMR	Q8BX10. Positions 88-288.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8BX10. 3 interactions.
PTM databases
PhosphoSite	Q8BX10.
Proteomic databases
PaxDb	Q8BX10.
PRIDE	Q8BX10.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000059229; ENSMUSP00000057760; ENSMUSG00000029500. ENSMUST00000112505; ENSMUSP00000108124; ENSMUSG00000029500.
GeneID	72542.
KEGG	mmu:72542.
UCSC	uc008yqh.2. mouse. uc008yqi.2. mouse.
Organism-specific databases
CTD	192111.
MGI	MGI:1919792. Pgam5.
Phylogenomic databases
eggNOG	NOG71348.
GeneTree	ENSGT00390000004796.
HOGENOM	HOG000261217.
HOVERGEN	HBG105576.
InParanoid	Q8BX10.
KO	K15637.
OMA	WLRMSLN.
OrthoDB	EOG4T4CW2.
Gene expression databases
Bgee	Q8BX10.
CleanEx	MM_PGAM5.
Genevestigator	Q8BX10.
Family and domain databases
InterPro	IPR013078. His_Pase_superF_clade-1. [Graphical view]
Pfam	PF00300. His_Phos_1. 1 hit. [Graphical view]
SMART	SM00855. PGAM. 1 hit. [Graphical view]
PROSITE	PS00175. PG_MUTASE. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	Pgam5. mouse.
NextBio	336451.
SOURCE	Search...

Entry information

Entry name

PGAM5_MOUSE

Accession

Primary (citable) accession number: Q8BX10
Secondary accession number(s): B2RSM6 , Q3UK19, Q80VY8, Q8BM78, Q9CZU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	March 1, 2003
Last modified:	April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program