Q29536 (KPYR_CANFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate kinase isozymes R/L
EC=2.7.1.40

Gene names

Name:

PKLR

Organism

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis › Canis lupus

Protein attributes

Sequence length	574 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Plays a key role in glycolysis By similarity.
Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium By similarity. Potassium By similarity.
Enzyme regulation	Allosterically activated by fructose 1,6-bisphosphate By similarity.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Homotetramer By similarity.
Involvement in disease	Defects in PKLR are a cause of inherited hemolytic anemia, an autosomal recessive disease of the Basenji dog that closely resembles human pyruvate kinase deficiency.
Miscellaneous	There are 4 isozymes of pyruvate kinase in mammals: L, R, M1 and M2. L type is major isozyme in the liver, R is found in red cells, M1 is the main form in muscle, heart and brain, and M2 is found in early fetal tissues.
Sequence similarities	Belongs to the pyruvate kinase family.
Sequence caution	The sequence DN338485 differs from that shown. Reason: Derived from EST data.

Ontologies

Keywords
Biological process	Glycolysis
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate
Molecular function	Kinase Transferase
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway response to other organism Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro potassium ion binding Inferred from electronic annotation. Source: InterPro pyruvate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

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

Isoform R-type (identifier: Q29536-1)

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 L-type (identifier: Q29536-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MSSQENIQPQELWSRISKSQRDLAKSILIGAPG → ME

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 574	574	Pyruvate kinase isozymes R/L		PRO_0000112093
Regions
	Region	475 – 480	6	Allosteric activator binding By similarity
	Region	559 – 564	6	Allosteric activator binding By similarity
Sites
	Metal binding	118	1	Potassium By similarity
	Metal binding	120	1	Potassium By similarity
	Metal binding	156	1	Potassium By similarity
	Metal binding	157	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	315	1	Magnesium By similarity
	Metal binding	339	1	Magnesium By similarity
	Binding site	116	1	Substrate By similarity
	Binding site	338	1	Substrate; via amide nitrogen By similarity
	Binding site	339	1	Substrate; via amide nitrogen By similarity
	Binding site	371	1	Substrate By similarity
	Binding site	525	1	Allosteric activator By similarity
	Binding site	532	1	Allosteric activator By similarity
	Site	313	1	Transition state stabilizer By similarity
Natural variations
	Alternative sequence	1 – 33	33	MSSQE…IGAPG → ME in isoform L-type.		VSP_042444
Experimental info
	Sequence conflict	423	1	A → R in AAB31627. Ref.2
	Sequence conflict	458 – 459	2	GA → AT in AAB31627. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform R-type [UniParc]. Last modified March 21, 2012. Version 2. Checksum: F18E28450B1C7F30	FASTA	574	62,048
	10 20 30 40 50 60 MSSQENIQPQ ELWSRISKSQ RDLAKSILIG APGGPAGYLR RASVAQLTLE LGTAFFQQQQ 70 80 90 100 110 120 LSAAMADTFL EHLCLLDIDS EPVAARSTSI IATIGPASHS VERLKEMIKA GMNIARLNFS 130 140 150 160 170 180 HGSHEYHAQS IANIREAVES FATSPLGYRP VAIALDTKGP EIRTGVLKGG PETEVELVKG 190 200 210 220 230 240 SWVLVTVDPA FRTLGDAHTV WVDYPNIVKV VPVGGRIFID DGLISLQVKK IDRKGLETQV 250 260 270 280 290 300 ENGGLLGSRK GVNLPGAEVD LPGLSEQDAQ DLRFGVEHNV DIVFASFVRK ASDVAAIRAA 310 320 330 340 350 360 LGPEGRTIKI ISKIENHEGV KKFDEILEVS DGIMVARGDL GIEIPAEKVF LAQKMMIGRC 370 380 390 400 410 420 NLAGKPVVCA TQMLESMITK PRPTRAETSD VANAVLDGAD CIMLSGETAK GKFPVEAVKM 430 440 450 460 470 480 QHAIAREAEA AVYHRQLFEE LRRAAPLSRD PTEVTAIGAV EAAFKCCAAA IIVLTKTGRS 490 500 510 520 530 540 AQLLSRYRPR AAVIAVTRSA QAARQAHLCR GVFPLLYSEP PEAIWADDVD RRVQFGIESG 550 560 570 KLRGFLRVGD LVIVVTGWRP GSGYTNIMRV LSIS
	Isoform L-type [UniParc]. Checksum: C4976F7282F91798	FASTA	543	58,657
	10 20 30 40 50 60 MEGPAGYLRR ASVAQLTLEL GTAFFQQQQL SAAMADTFLE HLCLLDIDSE PVAARSTSII 70 80 90 100 110 120 ATIGPASHSV ERLKEMIKAG MNIARLNFSH GSHEYHAQSI ANIREAVESF ATSPLGYRPV 130 140 150 160 170 180 AIALDTKGPE IRTGVLKGGP ETEVELVKGS WVLVTVDPAF RTLGDAHTVW VDYPNIVKVV 190 200 210 220 230 240 PVGGRIFIDD GLISLQVKKI DRKGLETQVE NGGLLGSRKG VNLPGAEVDL PGLSEQDAQD 250 260 270 280 290 300 LRFGVEHNVD IVFASFVRKA SDVAAIRAAL GPEGRTIKII SKIENHEGVK KFDEILEVSD 310 320 330 340 350 360 GIMVARGDLG IEIPAEKVFL AQKMMIGRCN LAGKPVVCAT QMLESMITKP RPTRAETSDV 370 380 390 400 410 420 ANAVLDGADC IMLSGETAKG KFPVEAVKMQ HAIAREAEAA VYHRQLFEEL RRAAPLSRDP 430 440 450 460 470 480 TEVTAIGAVE AAFKCCAAAI IVLTKTGRSA QLLSRYRPRA AVIAVTRSAQ AARQAHLCRG 490 500 510 520 530 540 VFPLLYSEPP EAIWADDVDR RVQFGIESGK LRGFLRVGDL VIVVTGWRPG SGYTNIMRVL SIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence, comparative analysis and haplotype structure of the domestic dog." Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R. , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S. Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Boxer.
[2]	"The molecular basis of canine pyruvate kinase deficiency." Whitney K.M., Goodman S.A., Bailey E.M., Lothrop C.D. Jr. Exp. Hematol. 22:866-874(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 56-574. Tissue: Reticulocyte.
[3]	Staten N.R. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-134 (ISOFORM L-TYPE). Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAEX03005338 Genomic DNA. No translation available. AH004600 mRNA. Translation: AAB31627.2. DN338485 mRNA. No translation available.
RefSeq	NP_001242947.1. NM_001256018.1. NP_001243191.1. NM_001256262.1.
3D structure databases
ProteinModelPortal	Q29536.
ModBase	Search...
Protein-protein interaction databases
STRING	9615.ENSCAFP00000030741.
Proteomic databases
PaxDb	Q29536.
PRIDE	Q29536.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	490425.
KEGG	cfa:490425.
Organism-specific databases
CTD	5313.
Phylogenomic databases
eggNOG	COG0469.
HOGENOM	HOG000021559.
HOVERGEN	HBG000941.
InParanoid	Q29536.
KO	K12406.
OrthoDB	EOG40GCQJ.
Enzyme and pathway databases
UniPathway	UPA00109; UER00188.
Family and domain databases
Gene3D	2.40.33.10. 1 hit. 3.20.20.60. 2 hits. 3.40.1380.20. 1 hit.
InterPro	IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase. IPR011037. Pyrv_Knase-like_insert_dom. IPR015794. Pyrv_Knase_a/b. IPR018209. Pyrv_Knase_AS. IPR015793. Pyrv_Knase_brl. IPR015795. Pyrv_Knase_C. IPR015806. Pyrv_Knase_insert_dom. [Graphical view]
PANTHER	PTHR11817. PTHR11817. 1 hit.
Pfam	PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view]
PRINTS	PR01050. PYRUVTKNASE.
SUPFAM	SSF50800. PK_B_barrel_like. 1 hit. SSF52935. Pyruvate_kinase. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR01064. pyruv_kin. 1 hit.
PROSITE	PS00110. PYRUVATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPYR_CANFA

Accession

Primary (citable) accession number: Q29536
Secondary accession number(s): F1P923, F1PXP8, F1PY57

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 21, 2012
Last modified:	April 3, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program