Reviewed, UniProtKB/Swiss-Prot Q08824 (PARP1_ONCMA)

Names and origin

Protein names

Recommended name:
    Poly [ADP-ribose] polymerase
      Short name=PARP
    EC=2.4.2.30
Alternative name(s):
    ADPRT
    NAD(+) ADP-ribosyltransferase
    Poly[ADP-ribose] synthetase

Gene names

Name:	parp1
Synonyms:	adprt

Organism

Oncorhynchus masou (Cherry salmon) (Masu salmon)

Taxonomic identifier

8020 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Protacanthopterygii › Salmoniformes › Salmonidae › Salmoninae › Oncorhynchus

Protein attributes

Sequence length	135 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Poly[ADP-ribose] polymerase modifies various nuclear proteins by poly(ADP-ribosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage.
Catalytic activity	NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
Subcellular location	Nucleus.
Tissue specificity	Predominantly expressed in ovary, oocytes and brain. Low expression in liver.
Miscellaneous	The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxyl group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.
Sequence similarities	Contains 1 PARP alpha-helical domain. Contains 1 PARP catalytic domain.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding NAD Zinc
Molecular function	Glycosyltransferase Transferase
PTM	ADP-ribosylation
Gene Ontology (GO)
Biological process	protein amino acid ADP-ribosylation Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW NAD+ ADP-ribosyltransferase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›135	›135	Poly [ADP-ribose] polymerase		PRO_0000211323
Regions
	Domain	‹1 – 21	›21	PARP alpha-helical
	Domain	30 – ›135	›106	PARP catalytic
Sites
	Active site	135	1	By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	135	1

Sequences

	Sequence		Length	Mass (Da)
	Q08824-1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: A60E8E98890E42DC	FASTA	135	15,411
	10 20 30 40 50 60 QAKVEMLDNL LDIEVAYSLL KGGAEDNKKD PIDINYEKLK TKIEVVDKTT KEAEIILQYV 70 80 90 100 110 120 KNTHAATHNT YTLVVEEIFK IVREGEYQKY RPFQDLPNRQ LLWHGSRATN YAGILSQGLR 130 IAPPEAPVTG YMFGK

References

[1]

"Isolation of cDNAs encoding the catalytic domain of poly(ADP-ribose) polymerase from Xenopus laevis and cherry salmon using heterologous oligonucleotide consensus sequences." Ozawa Y., Uchida K., Uchida M., Ami Y., Kushida S., Okada N., Miwa M. Biochem. Biophys. Res. Commun. 193:119-125(1993) [PubMed: 8503897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	D13809 mRNA. Translation: BAA02965.1.
PIR	PN0494.
3D structure databases
HSSP	HSSP built from PDB template 1A26 based on UniProtKB P26446.
SMR	Q08824. Positions 1-135.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q08824.
Enzyme and pathway databases
BRENDA	2.4.2.30. 274804.
Family and domain databases
InterPro	IPR012317. PARP_catalytic. IPR004102. PARP_reg. IPR001510. Znf_PARP. [Graphical view]
Gene3D	G3DSA:1.20.142.10. PARP_reg. 1 hit.
Pfam	PF00644. PARP. 1 hit. PF02877. PARP_reg. 1 hit. [Graphical view]
PROSITE	PS51060. PARP_ALPHA_HD. 1 hit. PS51059. PARP_CATALYTIC. 1 hit. PS00347. PARP_ZN_FINGER_1. Partial match. PS50064. PARP_ZN_FINGER_2. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PARP1_ONCMA

Accession

Primary (citable) accession number: Q08824

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)