P25022 (RAG2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
V(D)J recombination-activating protein 2
Short name=RAG-2

Gene names

Name:

RAG2

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	528 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. DNA cleavage by the RAG complex occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. In the RAG complex, RAG2 is not the catalytic component but is required for all known catalytic activities mediated by RAG1. It probably acts as a sensor of chromatin state that recruits the RAG complex to H3K4me3 By similarity.
Subunit structure	Component of the RAG complex composed of core components RAG1 and RAG2 By similarity.
Subcellular location	Nucleus By similarity.
Domain	The atypical PHD-type zinc finger recognizes and binds histone H3 trimethylated on 'Lys-4' (H3K4me3). The atypical PHD-type zinc finger also binds various phosphoinositides By similarity.
Sequence similarities	Belongs to the RAG2 family. Contains 1 PHD-type zinc finger.

Ontologies

Keywords
Biological process	DNA recombination
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB B cell homeostatic proliferation Inferred from electronic annotation. Source: Compara B cell lineage commitment Inferred from electronic annotation. Source: Compara T cell differentiation in thymus Inferred from sequence or structural similarity. Source: UniProtKB T cell lineage commitment Inferred from electronic annotation. Source: Compara V(D)J recombination Inferred from sequence or structural similarity. Source: UniProtKB chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of organ growth Inferred from electronic annotation. Source: Compara pre-B cell allelic exclusion Inferred from electronic annotation. Source: Compara
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro chromatin binding Inferred from sequence or structural similarity. Source: UniProtKB methylated histone residue binding Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylinositol-3,4,5-trisphosphate binding Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylinositol-3,4-bisphosphate binding Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylinositol-3,5-bisphosphate binding Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylinositol-4,5-bisphosphate binding Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 528	528	V(D)J recombination-activating protein 2		PRO_0000167140
Regions
	Zinc finger	417 – 485	69	PHD-type; atypical
	Compositional bias	354 – 413	60	Asp/Glu-rich (acidic)
Sites
	Metal binding	420	1	Zinc 1 By similarity
	Metal binding	424	1	Zinc 1 By similarity
	Metal binding	447	1	Zinc 2 By similarity
	Metal binding	453	1	Zinc 2 By similarity
	Metal binding	456	1	Zinc 1 By similarity
	Metal binding	459	1	Zinc 1 By similarity
	Metal binding	479	1	Zinc 2 By similarity
	Metal binding	482	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P25022 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 53E511D79F59DA06	FASTA	528	59,089
	10 20 30 40 50 60 MSLQMVSAVS NSSLLQPGSS LLNFDGHVFF FGQKGWPKRS CPTGVFFLDI KQNELKMKPA 70 80 90 100 110 120 AFSRDSCYLP PLRYPAICTL RGNGESDKHQ YIIHGGKTPN NDLSDKIYIM SMVNKTTKKT 130 140 150 160 170 180 TFQCIEKDLG GDVPEARYGH TINVVHSRGK SMIVIFGGRS YIPLAQRTTE KWNSVVDCLP 190 200 210 220 230 240 SVFLVDFEFG CCTSYILPEL QDGLSFHVSV ARDDTIYILG GHSLQNNTRP PSLYKLKVDL 250 260 270 280 290 300 PLGSPCVTCS ILPGGISVSS GIVTQTGDTE FVLVGGYQSD NQKRMICNTI VLEDNKIEIV 310 320 330 340 350 360 ERVSPDWTPD IKHCRMWFGC DMGKGSVLLG IPGANKQLIS DANYFYILRC NKAEEDEEEE 370 380 390 400 410 420 LTAQTCSQAS TEDQGDSTPF EDSEEFSFSA EASSFDVDDI DTYNEDDEED ESETGYWIIC 430 440 450 460 470 480 CASCNIDINT WVPFYSTELN KPAMILCSSG SGHWVHAQCM DLSESMLLQL SEANVKYFCN 490 500 510 520 EHVHLNKGLQ TPKKAVHLKK QPMKRLHKKK TMKLTTPVKK SFLRRLFE

References

[1]

"Selective expression of RAG-2 in chicken B cells undergoing immunoglobulin gene conversion." Carlson L.M., Oettinger M.A., Schatz D.G., Masteller E.L., Hurley E.A., McCormack W.I., Baltimore D., Thompson C.B. Cell 64:201-208(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M58531 Genomic DNA. Translation: AAA49052.1.
IPI	IPI00594284.
PIR	S42510.
UniGene	Gga.23148.
3D structure databases
ProteinModelPortal	P25022.
SMR	P25022. Positions 413-488.
ModBase	Search...
Protein-protein interaction databases
STRING	9031.ENSGALP00000012883.
Proteomic databases
PaxDb	P25022.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSGALT00000012898; ENSGALP00000012883; ENSGALG00000007940.
Phylogenomic databases
eggNOG	NOG39310.
GeneTree	ENSGT00390000012559.
HOGENOM	HOG000237346.
HOVERGEN	HBG006694.
InParanoid	P25022.
OMA	GHWVHAQ.
OrthoDB	EOG44XJGJ.
Family and domain databases
Gene3D	2.120.10.80. 1 hit.
InterPro	IPR011043. Gal_Oxase/kelch_b-propeller. IPR015915. Kelch-typ_b-propeller. IPR004321. RAG2. IPR025162. RAG2_PHD. [Graphical view]
PANTHER	PTHR10960. PTHR10960. 1 hit.
Pfam	PF03089. RAG2. 1 hit. PF13341. RAG2_PHD. 1 hit. [Graphical view]
SUPFAM	SSF50965. Gal_oxid_central. 1 hit.
PROSITE	PS01359. ZF_PHD_1. False negative. PS50016. ZF_PHD_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RAG2_CHICK

Accession

Primary (citable) accession number: P25022

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program