RAG2_CHICK
ID RAG2_CHICK Reviewed; 528 AA.
AC P25022;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=V(D)J recombination-activating protein 2;
DE Short=RAG-2;
GN Name=RAG2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1986866; DOI=10.1016/0092-8674(91)90221-j;
RA Carlson L.M., Oettinger M.A., Schatz D.G., Masteller E.L., Hurley E.A.,
RA McCormack W.I., Baltimore D., Thompson C.B.;
RT "Selective expression of RAG-2 in chicken B cells undergoing immunoglobulin
RT gene conversion.";
RL Cell 64:201-208(1991).
CC -!- FUNCTION: Core component of the RAG complex, a multiprotein complex
CC that mediates the DNA cleavage phase during V(D)J recombination. V(D)J
CC recombination assembles a diverse repertoire of immunoglobulin and T-
CC cell receptor genes in developing B and T lymphocytes through
CC rearrangement of different V (variable), in some cases D (diversity),
CC and J (joining) gene segments. DNA cleavage by the RAG complex occurs
CC in 2 steps: a first nick is introduced in the top strand immediately
CC upstream of the heptamer, generating a 3'-hydroxyl group that can
CC attack the phosphodiester bond on the opposite strand in a direct
CC transesterification reaction, thereby creating 4 DNA ends: 2 hairpin
CC coding ends and 2 blunt, 5'-phosphorylated ends. In the RAG complex,
CC RAG2 is not the catalytic component but is required for all known
CC catalytic activities mediated by RAG1. It probably acts as a sensor of
CC chromatin state that recruits the RAG complex to H3K4me3 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the RAG complex composed of core components RAG1
CC and RAG2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The atypical PHD-type zinc finger recognizes and binds histone
CC H3 trimethylated on 'Lys-4' (H3K4me3). The atypical PHD-type zinc
CC finger also binds various phosphoinositides (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RAG2 family. {ECO:0000305}.
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DR EMBL; M58531; AAA49052.1; -; Genomic_DNA.
DR PIR; S42510; S42510.
DR AlphaFoldDB; P25022; -.
DR SMR; P25022; -.
DR STRING; 9031.ENSGALP00000012883; -.
DR PaxDb; P25022; -.
DR VEuPathDB; HostDB:geneid_423165; -.
DR eggNOG; ENOG502QVKU; Eukaryota.
DR HOGENOM; CLU_516740_0_0_1; -.
DR InParanoid; P25022; -.
DR PhylomeDB; P25022; -.
DR TreeFam; TF331236; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0097519; C:DNA recombinase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
DR GO; GO:0033151; P:V(D)J recombination; ISS:UniProtKB.
DR CDD; cd15569; PHD_RAG2; 1.
DR Gene3D; 2.120.10.80; -; 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR004321; RAG2.
DR InterPro; IPR025162; RAG2_PHD.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR PANTHER; PTHR10960; PTHR10960; 1.
DR Pfam; PF03089; RAG2; 1.
DR Pfam; PF13341; RAG2_PHD; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; DNA recombination; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..528
FT /note="V(D)J recombination-activating protein 2"
FT /id="PRO_0000167140"
FT ZN_FING 417..485
FT /note="PHD-type; atypical"
FT REGION 364..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 459
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 528 AA; 59089 MW; 53E511D79F59DA06 CRC64;
MSLQMVSAVS NSSLLQPGSS LLNFDGHVFF FGQKGWPKRS CPTGVFFLDI KQNELKMKPA
AFSRDSCYLP PLRYPAICTL RGNGESDKHQ YIIHGGKTPN NDLSDKIYIM SMVNKTTKKT
TFQCIEKDLG GDVPEARYGH TINVVHSRGK SMIVIFGGRS YIPLAQRTTE KWNSVVDCLP
SVFLVDFEFG CCTSYILPEL QDGLSFHVSV ARDDTIYILG GHSLQNNTRP PSLYKLKVDL
PLGSPCVTCS ILPGGISVSS GIVTQTGDTE FVLVGGYQSD NQKRMICNTI VLEDNKIEIV
ERVSPDWTPD IKHCRMWFGC DMGKGSVLLG IPGANKQLIS DANYFYILRC NKAEEDEEEE
LTAQTCSQAS TEDQGDSTPF EDSEEFSFSA EASSFDVDDI DTYNEDDEED ESETGYWIIC
CASCNIDINT WVPFYSTELN KPAMILCSSG SGHWVHAQCM DLSESMLLQL SEANVKYFCN
EHVHLNKGLQ TPKKAVHLKK QPMKRLHKKK TMKLTTPVKK SFLRRLFE
