RAG2_ONCMY
ID RAG2_ONCMY Reviewed; 533 AA.
AC Q91193;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=V(D)J recombination-activating protein 2;
DE Short=RAG-2;
GN Name=rag2;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Shasta;
RX PubMed=8662087; DOI=10.1007/bf02602586;
RA Hansen J.D., Kaattari S.L.;
RT "The recombination activating gene 2 (RAG2) of the rainbow trout
RT Oncorhynchus mykiss.";
RL Immunogenetics 44:203-211(1996).
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 -!- DEVELOPMENTAL STAGE: First detected in the thymus during day 4 of
CC development. Expression then increases in the thymus for at least three
CC weeks.
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; U31670; AAB18138.1; -; Genomic_DNA.
DR EMBL; U25146; AAA65927.1; -; Genomic_DNA.
DR AlphaFoldDB; Q91193; -.
DR SMR; Q91193; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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: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 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 2: Evidence at transcript level;
KW Chromatin regulator; DNA recombination; Metal-binding; Nucleus; Zinc;
KW Zinc-finger.
FT CHAIN 1..533
FT /note="V(D)J recombination-activating protein 2"
FT /id="PRO_0000167142"
FT ZN_FING 419..488
FT /note="PHD-type; atypical"
FT REGION 358..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 449
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="2"
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 462
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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"
FT BINDING 485
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 533 AA; 59410 MW; 18AE5F4B79096D83 CRC64;
MSLQPLTAVN CGSLLQPGCS LLQLDGDIFL FGQKGWPRRS CPTGVFGVRL KHGELKLRPI
SSSNDSCYLP PLRCPALTRL EPHDGHPEGY LIHGGRTPNN EISSSLYLLT LDSRGCNRKV
TLRCQERELV GEQPGPRYGH TLSMVQSLGK RACVVFGGRS YMPAGERTTE NWNSVVDCPP
QVFIIDLEFG CCSAHTLPEL TDGQSFHLAL ARDDYVYFLG GQSLSLDFRP PRVYSLRDGV
PEGKPAVSCS TWTPSMSISS AIATRVGPSH EFIILGGYQL ETQKRMECSS VVLDDSGINI
EPREAPEWTG EIKHNHTWFG GSMGGGSALI GIPSEGRQAT PEAHYFYQVC FQKEGEGKGE
DGNQVCSQES TDFEDSAPLE DSEELYFGRE PHELEDSSEG EGDTYNEEDE EDESQTGYWV
KCCLGCQVDP NTWEPYYSTE LLRPAMIYCS KGEGGHWVHA QCMELTEGLL VRLSQGNGKY
FCLDHGGLPR QEMTPPRQVL SLKRSPMKPQ HRKGPMMRRM TPAKKRFFRR LFE
