RAG2_XENLA
ID RAG2_XENLA Reviewed; 520 AA.
AC Q91830;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=V(D)J recombination-activating protein 2;
DE Short=RAG-2;
GN Name=rag2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=HD-1;
RX PubMed=8376769;
RA Greenhalgh P.H., Olesen C.E., Steiner L.A.;
RT "Characterization and expression of recombination activating genes (RAG-1
RT and RAG-2) in Xenopus laevis.";
RL J. Immunol. 151:3100-3110(1993).
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 -!- TISSUE SPECIFICITY: Expressed within the thymus, liver and spleen in
CC juvenile frogs, and within the thymus and bone marrow of adults. A
CC lower level expression is seen in the ovaries.
CC {ECO:0000269|PubMed:8376769}.
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. {ECO:0000269|PubMed:8376769}.
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; L19325; AAA49943.1; -; Genomic_DNA.
DR PIR; I51556; I51556.
DR RefSeq; XP_018114730.1; XM_018259241.1.
DR RefSeq; XP_018114731.1; XM_018259242.1.
DR RefSeq; XP_018114732.1; XM_018259243.1.
DR AlphaFoldDB; Q91830; -.
DR SMR; Q91830; -.
DR DNASU; 100037211; -.
DR GeneID; 100037211; -.
DR CTD; 100037211; -.
DR Xenbase; XB-GENE-1018151; rag2.S.
DR OMA; WNSVVDC; -.
DR OrthoDB; 687724at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 100037211; Expressed in egg cell and 17 other tissues.
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 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 2: Evidence at transcript level;
KW Chromatin regulator; DNA recombination; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..520
FT /note="V(D)J recombination-activating protein 2"
FT /id="PRO_0000167143"
FT ZN_FING 415..477
FT /note="PHD-type; atypical"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 520 AA; 58636 MW; E5105425D5295BDE CRC64;
MTLRIVTPGS NTSLIQPGFS LLHFSSHVFY LGQKGWPKRS CPTGVFLLDL KNNDLKLRPA
TFTNDSCYLP PLRHPAVCSF SASQGGEITQ YLIHGGKTPN NEISHKLYIM TMAFPVNKRF
SLCCSEKDLA GDVPEARYGH SMNVVFSRGK NAVVMFGGRS YMPLNQRTTE NWNNVIDCEP
LVYLIDLQFG CSTSFNLREL QDGLSFHVSL ARNDTVYIFG GHSLGNNFRP PNVYKIKVDL
PLGSPAVSCT VINSKISFSS SIVTQTSPDE FVIVGGYESD SQKRLICNGV FLDDETIDIQ
EIETPDWTGE IKHSKTWFGA DMGKGAVLFG IPVDNKHQST DCSFFFYVLN FGDNDPALQT
CSQGSTEEQE DSMPLEDSEE FTFNRDGNIF DEDTYNEDDE DDESVTGYWI KCCPDCDMDR
NTWEPFYSTE LNKPSMIFCS KDGGHWVHSQ CMDLSETMLK YLSQNNIKYF CNEHVEVARG
VQTPEKTPPV KKTSLKSVRK RTTINRLSAV KKSFLRRLFE
