NF2IP_RAT
ID NF2IP_RAT Reviewed; 414 AA.
AC Q6AYG7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=NFATC2-interacting protein;
DE AltName: Full=Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein;
GN Name=Nfatc2ip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-54; SER-83 AND
RP SER-87, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-
CC driven transcription of a specific subset of cytokine genes, including
CC IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4
CC promoter; this leads to enhancement of histone H4 'Arg-3'-methylation
CC and facilitates subsequent histone acetylation at the IL4 locus, thus
CC promotes robust cytokine expression (By similarity). Down-regulates
CC formation of poly-SUMO chains by UBE2I/UBC9 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NFATC2, TRAF1, TRAF2 and PRMT1. Interacts with
CC UBE2I/UBC9 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=TRAF1 is associated with a fraction of NFATC2IP in the cytoplasm
CC and prevents its translocation to the nucleus. {ECO:0000250}.
CC -!- PTM: Methylation at the N-terminus by PRMT1 modulates interaction with
CC the NFAT complex and results in augmented cytokine production.
CC {ECO:0000250}.
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DR EMBL; BC079050; AAH79050.1; -; mRNA.
DR RefSeq; NP_001007693.1; NM_001007692.1.
DR AlphaFoldDB; Q6AYG7; -.
DR SMR; Q6AYG7; -.
DR STRING; 10116.ENSRNOP00000041221; -.
DR iPTMnet; Q6AYG7; -.
DR PhosphoSitePlus; Q6AYG7; -.
DR jPOST; Q6AYG7; -.
DR PaxDb; Q6AYG7; -.
DR PRIDE; Q6AYG7; -.
DR Ensembl; ENSRNOT00000090200; ENSRNOP00000073844; ENSRNOG00000057384.
DR GeneID; 308983; -.
DR KEGG; rno:308983; -.
DR UCSC; RGD:1359096; rat.
DR CTD; 84901; -.
DR RGD; 1359096; Nfatc2ip.
DR eggNOG; KOG1769; Eukaryota.
DR GeneTree; ENSGT00390000007119; -.
DR HOGENOM; CLU_055132_1_0_1; -.
DR InParanoid; Q6AYG7; -.
DR OMA; NVVDHMA; -.
DR OrthoDB; 979809at2759; -.
DR PhylomeDB; Q6AYG7; -.
DR TreeFam; TF328600; -.
DR PRO; PR:Q6AYG7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000057384; Expressed in testis and 18 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF11976; Rad60-SLD; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..414
FT /note="NFATC2-interacting protein"
FT /id="PRO_0000281011"
FT DOMAIN 343..414
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..229
FT /evidence="ECO:0000255"
FT COMPBIAS 11..30
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09130"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 311
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
SQ SEQUENCE 414 AA; 45430 MW; E11DAA35B3DB8F19 CRC64;
MAEPLRRRGP RSRGGRASRG ARRARAARGR CPRAPRSPTR LIPDTVLVDL VSDSDEEVLE
VVADPGEVPV ARLPAPAAPE QDSDSDSEGA AEGPAGAPRT LVRRRRRLLD PGEAPVVPVY
SGKVQSSLNL IPDNSSLLKL CPSEPEDEAD LTDSGSPPSE DALPPGSPWK KKLRKKHEKE
EKKMEEFPDQ DISPLPQPSS RNKSRKHTEA LQKLREVNKR LQDLRSCLSP KQHQSPALQN
TDDEVVLVEG SVLPQNPRLF TLKIRCRADL VRLPVKTSEP LQNVVDHMAS HLGVSPNRIL
LLFGETELSP TATPRTLKLG VADIIDCVVL ASSSEDTETS QELRLRVQGK EKHQMLEISL
SPDSPLKVLM SHYEEAMGLS GHKLSFFFDG TKLSGKELPT DLGLESGDLI EVWG
