NF2IP_MACFA
ID NF2IP_MACFA Reviewed; 408 AA.
AC Q9GLZ9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=NFATC2-interacting protein;
DE AltName: Full=Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein;
GN Name=NFATC2IP; ORFNames=QnpA-16750;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
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; AB050511; BAB17279.1; -; mRNA.
DR RefSeq; NP_001306469.1; NM_001319540.1.
DR AlphaFoldDB; Q9GLZ9; -.
DR BMRB; Q9GLZ9; -.
DR SMR; Q9GLZ9; -.
DR STRING; 9541.XP_005591595.1; -.
DR GeneID; 102144897; -.
DR eggNOG; KOG1769; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProt.
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; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..408
FT /note="NFATC2-interacting protein"
FT /id="PRO_0000281010"
FT DOMAIN 337..408
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 197..220
FT /evidence="ECO:0000255"
FT COMPBIAS 91..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYG7"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYG7"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09130"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09130"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09130"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 190
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 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 305
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 307
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NCF5"
SQ SEQUENCE 408 AA; 44581 MW; 5E0D6DD066AC2F24 CRC64;
MAEPVGKRGR LSRGSGAGRR PRAQRSPSRG TLDVVSVDLV SDSDEEIVEV TSARCAADEV
EVAPSEPPGP VASRDDSDSD SEGADARPAG PPREPVRRRR RLVLDPGEAP LVPVYSGKVK
SSLCLIPDDL SLLKLYPPGD EEEVELADSS GLYHEGSPSP GSPWKTKLRT KDKEEKKKTE
ILDLDNSPLS PPSPRTKSRK HTRALKKLSE VNKRLQDLRS CLSPEPPQGQ EQQGQEDEVV
LVEGPTLPET PRLFPLKIRC RADLVRLPLR MSEPLQSVVD HMATHLGVSP SRILLLFGET
ELSPTATPRT LKLGVADIID CVVLASSPEA TETSRQLQLR VQGKEKHQTL EVSLSRDSPL
KTLMSHYEEA MGLSGRKLSF FFDGTKLSGR ELPADLGMES GDLIEVWG
