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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
 
 
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