ID   ICE2_BOVIN              Reviewed;         981 AA.
AC   Q0VCQ7;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Little elongation complex subunit 2;
DE   AltName: Full=Interactor of little elongator complex ELL subunit 2;
DE   AltName: Full=NMDA receptor-regulated protein 2;
GN   Name=ICE2; Synonyms=NARG2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the little elongation complex (LEC), a complex
CC       required to regulate small nuclear RNA (snRNA) gene transcription by
CC       RNA polymerase II and III. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the little elongation complex (LEC), at least
CC       composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts
CC       with ICE1 (via C-terminus domain). Interacts with ELL (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with COIL
CC       in subnuclear Cajal and histone locus bodies. Translocates in the LEC
CC       complex to Cajal and histone locus bodies at snRNA genes in a ICE1-
CC       dependent manner. Associates to transcriptionally active chromatin at
CC       snRNA genes (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ICE2 family. {ECO:0000305}.
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DR   EMBL; BC120051; AAI20052.1; -; mRNA.
DR   RefSeq; NP_001069733.1; NM_001076265.1.
DR   AlphaFoldDB; Q0VCQ7; -.
DR   STRING; 9913.ENSBTAP00000007009; -.
DR   PaxDb; Q0VCQ7; -.
DR   PRIDE; Q0VCQ7; -.
DR   GeneID; 541255; -.
DR   KEGG; bta:541255; -.
DR   CTD; 79664; -.
DR   eggNOG; ENOG502QUWA; Eukaryota.
DR   InParanoid; Q0VCQ7; -.
DR   OrthoDB; 518363at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR   GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR   GO; GO:0035363; C:histone locus body; ISS:UniProtKB.
DR   GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR   GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR   GO; GO:0042795; P:snRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0042796; P:snRNA transcription by RNA polymerase III; ISS:UniProtKB.
DR   InterPro; IPR019535; ICE2_C.
DR   Pfam; PF10505; NARG2_C; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..981
FT                   /note="Little elongation complex subunit 2"
FT                   /id="PRO_0000297963"
FT   REGION          406..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..981
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..974
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q659A1"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q659A1"
FT   MOD_RES         573
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UZ18"
FT   MOD_RES         575
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UZ18"
SQ   SEQUENCE   981 AA;  109914 MW;  7EAB1C95C1DC7980 CRC64;
     MTSMMAMGEP RLNWDVSPKN GLKTFFSREN YKDQSMAPSL KELCILSSRR IGENLNASAG
     SVENEPTVNS AAQAKEKVKT TVGMVLLPKP RVPYPRFSRF SQREQRNYVD LLVKYAKVPP
     NSKTVGINKN DYLQYLEMKK HVNEEVTEFL KFLQNSAKKC AQDYNMLSDD ACLVTEQILK
     ACIEQVKKYP EFYTLHEVTS LMGFFPFRIE MGFKLEKTLL ALGSVKYVKT VFPSMPAKLQ
     LSKDTIPAIE TPEQIAAAMH YDISEDPNAE KLVARYHPQI ALTSQSLFTL LNNHGPSYKE
     QWEIPVCIQV IPVAGSKPIK VIYINSPLPQ KKMTMRERNQ IFHEVPLKFM MSKNTSVPVS
     AVFMDKPEEY ISEMDISYEV NECRKIETLE NLDLEFDDDV TELETFGATT TKPSKSPSPA
     STSTVAPMTD TLTAPSIADT SEAPTSPDIS AHSRSLSQIL MEQLQKEKQL VTGMIDSGPE
     ESKNKDDQRF IPCGEKVSNS DKPLVQDSDL KTSDPLQLES SMEIETSSKN DMATEMESVD
     ERVNVLENTD TNSKEKTVTS EAANTEDVVL DSSDTDEDCL IIDMECQSNS HGKTAEVGSN
     LSSKPASLNS SSGQTSTGNQ TNSTCPEESC VLKKPIKRVY KKFDPVGEIL KMQDELLKPI
     SRKIPELPLM NSENSKQPPI SEQPSAPSDA CSWPKSIWPS AFQKPKGRLP YELQDYVEDT
     SEYVAPQEGN FVYKLFSLQD LLLLVRCSVQ RIETRPRSKK RKKIRRQFPV YVLPKVEYQA
     CYGVEALTES ELCRLWTESL LHSNSSFYVG HIDAFTSKLF LLEEITSEEL KEKLSALKIS
     SLFNILQHIL RKLSSLQEGS YLLSHAAEDS SLLIYKTSDG KVTRTAYNLH KTHCGLPGVP
     SSLSVPWVPL DPSLLLPNHI HHGRIPCTFP PKSLGPTAQQ KIGGTRMPTR SHRNSVSVET
     KSLPAQQVEN EGVASSKRKI T