RED_RAT
ID RED_RAT Reviewed; 557 AA.
AC Q66HG8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Protein Red;
DE AltName: Full=Cytokine IK;
DE AltName: Full=IK factor;
GN Name=Ik;
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=Kidney;
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 PROTEIN SEQUENCE OF 108-127; 165-173; 229-236; 282-290; 310-331 AND
RP 535-541, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the
CC spliceosome. Auxiliary spliceosomal protein that regulates selection of
CC alternative splice sites in a small set of target pre-mRNA species.
CC Required for normal mitotic cell cycle progression. Recruits MAD1L1 and
CC MAD2L1 to kinetochores, and is required to trigger the spindle assembly
CC checkpoint. Required for normal accumulation of SMU1.
CC {ECO:0000250|UniProtKB:Q13123}.
CC -!- SUBUNIT: Component of the spliceosome B complex. Interacts with SMU1.
CC Interacts with MAD1L1. May interact with DHX15.
CC {ECO:0000250|UniProtKB:Q13123}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13123}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q13123}. Chromosome
CC {ECO:0000250|UniProtKB:Q13123}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q13123}. Note=Predominantly present throughout
CC the nucleoplasm during prometaphase, metaphase and anaphase. Is also
CC detected in nuclear foci that are not identical with Cajal bodies.
CC Starts to accumulate at chromosomes during telophase, and is nearly
CC exclusively associated with chromosomes in newly divided cells.
CC Colocalizes with MAD1L1 at mitotic spindle poles during metaphase and
CC anaphase. {ECO:0000250|UniProtKB:Q13123}.
CC -!- SIMILARITY: Belongs to the RED family. {ECO:0000305}.
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DR EMBL; BC081870; AAH81870.1; -; mRNA.
DR RefSeq; NP_001005537.1; NM_001005537.1.
DR AlphaFoldDB; Q66HG8; -.
DR SMR; Q66HG8; -.
DR iPTMnet; Q66HG8; -.
DR PhosphoSitePlus; Q66HG8; -.
DR jPOST; Q66HG8; -.
DR PaxDb; Q66HG8; -.
DR PRIDE; Q66HG8; -.
DR GeneID; 291659; -.
DR KEGG; rno:291659; -.
DR UCSC; RGD:1359352; rat.
DR CTD; 3550; -.
DR RGD; 1359352; Ik.
DR eggNOG; KOG2498; Eukaryota.
DR InParanoid; Q66HG8; -.
DR OrthoDB; 500537at2759; -.
DR PRO; PR:Q66HG8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0034501; P:protein localization to kinetochore; ISS:UniProtKB.
DR InterPro; IPR039896; Red-like.
DR InterPro; IPR012492; RED_C.
DR InterPro; IPR012916; RED_N.
DR PANTHER; PTHR12765; PTHR12765; 1.
DR Pfam; PF07807; RED_C; 1.
DR Pfam; PF07808; RED_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Spliceosome;
KW Ubl conjugation.
FT CHAIN 1..557
FT /note="Protein Red"
FT /id="PRO_0000288497"
FT REPEAT 342..343
FT /note="1"
FT REPEAT 344..345
FT /note="2"
FT REPEAT 346..347
FT /note="3"
FT REPEAT 348..349
FT /note="4"
FT REPEAT 350..351
FT /note="5"
FT REPEAT 352..353
FT /note="6"
FT REPEAT 354..355
FT /note="7"
FT REPEAT 356..357
FT /note="8"
FT REPEAT 358..359
FT /note="9"
FT REPEAT 360..361
FT /note="10"
FT REPEAT 362..363
FT /note="11"
FT REPEAT 364..365
FT /note="12"
FT REPEAT 366..367
FT /note="13"
FT REPEAT 368..369
FT /note="14"
FT REPEAT 370..371
FT /note="15"
FT REPEAT 372..373
FT /note="16"
FT REPEAT 374..375
FT /note="17"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..375
FT /note="17 X 2 AA tandem repeats of R-[ED]"
FT COMPBIAS 17..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT MOD_RES 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1M8"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT MOD_RES 485
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 386
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 388
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 404
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 408
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 496
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 501
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 541
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 543
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 544
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
FT CROSSLNK 553
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13123"
SQ SEQUENCE 557 AA; 65588 MW; 15FD9334FC887113 CRC64;
MPERDSEPFS NPLAPDGHDV DDPHSFHQSK LTNEDFRKLL MTPRAAPTSA PPSKSRHHEM
PREYNEDEDP AARRRKKKSY YAKLRQQEIE RERELAEKYR DRAKERRDGV NKDYEETELI
STTANYRAVG PTAEADKSAA EKRRQLIQES KFLGGDMEHT HLVKGLDFAL LQKVRAEIAS
KEKEEEELME KPQKETKKDE DPENKIEFKT RLGRNVYRML FKSKSYERNE LFLPGRMAYV
VDLDDEYADT DIPTTLIRSK ADCPTMEAQT TLTTNDIVIS KLTQILSYLR QGTRNKKLKK
KDKGKLEEKK PPEADMNIFE DIGDYVPSTT KTPRDKERER YRERERDRER DRDRERDRER
DRERERERDR EREREEEKKR HSYFEKPKVD DEPMDVDKGP GSAKELIKSI NEKFAGSAGW
EGTESLKKPE DKKQLGDFFG MSNSYAECYP ATMDDMAVDS DEEVDYSKMD QGNKKGPLGR
WDFDTQEEYS EYMNNKEALP KAAFQYGIKM SEGRKTRRFK ETNDKAELDR QWKKISAIIE
KRKKMEADGV EVKRPKY
