ID   AF1Q_RAT                Reviewed;          90 AA.
AC   Q5M971; Q52KR8;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Protein AF1q;
GN   Name=Mllt11; Synonyms=Af1q;
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=Brain;
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-60 AND SER-84, AND
RP   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: Cofactor for the transcription factor TCF7. Involved in
CC       regulation of lymphoid development by driving multipotent hematopoietic
CC       progenitor cells towards a T-cell fate. {ECO:0000250|UniProtKB:Q13015}.
CC   -!- SUBUNIT: Interacts with HSPA8 and LAMP2 isoform A; the interaction may
CC       target MLLT11 for degradation via chaperone-mediated autophagy.
CC       Interacts with TCF7. {ECO:0000250|UniProtKB:Q13015}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13015}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q13015}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q13015}.
CC       Note=Continuous nuclear export is followed by degradation.
CC       {ECO:0000250|UniProtKB:Q13015}.
CC   -!- PTM: Ubiquitinated, leading to degradation.
CC       {ECO:0000250|UniProtKB:Q13015}.
CC   -!- SIMILARITY: Belongs to the MLLT11 family. {ECO:0000305}.
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DR   EMBL; BC087583; AAH87583.1; -; mRNA.
DR   EMBL; BC094215; AAH94215.1; -; mRNA.
DR   RefSeq; NP_001013934.1; NM_001013912.1.
DR   AlphaFoldDB; Q5M971; -.
DR   STRING; 10116.ENSRNOP00000028664; -.
DR   iPTMnet; Q5M971; -.
DR   PhosphoSitePlus; Q5M971; -.
DR   jPOST; Q5M971; -.
DR   PaxDb; Q5M971; -.
DR   PRIDE; Q5M971; -.
DR   GeneID; 295264; -.
DR   KEGG; rno:295264; -.
DR   UCSC; RGD:1305525; rat.
DR   CTD; 10962; -.
DR   RGD; 1305525; Mllt11.
DR   eggNOG; ENOG502S7MB; Eukaryota.
DR   HOGENOM; CLU_2440320_0_0_1; -.
DR   InParanoid; Q5M971; -.
DR   OMA; FNYWKEP; -.
DR   OrthoDB; 1586302at2759; -.
DR   PhylomeDB; Q5M971; -.
DR   TreeFam; TF336906; -.
DR   ChiTaRS; Mllt11; rat.
DR   PRO; PR:Q5M971; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000021110; Expressed in frontal cortex and 20 other tissues.
DR   Genevisible; Q5M971; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR   GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISS:UniProtKB.
DR   GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   InterPro; IPR026778; MLLT11_fam.
DR   InterPro; IPR033461; WRNPLPNID.
DR   PANTHER; PTHR15404; PTHR15404; 1.
DR   Pfam; PF15017; WRNPLPNID; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..90
FT                   /note="Protein AF1q"
FT                   /id="PRO_0000064474"
FT   REGION          33..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           24..32
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q13015"
FT   COMPBIAS        36..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         60
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   90 AA;  10030 MW;  22E27D8D9B02589A CRC64;
     MRDPVSSQYS SFLFWRMPIP ELDLSELEGL GLSDSPTYKS KESNSIGKMG GQATGAERKS
     PEGDPLLEYS TFNFWRAPIA SIRSIDLDLL