GON4L_RAT
ID GON4L_RAT Reviewed; 2256 AA.
AC Q535K8; Q535K7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=GON-4-like protein;
DE AltName: Full=GON-4 homolog;
DE AltName: Full=Protein GON4;
GN Name=Gon4l; Synonyms=Gon4;
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 [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Lewis; TISSUE=Brain, and Heart;
RA Kuryshev V.Y., Vorobyov E., Zink D., Schmitz J., Rozhdestvensky T.S.,
RA Muenstermann E., Ernst U., Wellenreuther R., Moosmayer P., Bechtel S.,
RA Schupp I., Horst J., Korn B., Poustka A., Wiemann S.;
RT "An anthropoid specific segmental duplication in the human chromosome 1q22:
RT structure and evolution of the affected genes.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346, AND IDENTIFICATION BY
RP 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: Has transcriptional repressor activity, probably as part of a
CC complex with YY1, SIN3A AND HDAC1. Required for B cell lymphopoiesis.
CC {ECO:0000250|UniProtKB:Q9DB00}.
CC -!- SUBUNIT: Found in a complex with YY1, SIN3A and HDAC1.
CC {ECO:0000250|UniProtKB:Q9DB00}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=GON4L isoform A;
CC IsoId=Q535K8-1; Sequence=Displayed;
CC Name=2; Synonyms=GON4L isoform B;
CC IsoId=Q535K8-2; Sequence=VSP_016583, VSP_016584;
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DR EMBL; AY724781; AAW50122.1; -; mRNA.
DR EMBL; AY724782; AAW50123.1; -; mRNA.
DR RefSeq; NP_001019968.1; NM_001024797.1. [Q535K8-1]
DR AlphaFoldDB; Q535K8; -.
DR SMR; Q535K8; -.
DR STRING; 10116.ENSRNOP00000053632; -.
DR iPTMnet; Q535K8; -.
DR PhosphoSitePlus; Q535K8; -.
DR jPOST; Q535K8; -.
DR PaxDb; Q535K8; -.
DR PRIDE; Q535K8; -.
DR GeneID; 499653; -.
DR KEGG; rno:499653; -.
DR UCSC; RGD:1564691; rat. [Q535K8-1]
DR CTD; 54856; -.
DR RGD; 1564691; Gon4l.
DR eggNOG; ENOG502QT2W; Eukaryota.
DR InParanoid; Q535K8; -.
DR PhylomeDB; Q535K8; -.
DR PRO; PR:Q535K8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0030183; P:B cell differentiation; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.20.1160.11; -; 1.
DR InterPro; IPR033277; GON-4-like.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR003822; PAH.
DR InterPro; IPR036600; PAH_sf.
DR InterPro; IPR001005; SANT/Myb.
DR PANTHER; PTHR16088:SF11; PTHR16088:SF11; 2.
DR Pfam; PF02671; PAH; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47762; SSF47762; 2.
DR PROSITE; PS50090; MYB_LIKE; 1.
DR PROSITE; PS51477; PAH; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..2256
FT /note="GON-4-like protein"
FT /id="PRO_0000197111"
FT DOMAIN 1644..1716
FT /note="PAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 1726..1797
FT /note="PAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 2163..2216
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..1363
FT /note="Required for interaction with YY1, SIN3A AND HDAC1,
FT and transcriptional repression activity"
FT /evidence="ECO:0000250|UniProtKB:Q9DB00"
FT REGION 947..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1831..1886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1909..1966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2050..2078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2110..2148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2223..2256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..391
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..571
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1135
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1473..1498
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1556
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1833..1866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB00"
FT MOD_RES 1445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3T8J9"
FT MOD_RES 1921
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3T8J9"
FT MOD_RES 1994
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3T8J9"
FT VAR_SEQ 1820
FT /note="F -> V (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_016583"
FT VAR_SEQ 1821..2256
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_016584"
SQ SEQUENCE 2256 AA; 247903 MW; 6BAB871501111AD4 CRC64;
MLPCKKRSGV TESAQQQDDQ EGEDLHLEAA VKPDTDQLPD CTSESLSWGQ SHDSAGCPEV
HSMQDVGSQL SVEGTPLSSK MLTQRVNLAV SEAVDVPVSQ EIPVPSLESS HSLPVHMGKG
RLQSTASRKG KKIAFMPGQV TREDGGDHTV PEEPPSGEHA EEVKAEGGEL EMHSEGDLPS
LSSGSQSAKP RAQPRKSFQP DGSAFPQEKS LGPLVRQAEE DMEDGGLFIP TEEQDGEESD
KRKKTKKGTK RKRDGRGQEQ GTMTYDPKVD DMLDRTLEDG AKQHNLTAVN VRNILHEVIT
NEHVVAMMKA AISETEDMPL FEPKMTRSKL KEVVEKGVVI PTWNISPIKK ASETKQPPQF
VDIHLEDDDS SDEEYQPDEE EEDETAEESL LESDVESAAS SPRGVKRSRL RLSSEAAEAD
EESGVLSEVE KVATPALRHI SAEVVPMGPP PPPKPKQTRD STFMEKLNAV DEELAASPVC
MDSFQPMEDS LIAFRTRSKM PLKDVPLGQL EAELQAPDIT PDMYDPNTAD DEDWKLWLGG
LLNDDVENED EADDDDDPEY NFLEDLDEPD TEDFRTDRAV RITKKEVNGL MEELFETVQS
VVPSKFQDEM GFSNMEDDGP EEEERVTESR PSFNTPQALR FEEPLANLLN ERHRTVKELL
EQLKMKKSSV RQQPEVEKLK PQTEKVHQTL VLDPAQRSRL QQQMQQHVQL LTQIYLLTTS
NPNLSSEAST TRVFLKELGT FAENSTALHQ QFNPRFQTLF QPCNWVGAMQ LIEDFTHISI
DCSPHKTVKK TASEFPCLPK QVAWILATNK VFMYPELLPI CSLKANNPRD KTIFTKAEDN
LLALGLKHFE GTEFPKPLIS KYLVTCKTAH QLTVRIKNLN LNRAPNNVIK FYKKTKQLPV
LVRCCEEIQP HQWKPPIEKE EHRLPFWLKA SLQSIQEELR NLAGGATAGG SVTAATETST
DQHLQKTSPV VGGDTQYPLL LPKGVVLKLK PGSKRFSRKA WRQKRPLVQK PLLIQPSPSV
QPVFNPGKMA TWPTQSEVPP SNTVVQIPHL IQPAAVLQTL PGFPSVGVCG EDSFESPAAL
PAMPSGSEAR TSFPWSESQS APPSSSAPKL MLPSLGPSKF RKPYVRRKPT RRKGAKASPC
VKPAPIIHPT PVIFTVPATT VKVVSLGGGC NMIQPVTAAV APSPQTIPIT TLLVNPTSFP
CSLNQPLVAS SISPLLVSSN PLALPVTSLP EEKAHVSLDI AEGKNAPQNP EPKIKPQEPT
PQCATVFSKE EPRSWHPSAD TGNQEAVSES SACSWAAVKT EGQEGSSEKS VCGWTVVKTE
DGGHAVQPLP QDPQDSLNSP SKDLLNMVKL EAEDCMEEIS SDFPKQDIGE EVKEECCMEL
DRDSPQEKAS SVSEMSKQTA TPREETQAAK SPTVSQDAPD AIRDASKGLP QSTLSSMDQG
TVLNSPPGKP EDSANADGQS VGTPAGTDTG AEKDGAEEEE EEDFDDLTQD EEDELSSASE
ESVLSVPELQ ETMEKLTWLA SERRMSQEGE SEEENSQEEN SEPEEEEEEE AEGMETLQKE
DEATDEAGGG AAEKPPSTLA SPHTAPEVET SITPAGESIK AAGKGRSSHR ARSRRGSRAR
ASKDASKLLL LYDEDILDRD PLREQKDLAF AQAYLTRVRE ALQHIPGKYE DFLQIIYEFE
SNAQMHSAVD LFKSLQTLLH DWPQLLKDFA AFLLPEQALS CGLFEEQQAF EKSRKFLRQL
EICFAENPSH HQKIIKVLQG CADCLPQDIT ELKTQMWQLL RGHDHLQDEF SIFFDHLRPA
ANRMGDFEEI NWTEEKEYEF DGFEEVILPE VEEEEEPAKV STASKSKRRK EIGVQHQDKE
SEWPEAAKDG SCPCHEGGPE SKLKKSKRRN CHCSSKVCDS KSYKSKEPLE LVGSGPLQEA
STVPGTKEAG QGKDMSEEET MEGQENVEVS QNKTGRTTRK GEAPIPGSTV RTALLCSAEV
TPIELSLEGP TCCSPETPRL PPQTGAVVCS VRRNQAGPEV VSCLGTSSIP PKEGEDQKAV
ANSETIAPLP ETSETERLPG TVELPAPLPS PVSLSTRDTG RRHIYGKAGT QSWLLDNRAE
AKAAHMVAPI RGTSSGASAS EAAPTASREG LAEDSETQGK GPEAVLPKAS EATVCANNSK
VSSTGEKVVL WTREADRVIL TMCQEQGAQP HTFSVISQQL GNKTPVEVSH RFRELMQLFH
TACEASSEDE DDATSTSNAD QLSDHGDLLS EEELDE
