ID   QSER1_XENLA             Reviewed;        1673 AA.
AC   Q66IN2;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Glutamine and serine-rich protein 1;
GN   Name=qser1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an essential role in the protection and maintenance of
CC       transcriptional and developmental programs. Protects many bivalent
CC       promoters and poised enhancers from hypermethylation, showing a marked
CC       preference for these regulatory elements over other types of promoters
CC       or enhancers. Mechanistically, cooperates with tet1 and binds to DNA in
CC       a common complex to inhibit the binding of dnmt3a/3b and therefore de
CC       novo methylation. {ECO:0000250|UniProtKB:Q2KHR3}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q2KHR3}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH81280.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC081280; AAH81280.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q66IN2; -.
DR   IntAct; Q66IN2; 1.
DR   PRIDE; Q66IN2; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   InterPro; IPR025451; DUF4211.
DR   Pfam; PF13926; DUF4211; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; Reference proteome.
FT   CHAIN           1..1673
FT                   /note="Glutamine and serine-rich protein 1"
FT                   /id="PRO_0000288934"
FT   REGION          265..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..892
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          923..961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1050..1081
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1149..1182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1216..1272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1390..1476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1221..1235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1240..1272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1393..1412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1431..1451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1673 AA;  183336 MW;  7987903933BE4EA3 CRC64;
     MNFLSAIESR TAQAASSGTT LLPQFRAPSW QTGMHSSTAT ELFVTGALQT SGTFPTSALT
     AYQHPNTFSS RNFATTPSLA LQDGTFSAAT NGLLSPHDPL LQIKTSQTPT ALTFERIGSA
     VLSTSIPQSS TYRSAQESAP HLLQPQFSLL PSALGGTQQP AQPYSTSVFT GSTASIERAL
     QRECSVIKHH QRPSSTQSVQ AQLSGTQHSL PNYLTSVSGV SLHDASRQSS LLCAPLGALT
     HVSNGGPVQK TSQVSVELSQ SYPSVIPSPG YPPSSTKSKN CPTKAPPRSS KTPKSQSVVS
     PELTQSYTKS SQNQSSVNSS QAQAFSTAQL PSLLSVSQPP IYVSTQSPNL PSASQSQVFS
     TIKTEKLPPL YKPLTVFSSQ SQTITSGSQT LSYSSDQSLS LSSVSSETYS DQTRDLSSAN
     QSQSYSSNNS QGLTSVSQSQ VSYSSQSQVM SPVSPSDSYT SGQNQTLASP SLPFSTSSRG
     QNLSSSSPTQ NFISMHPTPN TQDSTSPQSQ KFLPSVQPSS FASSPHSQTM QNSRTTADSK
     SYVKRKSDTN LYASAKQEEK FQMQDLQALQ QTALETATPG LSEGELNTQE TAYSVSKADD
     RYSHSVIKSN SRMEEQVLGL QGTKKDERLI SPVGHMPQHV GHLNNSASHD GKKNTDLIQS
     TQVSAKDLSQ HTMLHKVLDT KMQEQPSTSP QLQAAMRHSQ HLQLPGAQVL LDSGCDLQMF
     QQSMLQSNMG QTKPSAQMQR IQSPPQVAHP FLQMDGQIIQ SNGAQSQQSL HAQGSDVIKM
     DTSNGKHLQQ HLHTKDHFSH RGRLDSKNQF DSLNPMCFSE SMLLTDERNF LSHVDDILAA
     TAAQEFAKSS NEENLSVKNQ DAKSRFQSLN VRHMSPNFTP PKPQNMNNLS INGSQSAVNL
     STVSTTQPKN VSLDQTHIQP MEQDLPSGMV SPVPGANQDD HEKNSENIKN PPNVNQEPKE
     GGNIQEEVGD AEFLSNNKTL SEENTTTEGD FIMGGDENAA LGQVQSHLSK IDPQAGGSST
     IEMEEDCPDI SQDGQQKGKD KMAIKQFTED ENANLKQIKR NMPLKRSVSK GPDVPGAQYS
     SHVSEGYYDS YQHQERMRQK IKEVEEKQPE VKTGFIASFL DFLKTGPKQQ FSAPAVRVPS
     RVRRPCTPVI RPPCPGPLSP QSVAGAPVSD SGSASPPKKA EEDLKKNLET LPSFSSDEDD
     ATVGNNDLQK SISTALSALD ENSEKRLKTE GDKAALSAKQ DPSTPRNGQD KTKAPESLKP
     SQPEATQPEQ LAKSQETIAI EGFTDEENTE SGGEGIYRER DEFVVKIEDI ELLKEALCTG
     KEPPAIWKVQ KALLQKFIPE IKDGQRSFAA TNSYLGYFGD AKTKYKRVYV KFVENANKKE
     YVRVCSRKPK SKVLQPARTT HTKASGGSKV SETPPPKTAP PKVVSAKPKA KPQKTKAEPP
     PKKRKQWKEE FSSSQSDSSP DMQSDEEEFA PPPPPIVTRF LNTRAMKETF KGYVELLVGL
     TLDGDMMQNL EKENDDVLLP HMRKIEGMLN ENRRRLLTKL QLEQPLKNAL ENYPDFAIIS
     RETKSKSAAC KIKVNGKWYN KKTLRPAKNP SKQSQEFPVE PEKSQLCSLY HALHHYKYHI
     YLKCKEEVSS VQKANRDLKQ EELVNHCLKN IKWVEDLFEK FGELLSRVQQ TCS