ID   WAC_XENTR               Reviewed;         628 AA.
AC   Q5U4Q0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=WW domain-containing adapter protein with coiled-coil;
GN   Name=wac;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a linker between gene transcription and histone H2B
CC       monoubiquitination at 'Lys-120' (H2BK120ub1). Positive regulator of
CC       amino acid starvation-induced autophagy. Positively regulates MTOR
CC       activity. May negatively regulate the ubiquitin proteasome pathway.
CC       {ECO:0000250|UniProtKB:Q9BTA9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BTA9}.
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DR   EMBL; BC084997; AAH84997.1; -; mRNA.
DR   RefSeq; NP_001011171.1; NM_001011171.1.
DR   AlphaFoldDB; Q5U4Q0; -.
DR   SMR; Q5U4Q0; -.
DR   STRING; 8364.ENSXETP00000059493; -.
DR   PaxDb; Q5U4Q0; -.
DR   DNASU; 496589; -.
DR   Ensembl; ENSXETT00000060642; ENSXETP00000059493; ENSXETG00000004545.
DR   GeneID; 496589; -.
DR   KEGG; xtr:496589; -.
DR   CTD; 51322; -.
DR   Xenbase; XB-GENE-6258902; wac.
DR   eggNOG; KOG0152; Eukaryota.
DR   InParanoid; Q5U4Q0; -.
DR   OrthoDB; 1111788at2759; -.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000004545; Expressed in testis and 17 other tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; ISS:UniProtKB.
DR   GO; GO:0010390; P:histone monoubiquitination; ISS:UniProtKB.
DR   GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR   CDD; cd00201; WW; 1.
DR   InterPro; IPR038867; WAC.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR15911; PTHR15911; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF51045; SSF51045; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Coiled coil; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..628
FT                   /note="WW domain-containing adapter protein with coiled-
FT                   coil"
FT                   /id="PRO_0000406982"
FT   DOMAIN          123..156
FT                   /note="WW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   REGION          1..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          599..625
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        34..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   628 AA;  68404 MW;  4CD0455341394880 CRC64;
     MVMYARKQAR LSDGCHDRRD SQPYQTLKYS SKSHPSSSDH RHDKMRDSTD PSPPNKMRRS
     NSPENKYIDS AGHGKAKSMH LHRVRERDGG TSFSPQENSH NHSAIHSSNS HSSTPSKTSD
     SAYDPADDWS EHISSSGKKY YYNCRTEVSQ WEKPKEWLER EQRQKETSKV AVNSFPKDRD
     YRREAMQAAA AVEEKHSSDT STMLPQNILS QTSRHNDRDY RLPRTDSHSS AAPVQQPVKA
     AVHPAAAPST VPSSPFTVQP DHPPPKKSYD ANGAALSKLP TPTSSIPVPK SERKETASSD
     KSSCTTPSTS SAPGLNLSAA PPSSSSSTVP VSPVPQSPIP PILQDPNLLR QLLPALQATL
     QLNNSNVDIS KINEAAVTQA SLQSILHKIL TAGPSAFNIT SLISQVAQLS AQAAQSNQSP
     MSLTSDASSP RSYVSPRIST PQTNTVPHKP LLSTPPVTSQ PKVGTPGSKQ GSSAQTASQQ
     SSAADKSQGH EPTSPRNLQR SSSQRSPSPG PNHNSSTCAS STSAPQNSSA RSSCSLTPTL
     AAYFNENLVK HVQGWPADHA EKQASRLREE AHNMGSIHMS EVCTELKNLR SLVRVCEIQA
     TLREQRILFL RQQIKELEKL KNQNSFMV