WAC_DANRE
ID WAC_DANRE Reviewed; 558 AA.
AC Q7ZUK7; Q6PUS1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=WW domain-containing adapter protein with coiled-coil;
GN Name=waca; Synonyms=wac;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) 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; AY576994; AAS92632.1; -; mRNA.
DR EMBL; BC048888; AAH48888.1; -; mRNA.
DR RefSeq; NP_955954.1; NM_199660.1.
DR AlphaFoldDB; Q7ZUK7; -.
DR SMR; Q7ZUK7; -.
DR STRING; 7955.ENSDARP00000073355; -.
DR PaxDb; Q7ZUK7; -.
DR GeneID; 323904; -.
DR KEGG; dre:323904; -.
DR CTD; 323904; -.
DR ZFIN; ZDB-GENE-030131-2624; waca.
DR eggNOG; KOG0152; Eukaryota.
DR InParanoid; Q7ZUK7; -.
DR OrthoDB; 1111788at2759; -.
DR PhylomeDB; Q7ZUK7; -.
DR Reactome; R-DRE-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR PRO; PR:Q7ZUK7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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; 2.
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..558
FT /note="WW domain-containing adapter protein with coiled-
FT coil"
FT /id="PRO_0000406981"
FT DOMAIN 120..153
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 529..555
FT /evidence="ECO:0000255"
FT COMPBIAS 31..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 131
FT /note="S -> N (in Ref. 1; AAS92632)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="Y -> F (in Ref. 1; AAS92632)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="E -> K (in Ref. 1; AAS92632)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="D -> N (in Ref. 1; AAS92632)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="L -> P (in Ref. 1; AAS92632)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="S -> T (in Ref. 1; AAS92632)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="Missing (in Ref. 1; AAS92632)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 60592 MW; 84F83593D163C7E9 CRC64;
MVMYARKQPR LGDGCTDRRD SQPYQTLKYS SKSHPDHRHE KMRDSNDATP PCKMLRRSDS
PDNKHMDNTG HGRAKAIHPH RGREREGGTS ISPQENSHNH SSLHSSNSHS NPNKSSDTPF
EPADDWSEHI SSSGKKYYYN CRTEVSQWEK PKEWLEREQR QKEATKTAAV VNSFPKDRDY
RREAMQATPA SYSSTKSSIA TEKPSSLTPS SSSAAVSGLD VPNSASSASG STVPVSPVMQ
SPAPPTLLQD PSLLRQLLLA LQTALQLNNA SVDMAKINEV LTAAVTQASL QSILHKILTA
GPSAFNITTL LSQATQLSNQ VAQQSSQSPM SLTSDASSPR SYVSPRISTP QTNTASLKPP
LSTTPVSSQT KINAMTVKSS SLPPPSSQQP LSTEKHHDNG NSPRTLQRQS SQRSPSPGPN
HMGSNSSSSS NNGGGGGGQG PGVVSGAMPP GSVPPGTAPG RATCSFTPTL AAHFNENLIK
HVQGWPAEHV EKQASRLREE AHTMGSIYMS ENCTELKNLR SLVRVCEIQA TLREQRILFL
RQQIKELEKL KNQNSFMV
