ID WWC2_MOUSE Reviewed; 1187 AA.
AC Q6NXJ0; Q3UGG4; Q3UH10; Q7TMY1; Q8CE61; Q9JJ63;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 143.
DE RecName: Full=Protein WWC2;
DE AltName: Full=WW domain-containing protein 2;
GN Name=Wwc2; Synonyms=D8Ertd594e; ORFNames=MNCb-4173;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-999, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286 AND SER-1017, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Negative regulator of the Hippo signaling pathway, also known
CC as the Salvador-Warts-Hippo (SWH) pathway. Enhances phosphorylation of
CC LATS1 and YAP1 and negatively regulates cell proliferation and organ
CC growth due to a suppression of the transcriptional activity of YAP1,
CC the major effector of the Hippo pathway.
CC {ECO:0000250|UniProtKB:Q6AWC2}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with WWC1 and WWC3.
CC Interacts with DLC1 and PRKCZ. Interacts (via WW domains) with LATS1
CC and LATS2. {ECO:0000250|UniProtKB:Q6AWC2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q6AWC2}.
CC -!- SIMILARITY: Belongs to the WWC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97983.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE28244.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB045323; BAA97983.1; ALT_FRAME; mRNA.
DR EMBL; AK028956; BAC26212.1; -; mRNA.
DR EMBL; AK147648; BAE28047.1; -; mRNA.
DR EMBL; AK147944; BAE28244.1; ALT_INIT; mRNA.
DR EMBL; BC054434; AAH54434.1; -; mRNA.
DR EMBL; BC067050; AAH67050.1; -; mRNA.
DR CCDS; CCDS22301.1; -.
DR RefSeq; NP_598552.2; NM_133791.4.
DR AlphaFoldDB; Q6NXJ0; -.
DR SMR; Q6NXJ0; -.
DR BioGRID; 206537; 2.
DR IntAct; Q6NXJ0; 1.
DR STRING; 10090.ENSMUSP00000056121; -.
DR GlyGen; Q6NXJ0; 8 sites, 1 O-linked glycan (8 sites).
DR iPTMnet; Q6NXJ0; -.
DR PhosphoSitePlus; Q6NXJ0; -.
DR SwissPalm; Q6NXJ0; -.
DR MaxQB; Q6NXJ0; -.
DR PaxDb; 10090-ENSMUSP00000056121; -.
DR PeptideAtlas; Q6NXJ0; -.
DR ProteomicsDB; 275221; -.
DR Pumba; Q6NXJ0; -.
DR Antibodypedia; 51479; 65 antibodies from 18 providers.
DR Ensembl; ENSMUST00000057561.9; ENSMUSP00000056121.8; ENSMUSG00000031563.9.
DR GeneID; 52357; -.
DR KEGG; mmu:52357; -.
DR UCSC; uc009lrm.2; mouse.
DR AGR; MGI:1261872; -.
DR CTD; 80014; -.
DR MGI; MGI:1261872; Wwc2.
DR VEuPathDB; HostDB:ENSMUSG00000031563; -.
DR eggNOG; KOG3209; Eukaryota.
DR GeneTree; ENSGT00410000025556; -.
DR HOGENOM; CLU_005420_0_0_1; -.
DR InParanoid; Q6NXJ0; -.
DR OMA; DTDYQYK; -.
DR OrthoDB; 1334597at2759; -.
DR PhylomeDB; Q6NXJ0; -.
DR TreeFam; TF324040; -.
DR BioGRID-ORCS; 52357; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Wwc2; mouse.
DR PRO; PR:Q6NXJ0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6NXJ0; Protein.
DR Bgee; ENSMUSG00000031563; Expressed in primary oocyte and 256 other cell types or tissues.
DR Genevisible; Q6NXJ0; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0035331; P:negative regulation of hippo signaling; ISO:MGI.
DR GO; GO:0046621; P:negative regulation of organ growth; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:0035330; P:regulation of hippo signaling; IBA:GO_Central.
DR CDD; cd08680; C2_Kibra; 1.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037771; C2_WWC.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR14791; BOMB/KIRA PROTEINS; 1.
DR PANTHER; PTHR14791:SF26; PROTEIN WWC2; 1.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1187
FT /note="Protein WWC2"
FT /id="PRO_0000309491"
FT DOMAIN 10..43
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 57..90
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 697..820
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 438..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1045
FT /note="Interaction with PRKCZ"
FT /evidence="ECO:0000250|UniProtKB:Q6AWC2"
FT COILED 121..194
FT /evidence="ECO:0000255"
FT COILED 224..256
FT /evidence="ECO:0000255"
FT COILED 302..423
FT /evidence="ECO:0000255"
FT COILED 859..885
FT /evidence="ECO:0000255"
FT COILED 1063..1143
FT /evidence="ECO:0000255"
FT COMPBIAS 882..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 999
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 352
FT /note="E -> G (in Ref. 2; BAE28244)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="I -> V (in Ref. 2; BAE28047)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="S -> F (in Ref. 1; BAA97983)"
FT /evidence="ECO:0000305"
FT CONFLICT 576..577
FT /note="SP -> FS (in Ref. 1; BAA97983)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="M -> V (in Ref. 1; BAA97983)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="A -> T (in Ref. 2; BAE28047)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="V -> A (in Ref. 1; BAA97983)"
FT /evidence="ECO:0000305"
FT CONFLICT 864
FT /note="T -> I (in Ref. 1; BAA97983)"
FT /evidence="ECO:0000305"
FT CONFLICT 1174
FT /note="R -> I (in Ref. 1; BAA97983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1187 AA; 132620 MW; 40FB67C9D1D3B296 CRC64;
MPRRAGSGQL PLPRGWEEAR DYDGKVFYID HNTRRTSWID PRDRLTKPLS FADCVGDELP
WGWEAGFDPQ IGAYYIDHIN KTTQIEDPRK QWRGEQEKML KDYLSVAQDA LRTQKELYHV
KEQRLALALD EYVRLNDAYK EKSSSHTSLF SGSSSSTKYD PDILKAEIST TQLRVKKLKR
ELSHMKQELL YKQQGFETLQ QIDEKMSGGQ SGYELNEAKA ILTELKSIRK AISSGEKEKQ
DLMQSLAKLQ ERFHLDQNMG SSEPDLRSSP VNSHLSLSRQ TLDAGSQTSI SGDIGVRSRS
NLAEKVRLSL QYEEAKRSMA NLKIELSKLD GEAWPGALDI EKEKLMLINE KEELLKELQF
ITPQKRSQEE LERLEAERQH LEEELMAARG SPSRALTERL KLEEKRKELL QKLEETTKLT
TSLYSQLQSL SSSTLSMSSG SSLGSLASSR GSLNTSSRGS LNSLSSSELY YSSQGDQMDT
DYQYKLDFLL QEKGGYIPSG PITTIHENEV VKSPSQPGQS GLCGVGVTAS SHTTPLTEAS
KSVASLSSRS SLSSLSPPGS PLVLDSVFPG SSHDTSPHQF PTDFEDCELS RRFADVGLGE
NQALLDSDSG GASQPLLEDK GLSDCPGELL CEGATDVEKS LPKRRGLHLR GDKTTRVSAA
ASDESVAGDS GVYEASMKQP GEMEDVPYSE EDVTIVETAQ VQIGLRYDTK SSSFMVIIAQ
LRNLHAFSIP HSSKVYFRVA LLPSSADVSC LFRTKVHPPT ESVLYNDVFR VAVSQAALQQ
KTLRVDLCSA SKHRREECLA GTQISLADLP FSNEIFMLWY NLLPSKQMPC KKNEDGNEEP
GARSQQPMLD PIDLDAVSAL LARTSAELLA VEQELAQEEE EEELRPERRG PGRDCLTMLR
EASDEPAALR ESGVPLAEGS RCTEDPKPCP RGPETSQCRK EPAEDPGQLP SGLPTLVDKE
TNTDEVVDSN MAVRPKDRSS LSSRQHPFVR NSVIVRSQTF SPGERSQYIC RLNRSDSDSS
TLAKKSLFVR NSTERRSLRV KRAVCQPTLR RTAQECPVRT SLDLELDLQA SLTRQSRLND
ELQALRGLRQ KLEELKAQGE TDLPPGVLED ERFQKLLKQA EKQAEQTKEE QKQDLNAERL
MRQVSKDVCR LREQSQKEPR QVQSFREKIA YFTRAKISIP SLPADDV
//
