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Database: UniProt
Entry: F6RWN6_MACMU
LinkDB: F6RWN6_MACMU
Original site: F6RWN6_MACMU 
ID   F6RWN6_MACMU            Unreviewed;       870 AA.
AC   F6RWN6; I3RSH1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 2.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE            EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:AFK29256.1};
RN   [1] {ECO:0000313|EMBL:AFK29256.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Jiang G.Y., Yang J.H., Liu S.F.;
RT   "Bioinformatic analysis of E3 ligase WWP2 in 14 different vertebrates.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885,
CC         ECO:0000256|PIRNR:PIRNR001569};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.
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DR   EMBL; JN712747; AFK29256.1; -; mRNA.
DR   RefSeq; NP_001254530.1; NM_001267601.1.
DR   AlphaFoldDB; F6RWN6; -.
DR   GeneID; 705464; -.
DR   KEGG; mcc:705464; -.
DR   CTD; 11060; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   HOGENOM; CLU_002173_0_1_1; -.
DR   OrthoDB; 5480520at2759; -.
DR   TreeFam; TF323658; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd04021; C2_E3_ubiquitin_ligase; 1.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 4.
DR   Gene3D; 2.20.70.10; -; 3.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR11254:SF396; NEDD4-LIKE E3 UBIQUITIN-PROTEIN LIGASE WWP2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 4.
DR   PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 4.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF51045; WW domain; 4.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 4.
DR   PROSITE; PS50020; WW_DOMAIN_2; 4.
PE   2: Evidence at transcript level;
KW   Ligase {ECO:0000313|EMBL:AFK29256.1};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PIRNR:PIRNR001569}.
FT   REGION          150..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        838
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001569-1"
SQ   SEQUENCE   870 AA;  98754 MW;  902073D22CDDE436 CRC64;
     MASASSSRAG VALPFEKSQL TLKVVSAKPK VHNRQPRINS YVEVAVDGLA SETKKTAKRI
     GSSELLWNEI IILNVTAQSH LDLKVWSCHT LRNELLGTAS VNLSNVLKNN GGKMENTQLT
     LNLQTENKGS VVSGGELTIF LDGPTVDLGS VPNGSAVTDG SQPPSRDSSG TAVAPENRHQ
     LPSTNCFGGR SRTHRHSGAA ARTTPATGEQ SPGARSRHRQ PVKNSGHSGL ANGTVNDEPT
     TATDPEEPSV VGVTSPPAAP LSVTPNPNTT SLPAPATPAE GEEPSTSGTQ QLPAAAQAPD
     ALPAGWEQRE LPNGRVYYVD HNTKTTTWER PLPPGWEKRT DPRGRFYYVD HNTRTTTWQP
     PTAEYVRNYE QWQSQRNQLQ GAMQHFSQRF LYQSSSASTD HDPLGPLPPG WEKRQDNGRV
     YYVNHNTRTT QWEDPRTQGM IQEPALPPGW EMKYTSEGVR YFVDHNTRTT TFKDPRPGFE
     SGTKQGSPGA YDRSFRWKYH QFRFLCHSNA LPSHVKISVS RQTLFEDSFQ QIMNMKPYDL
     RRRLYIIMRG EEGLDYGGIA REWFFLLSHE VLNPMYCLFE YAGKNNYCLQ INPASSINPD
     HLTYFRFIGR FIAMALYHGK FIDTGFTLPF YKRMLNKRPT LKDLESVDPE FYNSIVWIKE
     NNLEECGLEL YFIQDMEILG KVTTHELKEG GESIRVTEEN KEEYIMLLTD WRFTRGVEEQ
     TKAFLDGFNE VAPLEWLRYF DEKELELMLC GMQEIDMSDW QKSTIYRHYT KNSKQIQWFW
     QVVKEMDNEK RIRLLQFVTG TCRLPIGGFA ELIGSNGPQK FCIDKVGKET WLPRSHTCFN
     RLDLPPYKSY EQLREKLLYA IEETEGFGQE
//
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