ID A0A3Q7SE51_VULVU Unreviewed; 923 AA.
AC A0A3Q7SE51;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN Name=NEDD4L {ECO:0000313|RefSeq:XP_025853456.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025853456.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025853456.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025853456.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025853456.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_025853456.1; XM_025997671.1.
DR AlphaFoldDB; A0A3Q7SE51; -.
DR KEGG; vvp:112919291; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000286640; Unplaced.
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; cd04033; C2_NEDD4_NEDD4L; 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:SF310; E3 UBIQUITIN-PROTEIN LIGASE NEDD4-LIKE; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 3.
DR PRINTS; PR00360; C2DOMAIN.
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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..93
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 160..193
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 332..365
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 444..477
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 495..528
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 588..922
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 146..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 890
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 923 AA; 106786 MW; 9E9E16AD2EF269D7 CRC64;
MSLEDNYSDP YVKLSLYVAD ENRELALVQT KTIKKTLNPK WNEEFYFRVN PSNHRLLFEV
FDENRLTRDD FLGQVDIPLS HLPTEDPTME RPYTFKDFLL RPRSHKSRVK GFLRLKMAYM
PKNGGQDEEN SEQRDDMEHG WEVVDSNDSA SQHQEELPPP PLPPGWEEKV DNLGRTYYVN
HNNRTTQWHR PSLMDVSSES DSNIRQINQE AAHRRFRSRR HISEDLEPEP GEGGDGPEPW
ETISEEVNIT GDPLSLALPP PPSSPVSRTS PQELSEELSR RLQITPDSNG EQFGSLMQRE
PSSRLRSCSV TDGVAEQAHL PPPSVAYAHT TPGLPSGWEE RKDAKGRTYY VNHNNRTTTW
TRPIMQLAED GASGSATNSN NHLIEPQIRR PRSLSSPTVT LSAPLEGAKD SPIRRAVKDT
LSNPQSPQPS PYNSPKPQHK VTQSFLPPGW EMRIAPNGRP FFIDHNTKTT TWEDPRLKFP
VHMRSKASLN PNDLGPLPPG WEERIHLDGR TFYIDHNSKI TQWEDPRLQN PAITGPKAVP
YSREFKQKYD YFRKKLKKPA DIPNRFEMKL HRNNIFEESY RRIMSVKRPD VLKARLWIEF
ESEKGLDYGG VAREWFFLLS KEMFNPYYGL FEYSATDNYT LQINPNSGLC NEDHLSYFTF
IGRVAGLAVF HGKLLDGFFI RPFYKMMLGK QITLNDMESV DSEYYNSLKW ILENDPTELD
LMFCIDEENF GQTYQVDLKP NGSEIMVTNE NKREYIDLVI QWRFVNRVQK QMNAFLEGFT
ELLPIDLIKI FDENELELLM CGLGDVDVND WRQHSIYKNG YCPNHPVIQW FWKAVLLMDA
EKRIRLLQFV TGTSRVPMNG FAELYGSNGP QLFTIEQWGS PDKLPRAHTC FNRLDLPPYE
TFEDLREKLL MAVENAQGFE GVD
//
