ID H9GFW3_ANOCA Unreviewed; 954 AA.
AC H9GFW3;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=NEDD4L {ECO:0000313|Ensembl:ENSACAP00000009808.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000009808.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000009808.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000009808.3};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000009808.3}
RP IDENTIFICATION.
RG Ensembl;
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR AlphaFoldDB; H9GFW3; -.
DR STRING; 28377.ENSACAP00000009808; -.
DR Ensembl; ENSACAT00000010008.4; ENSACAP00000009808.3; ENSACAG00000009877.4.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000156873; -.
DR HOGENOM; CLU_002173_0_3_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000009877; Expressed in heart and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IBA:GO_Central.
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:UP000001646};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 4..126
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 192..225
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 383..416
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 496..529
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 547..580
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 639..953
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 153..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 921
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 954 AA; 110041 MW; 61894B88051FCBE8 CRC64;
MATGMVEPVY GLSEEEEESR VLRVKVVAGI DLAKKDIFGA SDPYVKLSLY ASDESRELAL
VQTKTIKKTL NPKWNEEFYF RVNPSNHRLL FEVFDENRLT RDDFLGQVDV PLNHLPTEDP
TMERPYTFKD FLLRPRSHKS RVKGFLRLKM AYMPKNGGQE DDNDQREDSE HGWEVVDSND
SPAQRQEELP PPPLPPGWEE KVDNLGRTYY VNHNNRTTQW HRPSLMDVAS ESDNNIRQIN
QEAAHRRFRS RRHISEDLDP EPLESGDVPE PWETISEENA SSDSLSLSLP PPPASPVSRT
TPQELSDELN RRLQITPDSN GEQLSSMIQR DPSARLRSCS VTDAVAEQSH LTLQTGPPRR
VRSSTVTGGE ESTPSVAYVH TTPGLPSGWE ERKDAKGRTY YVNHNNRTTT WTRPIMQLAE
DGATGSTSNS NNHLTEPQIR RPRSLSTPTV TLSAPLEGLL KESPVRRAVK DTLSNPQSPQ
PSPYNSPKPQ HKLTQSFLPP GWEMRIAPNG RPFFIDHNTK TTTWEDPRLK FPVHLRPKPA
LNPNDLGPLP PGWEERIHLD GRTFYIDHNN KITQWEDPRL QNPAITGPAV PYSREFKQKY
DYFRKKLKKP ADIPNRFEMK LHRNNIFEES YRRIMSVKRP DVLKARLWIE FESEKGLDYG
GVAREWFFLL SKEMFNPYYG LFEYSATDNY TLQINPNSGL CNEDHLSYFT FIGRVAGLAV
YHGKLLDGFF IRPFYKMMLG KPITLKDMES VDSEYYNSLK WILENDPTEL DLMFCIDEEN
FGQTYQVDLK PNGSEITVTN ENKREYIDLV IQWRFVNRVQ KQMNAFLELL MCGLGDVDVN
DWRQHTIYKN GYCPNHPVIQ WYWKAVLLMD AEKRIRLLQF VTGTSRVPMN GFAELYGSNG
PQLFTIEQWG SPEKLPRAHT CFNRLDLPPY ESFEELREKL LMAVENAQGF EGVD
//
