ID G1T7I0_RABIT Unreviewed; 966 AA.
AC G1T7I0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 84.
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:ENSOCUP00000012456.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000012456.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000012456.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000012456.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000012456.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000012456.3};
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 EMBL; AAGW02050536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02050537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02050538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02050539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1T7I0; -.
DR PaxDb; 9986-ENSOCUP00000012456; -.
DR Ensembl; ENSOCUT00000014484.3; ENSOCUP00000012456.3; ENSOCUG00000014471.3.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000156873; -.
DR HOGENOM; CLU_002173_0_3_1; -.
DR TreeFam; TF323658; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001811; Chromosome 9.
DR Bgee; ENSOCUG00000014471; Expressed in upper lobe of left lung and 16 other cell types or tissues.
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:UP000001811};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 13..136
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 203..236
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 375..408
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 488..521
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 539..572
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 631..965
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 189..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 933
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 966 AA; 111364 MW; E694BFB26CA32208 CRC64;
MDTTTGGREC PTEDQCCNLF LTFFQQGESR ILRVKVVSGI DLAKKDIFGA SDPYVKLSLY
VADENRELAL VQTKTIKKTL NPKWNEEFYF RVNPSNHRLL FEVFDENRLT RDDFLGQVDV
PLSHLPTEDP TMERPYTFKD FLLRPRSHKS RVKGFLRLKM AYMPKNGAQD EENSEPRDDM
EHGWEVVDSN DSASQHQEEL PPPPLPPGWE EKVDNLGRTY YVNHNNRTTQ WHRPSLMDVS
SESDSNIRQI NQEAAHRRFR SRRHISEDLE PEPSEGGEAP EPWETISEEV NLAGDSLGLA
VPPPPASPVS RTSPQELTEE LSRRLQVTPD ANGEQFSSLI QREPSSRLRS CSVTDAVAEQ
AHLPPPSVAY VHTTPGLPSG WEERKDAKGR TYYVNHNNRT TTWTRPIMQL AEDGAASGSA
TNSSNHLIEP QIRRPRSLSS PTVTLSAPLE GAKDSPVRRA VKDTLSNPQS PQPSPYNSPK
PQHRVTQSFL PPGWEMRIAP NGRPFFIDHN TKTTTWEDPR LKFPVHMRSK ASLNPNDLGP
LPPGWEERIH LDGRTFYIDH NSKITQWEDP RLQNPAITGP AVPYSREFKQ KYDYFRKKLK
KPADIPNRFE MKLHRNNIFE ESYRRIMSVK RPDVLKARLW IEFESEKGLD YGGVAREWFF
LLSKEMFNPY YGLFEYSATD NYTLQINPNS GLCNEDHLSY FTFIGRVAGL AVFHGKLLDG
FFIRPFYKMM LGKQITLNDM ESVDSEYYNS LKWILENDPT ELDLMFCIDE ENFGQTYQVD
LKPNGSEIMV TNENKREYID LVIQWRFVNR VQKQMNAFLE GFTELLPIDL IKIFDENELE
LLMCGLGDVD VNDWRQHSIY KNGYCPNHPV IQWFWKAVLL MDAEKRIRLL QFVTGTSRVP
MNGFAELYGS NGPQLFTIEQ WGSPEKLPRA HTCFNRLDLP PYETFEDLRE KLLMAVENAQ
GFEGVD
//
