ID A0A2K5V0F6_MACFA Unreviewed; 997 AA.
AC A0A2K5V0F6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 23.
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:ENSMFAP00000018210.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000018210.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000018210.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000018210.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A2K5V0F6; -.
DR Ensembl; ENSMFAT00000068755.2; ENSMFAP00000018210.2; ENSMFAG00000032021.2.
DR VEuPathDB; HostDB:ENSMFAG00000032021; -.
DR GeneTree; ENSGT00940000156873; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233100; Chromosome 18.
DR Bgee; ENSMFAG00000032021; Expressed in adult mammalian kidney and 13 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; 3.
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; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 4.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Signal {ECO:0000256|SAM:SignalP};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..997
FT /note="HECT-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030051236"
FT DOMAIN 10..130
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 197..230
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 389..422
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 501..534
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 552..576
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 662..996
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 182..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 964
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 997 AA; 114477 MW; C60B606B0F56C202 CRC64;
MAPLSAALLL WHSVCVPVCY GESRILRVKV VSGIDLAKKD IFGASDPYVK LSLYVADENR
ELALVQTKTI KKTLNPKWNE EFYFRVNPSN HRLLFEVFDE NRLTRDDFLG QVDVPLSHLP
TEDPTMERPY TFKDFLLRPR SHKSRVKGFL RLKMAYMPKN GGQDEENSDQ RDDMEHGWEV
VDSNDSASQH QEELPPPPLP PGWEEKVDNL GRTYYVNHNN RTTQWHRPSL MDVSSESDNN
IRQINQEAAH RRFRSRRHIS EDLEPEPSEG GDVPEPWETI SEEVNIAGDS LGLALPPPPA
SPGSRTSPQE LSEELSRRLQ ITPDSNGEQF SSLVQREPSS RLRSCSVTDA VAEQGHLPPP
SAPARRARSS TVTGGEEPTP SVAYVHTTPG LPSGWEERKD AKGRTYYVNH NNRTTTWTRP
IMQLAEDGAS GSATNSNNHL IEPQIRRPRS LSSPTVTLSA PLEGAKDSPV RRAVKDTLSN
PQSPQPSPYN SPKPQHKVTQ SFLPPGWEMR IAPNGRPFFI DHNTKTTTWE DPRLKFPVHM
RSKTSLNPND LGPLPPGWEE RIHLDGRTFY IDHSSQVLCG ENDTRESVPS YDSKITQWED
PRLQNPAITG PAVPYSREFK QKYDYFRKKL KKPADIPNRF EMKLHRNNIF EESYRRIMSV
KRPDVLKARL WIEFESEKGL DYGGVAREWF FLLSKEMFNP YYGLFEYSAT DNYTLQINPN
SGLCNEDHLS YFTFIGRVAG LAVFHGKLLD GFFIRPFYKM MLGKQITLND MESVDSEYYN
SLKWILENDP TELDLMFCID EENFGQTYQV DLKPNGSEIM VTNENKREYI DLVIQWRFVN
RVQKQMNAFL EGFTELLPID LIKIFDENEL ELLMCGLGDV DVNDWRQHSI YKNGYCPNHP
VIQWFWKAVL LMDAEKRIRL LQFVTGTSRV PMNGFAELYG SNGPQLFTIE QWGSPEKLPR
AHTCFNRLDL PPYETFEDLR EKLLMAVENA QGFEGVD
//
