ID W5MXQ1_LEPOC Unreviewed; 1022 AA.
AC W5MXQ1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=AREL1 {ECO:0000313|Ensembl:ENSLOCP00000013160.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000013160.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000013160.1}
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};
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DR EMBL; AHAT01003752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006632272.1; XM_006632209.2.
DR RefSeq; XP_015206041.1; XM_015350555.1.
DR RefSeq; XP_015206042.1; XM_015350556.1.
DR AlphaFoldDB; W5MXQ1; -.
DR STRING; 7918.ENSLOCP00000013160; -.
DR Ensembl; ENSLOCT00000013188.1; ENSLOCP00000013160.1; ENSLOCG00000010734.1.
DR GeneID; 102692889; -.
DR KEGG; loc:102692889; -.
DR CTD; 9870; -.
DR eggNOG; KOG0939; Eukaryota.
DR GeneTree; ENSGT00940000156723; -.
DR HOGENOM; CLU_014403_0_0_1; -.
DR InParanoid; W5MXQ1; -.
DR OMA; NLCIFGP; -.
DR OrthoDB; 5480520at2759; -.
DR Proteomes; UP000018468; Linkage group LG7.
DR Bgee; ENSLOCG00000010734; Expressed in mesonephros and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd00078; HECTc; 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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR11254:SF340; APOPTOSIS-RESISTANT E3 UBIQUITIN PROTEIN LIGASE 1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT TRANSMEM 177..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 250..356
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT DOMAIN 682..1022
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 521..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 989
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1022 AA; 117724 MW; 1816F9A566103B36 CRC64;
MDRRFLLTFA FCSILWVLFW EIRWKKAKEN QIEEWLHGNS LSEYKDIFED VQSLEELTLS
LLSRLEEVLQ ETQYWQEIEE SRNQLLRDFA FQEWLCSQGL EHYYHTLKSL GCSSLDDLAE
FDSQLQLSLA AWGYYYEDYI KLSTGVKVLQ ASRGRRDQDY ETRLVHSLAE RRLNEKWSIA
GALIFGCTVA LCFLIRDLMF YVIGGITVSI IAFVFTIKFL CELAARVVSF LQNEDRGRRG
DRSIYDYVRG NYLDPRSCKV SWDWKDPQEV GHTMAFRVQL FYKNGQPYPA NRLVGLRVHI
SHIELALDIP VTQEVLQEPN SNVVKVAFTV RKAGRYEITV KLGGLDVAYS PYYKIFQPGT
VVPSKTKIAS HFSTLVLTNG QQHTLQIEPR DEYGNPTSNS VSLIDEDNYS VRIHPLGTQD
EECSEDYYCK SVSSNKELCQ VLLRLTIRKK GCFRTCISYQ NQPISNGEFD VIVLSENEKN
CVEKNVSTPG VSIYFEAYLY STGNYANASW QLPASSLLAP QRRPSTANED EEEDRDSPSE
GQPEKVKKPK KVYCYISPKQ LSVKEFYLKI IPWRLYTFRV CPGTKFSYHG PDPIHKYLTL
VVDDGIQPPI ELSCKDRNIM AATFIRFLHK NIGGSETFQD KVSFFQRELR HLHSKRPRTK
TCLKISRHSI LDSSLKATRN FSVSDWSKNL EVVFQDEEAL DWGGPRREWF ELICKALFDT
SNQLFTRFSD NNQGLVHPNA DRPPHLRLKV YEFAGRVVGK CLYESALGGA YKQLVRARFT
RSFLAQIIGL RMNYKYFETD DQEFYKTKVC FILNNDVSEM DLVFAEEKYN RSGHLEKVVE
LIAGGSQIAV TNENKIHYLN LLAQYRLANQ VREEVEHFLK GLNELVPENL LAIFDENELE
LLMCGTGDIN VMDFKAHAVI VGGSWHFREK VMKWFWAVVS SFTQEELARL LQFTTGSSQL
PPGGFNTLCP SFQIIAAPTH STLPTAHTCF NQLCLPYYDS YEELHKMLKL AISEGSEGFG
ML
//
