ID A0A1S3SPV7_SALSA Unreviewed; 1023 AA.
AC A0A1S3SPV7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=LOC106611059 {ECO:0000313|RefSeq:XP_014066384.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014066384.1};
RN [1] {ECO:0000313|RefSeq:XP_014066384.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014066384.1};
RG RefSeq;
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};
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DR RefSeq; XP_014066384.1; XM_014210909.1.
DR AlphaFoldDB; A0A1S3SPV7; -.
DR STRING; 8030.ENSSSAP00000058849; -.
DR PaxDb; 8030-ENSSSAP00000058849; -.
DR GeneID; 106611059; -.
DR KEGG; sasa:106611059; -.
DR OMA; WQLWSSA; -.
DR OrthoDB; 5480520at2759; -.
DR Proteomes; UP000087266; Chromosome ssa09.
DR Bgee; ENSSSAG00000055185; Expressed in semen and 15 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
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:UP000087266};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1023
FT /note="HECT-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010302867"
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 683..1023
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 523..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 990
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1023 AA; 117634 MW; BE914BECF1BD70E2 CRC64;
MDRRFLLTFL FCSVSWIFFW EVCWKKGKES QIEEWIQGHS LSEYKHLLED VETLEELSLS
VLTRLEDVVR EKRRWRDIAE AHIQLLRDFA FQEWLCSQSL EHYYHTLKTL GCMTLDDLAQ
FDSQLQLSLA AWGYYYEDYI KLSTGVKVLQ ASRGSRDQDY EIQLVHNLAE RRLNEKWSIA
GALIFGCTVA LCFLIRDLMF YVIGGITVSI IAFVFTIKFL CELAARVVSF LQNDDTGRRG
DRSIYDYVRG NYLDPRSCNV SWDWKDPQEV GQTMSFRVQL FYKNGQPFPA HRPVGLRVNI
THIELALDIP VTQEVLQEPE SNVVKVTFTV RKAGRYEVAV KLGGLNVAYS PYYKIFQPGT
VVPSKTKIAY HFSTLVLVYG QQHTLQIEPR DEYGNPTSNS TSLIDEVNYS VHVHSLGTVD
DDSLEEYYSK SVTSNKQLCQ VLLKLTLRKK GCFRARISYN DLPISNGEFD IIVLSENEKN
CVEKNVSTPG ISIYFEAYLY GAGNYSNYSN SSWQLPASAL MAPQSRPSMG DEEDEHDSPV
EDQPEKVKKP KKVYCYISPK QLSVKEFYLK IIPWRLFTFR VCPGTKFTYY GPDPVHKYLT
LVVDDGIQPP VELSCKDRNI MAATFIRFLH KNIGGSETFQ DKVSFFQREL RHIHSKRPRT
KTCLKITRHC ILDSSLKSTR NFSVSDWSKN FEVVFQDEEA LDWGGPRREW FELVCKTLFD
TTNQLFTRFS DDNQGLVHPN AERPAHLRLK MYEFAGRVVG KCLYESALGG AYKQMVRARF
TRSFLAQIIG LRMNYKYFET DDQEFYKMKV CVILNNDVSE MDLVFAEEKY SKSGQLEKVV
ELISGGAQIA VNNENKMHYL NLLAQYRLAS QVRDEVEHFL KGLNELVPEN LLAIFDENEL
ELLLCGTGDI DVQDFKAHAV VVGGSWHFRE KVMKWFWAVV SSFTQEELAR LLQFTTGSSQ
LPPGGFSTLC PSFQIIAAPT HSTLPTAHTC FNQLCLPTYD SYEELHKMLK LAISEGSEGF
GML
//