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Database: UniProt
Entry: A0A1S3SPV7_SALSA
LinkDB: A0A1S3SPV7_SALSA
Original site: A0A1S3SPV7_SALSA 
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
//
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