ID A0A1S3LY71_SALSA Unreviewed; 913 AA.
AC A0A1S3LY71;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=LOC106569226 {ECO:0000313|RefSeq:XP_013995857.1};
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_013995857.1};
RN [1] {ECO:0000313|RefSeq:XP_013995857.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013995857.1};
RG RefSeq;
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_013995857.1; XM_014140382.1.
DR AlphaFoldDB; A0A1S3LY71; -.
DR STRING; 8030.ENSSSAP00000086647; -.
DR PaxDb; 8030-ENSSSAP00000086647; -.
DR GeneID; 106569226; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000087266; Chromosome ssa14.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR PANTHER; PTHR13145; SSM4 PROTEIN; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 102..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 522..540
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 631..653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 673..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 718..741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 761..783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 807..832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 852..870
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..63
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 179..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 102799 MW; 0C1F452E04653E8F CRC64;
MDTAEEGDIC RVCRSEGTLD KPLYHPCVCT GSIKFIHQEC LVQWLKHSRK EYCELCKHRF
AFTPIYSPDM PSRLPVQDIF AGLLTSVGTA IRYWFHYTLV AFAWLGVVPL TACRIYKCLF
TGSVSSLLTL PLDMLSTENL LADCLQGCFV VTCTLCAFIS LVWLREQIVH GGAPQWLEQN
QQQPQHAPAP QPNEQAPGPG QGAAENQPAP VAAEPPADNG PAAEVPDIQM DPAEDMELED
EAGAEDVADA NNGAQDDMNW NALEWDRAAE ELTWERMLGL DGSLVFLEHV FWVVSLNTLF
ILVFAFCPYH IGHFTVVGLG FEENVRASHF EGLITTIVGY ILLAMLLILC HGLAALVRFQ
RSRHLLGVCY IVVKVSLLVV VEIGVFPLIC GWWLDICSLE MFDASLKDRE LSFDSAPGTT
MFLHWLVGMV YVFYFASFIL LLREVLRPGV LWFLRNLNDP DFNPVQEMIH LPIYRHLRRF
ILSVVVFGSI VLLMLWLPIR TIKLILPAFL PYNVMLYSDA PVSELSLELL LLQVVLPALL
EQGHTRQWLK GLVRAWTVTA GYLLDLHSYL LGDQEENDDD ADQQANNNQQ RRNNNNAIPE
GLHAAHQAIL QQGGPVGVQP YHRPMKFTFR IVLLIVFMCV TLLVASLACL TLPVFTGRYL
MSFWTGSAKI HELYTAACGL YVCWLSIRVI TVLLSWMPQG RRAILLKVQE WTLMILKTVV
IAVLLAGAIP LLLGLLFEMV IVAPLRVPLD QTPLFYPWQD WALGVLHAKI IAAITLMGPQ
WWLKTVIEQV YANGIRNIDL HFIIRKLAAP VICVLLVSLC VPYVISAGIV PIVAQYSPGV
TMEMQNLVQR RIYPFLLMVV MLLGILSFQI RQFKRLYEHI KNDKYLVGQR LVNYERKAAG
RSSTATHSSS SQE
//
