ID   A0A1S3P186_SALSA        Unreviewed;       285 AA.
AC   A0A1S3P186;
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=LOC106582589 {ECO:0000313|RefSeq:XP_014021291.1};
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_014021291.1};
RN   [1] {ECO:0000313|RefSeq:XP_014021291.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014021291.1};
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}.
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DR   RefSeq; XP_014021291.1; XM_014165816.1.
DR   AlphaFoldDB; A0A1S3P186; -.
DR   STRING; 8030.ENSSSAP00000060636; -.
DR   PaxDb; 8030-ENSSSAP00000060636; -.
DR   OrthoDB; 1342875at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000087266; Chromosome ssa21.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR046356; MARCHF4/9/11.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46053; E3 UBIQUITIN-PROTEIN LIGASE MARCH4-LIKE; 1.
DR   PANTHER; PTHR46053:SF3; E3 UBIQUITIN-PROTEIN LIGASE MARCHF4; 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        206..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          123..183
FT                   /note="RING-CH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51292"
FT   REGION          43..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   285 AA;  31701 MW;  0446495C688A7B3B CRC64;
     MLRGLDMLKS RCCVLFGDLK VLLLRTPTPV SIPTTGHIPD SHVVPSEVSV PDNNTLTAHE
     GQRDVWTAPP PGAANGPERD RLSGWVDAAA TEPSEVLHCS GSSDSWAKDK LEQRFSLCSY
     SESGSIRTPV CRICFQGPET GELLSPCRCS GSVRCTHQPC LIKWISERGS WACELCYYKY
     QVISISTRNP LQWQSISLAG IEKVQIAAAL LGSMFLVASL SWLVWSSFSP SARWQRHDLL
     FQICYGMYGF MDVVCFALII HEGPSVFRIF NRWKATTTRP LTVRT
//