ID   MKRN1_TAKRU             Reviewed;         429 AA.
AC   Q5NU14; Q5KSL0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase makorin-1;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferase makorin-1 {ECO:0000305};
GN   Name=mkrn1 {ECO:0000312|EMBL:BAD80899.1};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAD80899.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC   TISSUE=Liver {ECO:0000312|EMBL:BAD86842.1}, and
RC   Ovary {ECO:0000312|EMBL:BAD80899.1};
RA   Abe S., Kobayashi Y.;
RT   "Takifugu rubripes mRNA for MKRN1, complete CDS.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of
CC       ubiquitin moieties onto substrate proteins. {ECO:0000250}.
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;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000269|Ref.1};
CC         IsoId=Q5NU14-1; Sequence=Displayed;
CC       Name=b {ECO:0000269|Ref.1};
CC         IsoId=Q5NU14-2; Sequence=VSP_052995;
CC   -!- MISCELLANEOUS: [Isoform b]: Non-canonical splice acceptor and donor
CC       sites. {ECO:0000305}.
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DR   EMBL; AB182269; BAD80899.1; -; mRNA.
DR   EMBL; AB185115; BAD86842.1; -; mRNA.
DR   RefSeq; NP_001072050.1; NM_001078582.1. [Q5NU14-1]
DR   AlphaFoldDB; Q5NU14; -.
DR   STRING; 31033.ENSTRUP00000030501; -.
DR   GeneID; 777952; -.
DR   KEGG; tru:777952; -.
DR   CTD; 23608; -.
DR   eggNOG; KOG1039; Eukaryota.
DR   InParanoid; Q5NU14; -.
DR   OrthoDB; 1388677at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR045072; MKRN-like.
DR   InterPro; IPR031644; MKRN1_C.
DR   InterPro; IPR041367; Znf-CCCH_4.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11224; PTHR11224; 1.
DR   Pfam; PF15815; MKRN1_C; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF18044; zf-CCCH_4; 3.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 4.
DR   SUPFAM; SSF90229; SSF90229; 2.
DR   PROSITE; PS50103; ZF_C3H1; 4.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Metal-binding; Reference proteome; Repeat;
KW   Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..429
FT                   /note="Probable E3 ubiquitin-protein ligase makorin-1"
FT                   /id="PRO_0000361046"
FT   ZN_FING         18..45
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         48..75
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         153..180
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         226..280
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         309..338
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          181..208
FT                   /note="Makorin-type Cys-His"
FT                   /evidence="ECO:0000255"
FT   REGION          343..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         52..136
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_052995"
FT   CONFLICT        312
FT                   /note="R -> S (in Ref. 1; BAD86842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        321
FT                   /note="G -> S (in Ref. 1; BAD86842)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   429 AA;  48903 MW;  A41963827049068D CRC64;
     MAEAAVASTV TLPVTGGWTK HVTCRYFMHG LCKEGDNCRY SHDLTSSKPA AMMCKFFQKG
     NCVFGERCRF EHCKPTKSEE VSNPQMLLLS STPPPIDPEC SESGPRLKTQ DWANAAEFVP
     GQPYCGRAES VDVEISIPLI EELNGDATTD KEELRKQLCP YAAVGECRYG VNCAYLHGDV
     CDMCGLQVLH PTDSSQRSEH TKACIEAHEK DMEISFAIQR SKDMMCGVCM EVVFEKANPS
     ERRFGILSNC SHCYCLKCIR KWRSAKQFES KIIKSCPECR ITSNFVIPSE YWVEDKEDKQ
     KLIQKYKDGM GRKPCRYFDE GRGICPFGAN CFYKHAFPDG RLEEAQPQRR QTGSSSRNRN
     SRRTQLWDII DERESTGSLD NDDEEMVTFE LSEMLLMLLA AGNDEEVTDS EDEWDLFHEE
     LDDFYEIYL