ID   MKRN1_NOTEU             Reviewed;         478 AA.
AC   Q9TT91;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=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;
OS   Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX   NCBI_TaxID=9315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10843807; DOI=10.1006/geno.2000.6199;
RA   Gray T.A., Hernandez L., Carey A.H., Schaldach M.A., Smithwick M.J.,
RA   Rus K., Marshall Graves J.A., Stewart C.L., Nicholls R.D.;
RT   "The ancient source of a distinct gene family encoding proteins featuring
RT   RING and C(3)H zinc-finger motifs with abundant expression in developing
RT   brain and nervous system.";
RL   Genomics 66:76-86(2000).
CC   -!- FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of
CC       ubiquitin moieties onto substrate proteins. These substrates include
CC       FILIP1, p53/TP53, CDKN1A and TERT. Keeps cells alive by suppressing
CC       p53/TP53 under normal conditions, but stimulates apoptosis by
CC       repressing CDKN1A under stress conditions. Acts as a negative regulator
CC       of telomerase. Has negative and positive effects on RNA polymerase II-
CC       dependent transcription. {ECO:0000250|UniProtKB:Q9UHC7}.
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   -!- SUBUNIT: Interacts with p53/TP53 and CDKN1A. Interacts with TERT,
CC       modulating telomere length homeostasis (By similarity). {ECO:0000250}.
CC   -!- PTM: Auto-ubiquitinated; which leads to proteasomal degradation.
CC       {ECO:0000250}.
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DR   EMBL; AF192786; AAF17489.1; -; mRNA.
DR   AlphaFoldDB; Q9TT91; -.
DR   PRIDE; Q9TT91; -.
DR   HOGENOM; CLU_040815_4_1_1; -.
DR   TreeFam; TF315108; -.
DR   UniPathway; UPA00143; -.
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; IPR029035; DHS-like_NAD/FAD-binding_dom.
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; SSF52467; SSF52467; 1.
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   Metal-binding; Repeat; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..478
FT                   /note="E3 ubiquitin-protein ligase makorin-1"
FT                   /id="PRO_0000055953"
FT   ZN_FING         51..78
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         80..107
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         204..231
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         277..331
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         360..389
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          232..259
FT                   /note="Makorin-type Cys-His"
SQ   SEQUENCE   478 AA;  52905 MW;  CB2D9B147433853E CRC64;
     MAEAAAPGTT ATTSGAAAAA AVAAASPTLT PTVASQSPAA GGGGGGSGGG WTKQVTCRYF
     MHGVCKKGNN CRYSHDLSTS QSAMVCRYYQ RGCCAYGDRC RYEHTKPLKR EEVTAANLAA
     KSDLPASSSL PALVEPLAEV STGEAESVNS NFAAAGAGGE DWVNAIEFVP GQPYCGRAAP
     SCTEAPLQGM VIEEELEKQQ TNVEMKKQLC PYAAVGECRY GENCVYLHGD ACDMCGLQVL
     HPVDAAQRSQ HIKSCIEAHE KDMELSFAVQ RSKDMVCGIC MEVVYEKANP SERRFGILSN
     CNHTYCLKCI RKWRSAKQFE SKIIKSCPEC RITSNFVIPS EYWVEEKEEK QKLIQKYKEA
     MSNKPCRYFD EGRGSCPFGG NCFYKHAYPD GRREEPQRQK VGTSNRYRAQ RRNRFWELIE
     ERESSNPFDN DEDEVVTFEL GEMLLMLLAA GGDDDLTDPE DEWDLFHDEL EDYYDLDL