ID G1U3K8_RABIT Unreviewed; 415 AA.
AC G1U3K8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=E3 ubiquitin-protein ligase makorin-2 {ECO:0000256|ARBA:ARBA00029530};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING-type E3 ubiquitin transferase makorin-2 {ECO:0000256|ARBA:ARBA00030863};
GN Name=MKRN2 {ECO:0000313|Ensembl:ENSOCUP00000023971.1};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000023971.1, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000023971.1, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000023971.1,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000023971.1}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000023971.1};
RG Ensembl;
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: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AAGW02056415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008258636.1; XM_008260414.2.
DR AlphaFoldDB; G1U3K8; -.
DR PaxDb; 9986-ENSOCUP00000023971; -.
DR Ensembl; ENSOCUT00000028395.3; ENSOCUP00000023971.1; ENSOCUG00000014171.4.
DR GeneID; 100340148; -.
DR CTD; 23609; -.
DR eggNOG; KOG1039; Eukaryota.
DR GeneTree; ENSGT00950000183077; -.
DR HOGENOM; CLU_040815_0_1_1; -.
DR OMA; MQGVCRE; -.
DR OrthoDB; 2906101at2759; -.
DR Proteomes; UP000001811; Chromosome 9.
DR Bgee; ENSOCUG00000014171; Expressed in testis and 17 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR CDD; cd16731; RING-HC_MKRN2; 1.
DR Gene3D; 2.30.30.1190; -; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045072; MKRN-like.
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:SF17; E3 UBIQUITIN-PROTEIN LIGASE MAKORIN-2; 1.
DR PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF00642; zf-CCCH; 3.
DR Pfam; PF14608; zf-CCCH_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF90229; CCCH zinc finger; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50103; ZF_C3H1; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 2..29
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 31..58
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 165..192
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 238..292
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 321..350
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 2..29
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 31..58
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 165..192
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 321..350
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 118..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 46216 MW; 44A7DA6E667A302C CRC64;
MSTKQVTCRY FMHGVCREGS QCLFSHDLAN SKPSTICKYY QKGYCAYGTR CRYDHTRPSA
AAAGAVGALP HAVPSPGCHS PRPSSDLTVS LVKTHSNEPG KREKRTLVLR DRNLSGLAEE
KAPPSAVSNP GSCSDPQTSL EVKPHSYLDA IRSGLDDLEA SSSYSSEQQL CPYAAAGACR
FGAACVYLHG DVCEICRLPV LHPFDPEQRK AHEKICMSTF EHEMEKAFAF QASQDKVCSI
CMEVILEKAS ASERRFGILS NCNHTYCLSC IRQWRCAKQF ENPIIKSCPE CRVISEFVIP
SVYWVEDQNK KNELIEAFKQ GMGKKACKYF EQGKGTCPFG SKCLYRHAYP DGRLAEPEKP
RKQLSSEGTV RFFNSVRLWD FIENRESQHV PSADDDVTEL GDLFMHLSGV ESSAP
//
