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Database: UniProt
Entry: A0A2I2YMI5_GORGO
LinkDB: A0A2I2YMI5_GORGO
Original site: A0A2I2YMI5_GORGO 
ID   A0A2I2YMI5_GORGO        Unreviewed;       389 AA.
AC   A0A2I2YMI5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, 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};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000036151.1, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000036151.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000036151.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000036151.1}
RP   IDENTIFICATION.
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}.
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DR   EMBL; CABD030123983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2YMI5; -.
DR   Ensembl; ENSGGOT00000068653.1; ENSGGOP00000036151.1; ENSGGOG00000024940.2.
DR   GeneTree; ENSGT00950000183077; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001519; Chromosome X.
DR   Bgee; ENSGGOG00000024940; Expressed in testis and 4 other cell types or tissues.
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:0000209; P:protein polyubiquitination; IEA:InterPro.
DR   CDD; cd16730; RING-HC_MKRN1_3; 1.
DR   Gene3D; 2.30.30.1190; -; 1.
DR   Gene3D; 3.30.1370.210; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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:SF53; E3 UBIQUITIN-PROTEIN LIGASE MAKORIN-4-RELATED; 1.
DR   PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR   Pfam; PF15815; MKRN1_C; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF14608; zf-CCCH_2; 2.
DR   Pfam; PF18044; zf-CCCH_4; 2.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 4.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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          1..21
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          28..50
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          147..174
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          220..274
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          303..332
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         1..21
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         28..50
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         147..174
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         303..332
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ   SEQUENCE   389 AA;  44205 MW;  8D07BD49F4D16C58 CRC64;
     MIPEYGICKE GDNCRYSHDL SDRLCGVVCK YFQRGCCVYG DRCRCEHSKP LKQEEAPATE
     LTTKSSLAAS SSLSSIVGPL VEMNTNEAES RNSNFATVVA GSEDWANAIE FVPGQPYCGR
     TVPSCTEAPL QGSVTKEESE EEQTAVETKK QLCPYAAVGQ CRYGENCVYL HGDLCDMCGL
     QVLHPMDAAQ RSQHIQACTE AHEKDMEFSF AVQRSKDKVC GICMEVIYEK ANPNEHRFGI
     LSNCNHTFCL KCIRKWRSAK EFESRIVKSC PQCRITSNFV IPSEYWVEEK EEKQKLIQKY
     KEAMSDKACK YFDEGRGSCP FGENCFYKHM YPDGRREEPQ RQQVGTSSRN PGQRRNHFWE
     FFEEGANSNP FDDEEEAVTF ELGEMLLML
//
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