ID A0A2I3N953_PAPAN Unreviewed; 503 AA.
AC A0A2I3N953;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
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 Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000044555.2, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000044555.2, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000044555.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2I3N953; -.
DR Ensembl; ENSPANT00000054732.2; ENSPANP00000044555.2; ENSPANG00000010629.3.
DR GeneTree; ENSGT00950000183077; -.
DR OMA; YESPCAW; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000028761; Chromosome X.
DR Bgee; ENSPANG00000010629; Expressed in testis and 1 other cell type or tissue.
DR ExpressionAtlas; A0A2I3N953; baseline.
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; 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; 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; 1.
DR Pfam; PF18044; zf-CCCH_4; 2.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000028761};
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 80..107
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 109..136
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 233..260
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 306..360
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 389..418
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 80..107
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 109..136
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 233..260
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 389..418
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 54770 MW; EDEDDF5CE700FB4E CRC64;
MAEAAAPGTT ATTSGAGAAA AEAAAAVSPT RIPTVTAPSP RAGGGVGGSD GSGGSGDSAA
SDDSGACGGS GAYGGSGNSW TKQVTCRYFV YGICKEGDNC RYSHDLSDRP CGVVCSCFQR
GYCLYGDRCR CEHSKPLKQE EATATELTTE SSLAASSSLS SIVGPLVEMN TNESESRNSN
FATVGAGSED WANAIEFVPG QPYCGRTVPS CTEAPLQGPV TKEESEKEQT AVETKKELCP
YAAVGQCRYG ENCVYLHGDL CDICGLQALH PMDAAQRSQH IQSCIEAHEK AMEFSFAVQR
SKDRVCGICM EVVYEKANPS EHRFGILSNC NHTFCLKCIR KWRSAKEFES RIVKSCPQCR
ITSNFVIPSE YWVEEKEEKQ KLIQKYKKAM SNKACRYFDE GRGSCPFGEN CFYKHVYPDG
RREEPQRQQE ETSSRHQAQG RNHFLEFFEE GANSNPFDDE EEAVTFELGE MLLMLSTAGG
DNELTDSEDV WDLFCDEFCA LDL
//
