GenomeNet

Database: UniProt
Entry: A0A096NZF9_PAPAN
LinkDB: A0A096NZF9_PAPAN
Original site: A0A096NZF9_PAPAN 
ID   A0A096NZF9_PAPAN        Unreviewed;      1888 AA.
AC   A0A096NZF9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN   Name=UBR3 {ECO:0000313|Ensembl:ENSPANP00000018480.3};
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:ENSPANP00000018480.3, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000018480.3, 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:ENSPANP00000018480.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC       rule pathway. Recognizes and binds to proteins bearing specific N-
CC       terminal residues that are destabilizing according to the N-end rule,
CC       leading to their ubiquitination and subsequent degradation.
CC       {ECO:0000256|RuleBase:RU366018}.
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         ECO:0000256|RuleBase:RU366018};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC   -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC       ECO:0000256|RuleBase:RU366018}.
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DR   STRING; 9555.ENSPANP00000018480; -.
DR   Ensembl; ENSPANT00000021922.3; ENSPANP00000018480.3; ENSPANG00000005674.3.
DR   eggNOG; KOG1139; Eukaryota.
DR   GeneTree; ENSGT00950000183075; -.
DR   HOGENOM; CLU_000651_2_1_1; -.
DR   OMA; ICNCTTA; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000028761; Chromosome 10.
DR   Bgee; ENSPANG00000005674; Expressed in gastrocnemius and 69 other cell types or tissues.
DR   ExpressionAtlas; A0A096NZF9; baseline.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0042048; P:olfactory behavior; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl.
DR   GO; GO:0001967; P:suckling behavior; IEA:Ensembl.
DR   GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR   CDD; cd16483; RING-H2_UBR3; 1.
DR   CDD; cd19673; UBR-box_UBR3; 1.
DR   Gene3D; 2.10.110.30; -; 1.
DR   InterPro; IPR044046; E3_ligase_UBR-like_C.
DR   InterPro; IPR039164; UBR1-like.
DR   InterPro; IPR003126; Znf_UBR.
DR   PANTHER; PTHR21497:SF39; E3 UBIQUITIN-PROTEIN LIGASE UBR3; 1.
DR   PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR   Pfam; PF18995; PRT6_C; 1.
DR   Pfam; PF02207; zf-UBR; 1.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU366018};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU366018};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW   Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT   DOMAIN          118..189
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51157"
FT   ZN_FING         118..189
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1008..1028
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1164..1186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1028
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1171..1186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1888 AA;  212546 MW;  9AF91346E0D2ECB7 CRC64;
     MAAAAAAAVG GQQPSQPELP ASGLALDKAA TAAHLKAALS RPDNRAGAEE LQALLERVLS
     AERPLAAAAG GEDAAAAGGG GGPGAAEEEA LEWCKCLLAG GGGYDEFCAA VRAYDPAALC
     GLVWTANFVA YRCRTCGISP CMSLCAECFH QGDHTGHDFN MFRSQAGGAC DCGDSNVMRE
     SGFCKRHQIK SSSNIPCVPK DLLMMSEFVL PRFIFCLIQY LREGYNEPAA DGPSEKDLNK
     VLQLLEPQIS FLEDLTKMGG AMRSVLTQVL TNQQNYKDLT SGLGENACVK KSHEKYLIAL
     KSSGLTYPED KLVYGVQEQS AGTSSLAVQG FVGATGTLGQ VDSSDEDDQD GSQGLGKRKR
     VKLSSGTKDQ SIMDVLKHKS FLEELLFWTI KYEFPQKMVT FLLNMLPDQE YKVAFTKTFV
     QHYAFIMKTL KKSHESDTMS NRIVHISVQL FSNEELARQV TEECQLLDIM VTVLLYMMES
     CLIKSELQDE ENSLHVVVNC GEALLKNNTY WPLVSDFINI LSHQSVAKRF LEDHGLLVTW
     MNFVSFFQGM NLNKRELNEH VEFESQTYYA AFAAELEACA QPMWGLLSHC KVRETQEYTR
     NVVRYCLEAL QDWFDAINFV DEPAPNQVTF HLPLHRYYAM FLSKAVKCQE LDLDSVLPDQ
     EMLMKLMIHP LQIQASLAEI HSNMWVRNGL QIKGQAMTYV QSHFCNSMID PDIYLLQVCA
     SRLDPDYFIS SVFERFKVVD LLTMASQHQN TVLDAEHERS MLEGALTFLV ILLSLRLHLG
     MSDDEILRAE MVAQLCMNDR THSSLLDLIP ENPNPKSGII PGSYSFESVL SAVADFKAPV
     FEPGGSMQQG MYTPKAEVWD QEFDPVMVIL RTVYRRDVQS AMDRYTAFLK QSGKFPGNPW
     PPYKKRTSLH PSYKGLMRLL HCKTLHIVLF TLLYKILMDH QNLSEHVLCM VLYLIELGLE
     NSAEEESDEE ASVGGPERCH DSWFPGSNLV SNMRHFINYV RVRVPETAPE VKRDSPASTS
     SDNLGSFQNS GTAQVFSLVA ERRKKFQEII NRSSSEANQV VRPKTSSKWS APGSAPQLTT
     AILEIKESIL SLLIKLHHKL SGKQNSYYPP WLDDIEILIQ PEIPKYSHGD GITAVERILL
     KAASQSRMNK RIIEEICRKV TPPVPPKKVT AAEKKTLDKE ERRQKARERQ QKLLAEFASR
     QKSFMETAMD VDSPENDIPM EITTAEPQVS EAVYDCVICG QSGPSSEDRP TGLVVLLQAS
     SVLGQCRDNV EPKKLPITEE EQIYPWDTCA AVHDVRLSLL QRYFKDSSCL LAVSIGWEGG
     VYVQTCGHTL HIDCHKSYME SLRNDQVLQG FSVDKGEFTC PLCRQFANSV LPCYPGSNVE
     NNPWQRPSNK SIQDLIKEVE ELQGRPGAFP SETNLSKEME SVMKDIKNTT QKKYRDYSKT
     PGSPDNDFLF MYSVARTNLE LELIHRGGNL CSGGASTAGK RSCLNQLFHV LALHMRLYSI
     DSEYNPWRKL TQLEEMNPQL GYEEQQPEVP ILYHDVTSLL LIQILMMPQP LRKDHFTCIV
     KVLFTLLYTQ ALAELSVKCS EEDRSAWKHA GALKKSTCDA EKSYEVLLSF VISELSKGKL
     YHEEGTQECA MVNPIAWSPE SMEKYLQDFC LPFLRITSLL QHHLFGEDLP SCQEEEEFSV
     LASCLGLLPT FYQTEHPFIS ASCLDWPVPA FDIITQWCFE IKSFTERHAE QGKALLIQES
     KWKLPHLLQL PENYNTIFQY YHRKTCSVCT KVPKDPAVCL VCGTFVCLKG LCCKQQSYCE
     CVLHSQNCGA GTGIFLLINA SVIIIIRGHR FCLWGSVYLD AHGEEDRDLR RGKPLYICKE
     RYKVLEQQWI SHTFDHINKR WGPHYNGL
//
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