RN157_RAT
ID RN157_RAT Reviewed; 682 AA.
AC M0R5D6;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=E3 ubiquitin ligase Rnf157 {ECO:0000303|PubMed:25342469};
DE EC=2.3.2.27 {ECO:0000269|PubMed:25342469};
DE AltName: Full=RING finger protein 157 {ECO:0000303|PubMed:25342469};
DE AltName: Full=RING-type E3 ubiquitin transferase Rnf157 {ECO:0000305};
GN Name=Rnf157;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=25342469; DOI=10.1038/cdd.2014.163;
RA Matz A., Lee S.J., Schwedhelm-Domeyer N., Zanini D., Holubowska A.,
RA Kannan M., Farnworth M., Jahn O., Goepfert M.C., Stegmueller J.;
RT "Regulation of neuronal survival and morphology by the E3 ubiquitin ligase
RT RNF157.";
RL Cell Death Differ. 22:626-642(2015).
CC -!- FUNCTION: E3 ubiquitin ligase that ubiquitinates APBB1 for its
CC degradation by the proteasome and thus prevents apoptosis and promotes
CC survival of neurons (By similarity). Has a dual role in neurons as it
CC is also required for dendrite growth and maintenance for which its
CC ligase activity is not critical (By similarity). May act as a scaffold
CC molecule to regulate this process (By similarity). Acts as a downstream
CC effector of the interconnected PI3K and MAPK signaling pathways and
CC thus participates in the regulation of the cell cycle (By similarity).
CC {ECO:0000250|UniProtKB:Q96PX1}.
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:0000250|UniProtKB:Q96PX1};
CC -!- SUBUNIT: Interacts with APBB1 (By similarity). Interacts with CHD1;
CC CHD1-binding controls RNF157 stability (By similarity). Interacts also
CC with ATRN, MEGF8, TECR, MSI2, PLRG1, BYSL, MTERF3, PSMA1, MRPS18B,
CC PRPF4, FASTKD2, SLC25A1, SMU1, CNOT9, MRPS2, MAGT1, FXR2, EMD, PSMD8,
CC HDAC1, RAN, HSD17B12, TXNDC5 AND MRPL19 (By similarity).
CC {ECO:0000250|UniProtKB:Q96PX1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25342469}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain
CC (PubMed:25342469). {ECO:0000269|PubMed:25342469}.
CC -!- DOMAIN: The D-box motifs play a key role in RNF157 stabilization.
CC {ECO:0000250|UniProtKB:Q96PX1}.
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DR EMBL; AABR07030824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M0R5D6; -.
DR RGD; 1591154; Rnf157.
DR VEuPathDB; HostDB:ENSRNOG00000049862; -.
DR HOGENOM; CLU_016631_2_0_1; -.
DR OMA; EDSCPVH; -.
DR PRO; PR:M0R5D6; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000049862; Expressed in frontal cortex and 17 other tissues.
DR ExpressionAtlas; M0R5D6; baseline and differential.
DR GO; GO:0044297; C:cell body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IMP:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996; PTHR22996; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Lipoprotein; Metal-binding; Myristate; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..682
FT /note="E3 ubiquitin ligase Rnf157"
FT /id="PRO_0000442439"
FT ZN_FING 277..317
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 440..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 330..333
FT /note="D-box 1"
FT /evidence="ECO:0000250|UniProtKB:Q96PX1"
FT MOTIF 658..661
FT /note="D-box 2"
FT /evidence="ECO:0000250|UniProtKB:Q96PX1"
FT COMPBIAS 443..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PX1"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PX1"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PX1"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 682 AA; 74565 MW; EEC116375F3B4C52 CRC64;
MGALTSRQHA GVEEVDIPSN SVYRYPPKSG SYFASHFIMG GEKFDCTHPE GYLFGENSDL
NFLGNRPVSF PYAAPPPHEP VKTLRSLINI RKDTLRLVKC AEEVKSHGEE AGKAKVHYNV
EFTFDTDARV AITIYYQATE EFQNGIASYI PKDNSLQSET VHYKRGVCQQ FCLPSHTVDP
SEWAEEELGF DLDREVYPLV VHAVVDEGDE YFGHCHVLLG TFEKHSDGTF CVKPLKQKQV
WDGVTYLLQE DYGIENKSNT QDFKVAEDDV RDNSAECVVC LSDVRDTLIL PCRHCASCNV
HCADTLRYQA NNCPICRLPF RALLQIRAMR KKLGPLSPSS FNPIISSQTS DSEEHSSSEN
IPAGYEVVSL LEALNGPLTS SPAVPPLHVL GDGHLSGMLP SYGSDGHLPP VRTLSPLDHL
SDCNSQGLKL NKSLSKSISQ NSSVLHEEED ERSCSESDTQ LSQRLSAQHP EEGPDVTPES
ENLTLSSSGA VDQSSCTGTP LSSTISSPED PASSSLAQSV MSMASSQIST DTVSSMSGSY
IAPGTEEEGE APPSPRAASR APSEEEETPA ESPDSNFAGL PAGEQDAEGN DIMEEEDRSP
VQEDGQRTCA FLGMECDNNN DFDVASVKAL DNKLCSEVCL PGTWQHDAAI INRHNTQRRR
LSPSSLEDPE EDRPCVWDPL AV
