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RN227_MOUSE
ID   RN227_MOUSE             Reviewed;         190 AA.
AC   Q9DCB3; A0A140LI80; Q9JJ82;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-JUL-2018, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=RING finger protein 227 {ECO:0000305};
GN   Name=Rnf227 {ECO:0000250|UniProtKB:A6NIN4};
GN   Synonyms=Chd3os {ECO:0000312|MGI:MGI:1915359};
GN   ORFNames=MNCb-2875 {ECO:0000312|EMBL:BAA95115.1};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-190.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 93-190.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT   oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA95115.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB22482.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL645527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK002962; BAB22482.1; ALT_INIT; mRNA.
DR   EMBL; AB041807; BAA95115.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q9DCB3; -.
DR   PhosphoSitePlus; Q9DCB3; -.
DR   PRIDE; Q9DCB3; -.
DR   Ensembl; ENSMUST00000129321; ENSMUSP00000146712; ENSMUSG00000043419.
DR   MGI; MGI:1915359; Rnf227.
DR   VEuPathDB; HostDB:ENSMUSG00000043419; -.
DR   GeneTree; ENSGT00390000002475; -.
DR   InParanoid; Q9DCB3; -.
DR   OMA; REEDCMT; -.
DR   ChiTaRS; Chd3os; mouse.
DR   PRO; PR:Q9DCB3; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9DCB3; protein.
DR   Bgee; ENSMUSG00000043419; Expressed in superior colliculus and 207 other tissues.
DR   ExpressionAtlas; Q9DCB3; baseline and differential.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR027952; DUF4632.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF15451; DUF4632; 1.
DR   Pfam; PF14634; zf-RING_5; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..190
FT                   /note="RING finger protein 227"
FT                   /id="PRO_0000329084"
FT   ZN_FING         18..81
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          108..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        115
FT                   /note="D -> G (in Ref. 3; BAA95115)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        160
FT                   /note="A -> E (in Ref. 3; BAA95115)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   190 AA;  20820 MW;  3B3EBFE3A1948FF3 CRC64;
     MQLLMRVPSL PELGELDCNI CFRPYNLGAR APRRLPGTAR ARCGHTLCTA CLRELAARGD
     GSRTAARVVR LRRAVTCPFC RAPSPLPRGG VTEIALDPVL WSRLEEKARA EREGDPMGSP
     AKDSGEDGED DDGEAESEKG AGPPSAGWRA LRRILDRVLA PARRLRRPLP SNVLYCPEVK
     DIAHMTRCTL
 
 
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