GenomeNet

Database: UniProt
Entry: M0R9X3_RAT
LinkDB: M0R9X3_RAT
Original site: M0R9X3_RAT 
ID   M0R9X3_RAT              Unreviewed;       565 AA.
AC   M0R9X3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=RNA binding motif 31, Y-linked {ECO:0000313|Ensembl:ENSRNOP00000066307.1};
GN   Name=Rbm31y {ECO:0000313|Ensembl:ENSRNOP00000066307.1,
GN   ECO:0000313|RGD:1562219};
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 {ECO:0000313|Ensembl:ENSRNOP00000066307.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000066307.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000066307.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
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] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000066307.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000066307.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_001066404.1; XM_001066404.4.
DR   RefSeq; XP_229073.1; XM_229073.4.
DR   AlphaFoldDB; M0R9X3; -.
DR   SMR; M0R9X3; -.
DR   STRING; 10116.ENSRNOP00000066307; -.
DR   iPTMnet; M0R9X3; -.
DR   PhosphoSitePlus; M0R9X3; -.
DR   jPOST; M0R9X3; -.
DR   PaxDb; 10116-ENSRNOP00000066307; -.
DR   Ensembl; ENSRNOT00000004491.6; ENSRNOP00000066307.1; ENSRNOG00000003377.6.
DR   KEGG; rno:302780; -.
DR   AGR; RGD:1562219; -.
DR   CTD; 74484; -.
DR   RGD; 1562219; Rbm31y.
DR   eggNOG; KOG0118; Eukaryota.
DR   GeneTree; ENSGT00940000154426; -.
DR   HOGENOM; CLU_482287_0_0_1; -.
DR   InParanoid; M0R9X3; -.
DR   OMA; ANPNVYM; -.
DR   OrthoDB; 5189206at2759; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000003377; Expressed in testis.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR   GO; GO:0034046; F:poly(G) binding; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   PANTHER; PTHR48033; RNA-BINDING (RRM/RBD/RNP MOTIFS) FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48033:SF14; RNA-BINDING MOTIF 31, Y-LINKED; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF101967; Adhesin YadA, collagen-binding domain; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT   DOMAIN          33..110
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          118..197
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          203..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   565 AA;  62292 MW;  A746F49E3675EA09 CRC64;
     MNTASLAVRK YNERDQLREG FRIDATKNQQ DASKMFIGGL SQELNKQVLL EYLSKFGEII
     DFIIKIDPNT GLSRGFGFVL FKDSSTVEKV LRVKDHKVDG KKIEFKRAKA LESQFPIKKV
     FVGGLNPRMS EEKIRAYFGT FGQIEAIELP LCSDTQERRA FGFIKYMDEN PVRKVLETRY
     HFIGSSRCEV KMAFPKEYPA RQLSKSKTRA KDRARTAVPA AELENHWRGG GSQNFHIMDN
     SDTQEANQDA HRAGSYTSRA NSDVTLSNAR GFRDTPNAFQ ANPNVIVTNS SAFRASRTAL
     RPISNTVGLS HYALGANPNA FLANQYTFGA IPNALRTSQY TLGTYPNALG VSQYALAAYP
     NAFGINQCTL GANPNVFWTN QYPLGTYPDA FGIGQYAWNM SPNVFGANQY TLGTNSDAFR
     PNCYSFVANP YDIRTNHYVL ATNPNVSRTS QYILGANPNA FGSSHYSVGA SQNVFGPNQH
     SFGVNGNFCG AAGSSGGTGG FNFSQVYGNF LNVCNTLPAF HGSNGDYFFL YSYGAYDVGS
     APNYNVQINQ STLLGNGYQG IYSAF
//
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