GenomeNet

Database: UniProt
Entry: A0A0G2QC60_RAT
LinkDB: A0A0G2QC60_RAT
Original site: A0A0G2QC60_RAT 
ID   A0A0G2QC60_RAT          Unreviewed;       220 AA.
AC   A0A0G2QC60;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Rhombotin-2 {ECO:0000256|ARBA:ARBA00040621};
DE   AltName: Full=LIM domain only protein 2 {ECO:0000256|ARBA:ARBA00041884};
GN   Name=Lmo2 {ECO:0000313|Ensembl:ENSRNOP00000012625.7,
GN   ECO:0000313|RGD:1307101};
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:ENSRNOP00000012625.7, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000012625.7, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000012625.7,
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:0000313|Ensembl:ENSRNOP00000012625.7}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000012625.7};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; NP_001032435.2; NM_001037358.2.
DR   AlphaFoldDB; A0A0G2QC60; -.
DR   SMR; A0A0G2QC60; -.
DR   STRING; 10116.ENSRNOP00000012625; -.
DR   PaxDb; 10116-ENSRNOP00000012625; -.
DR   Ensembl; ENSRNOT00000012625.7; ENSRNOP00000012625.7; ENSRNOG00000009401.8.
DR   GeneID; 362176; -.
DR   KEGG; rno:362176; -.
DR   AGR; RGD:1307101; -.
DR   CTD; 4005; -.
DR   RGD; 1307101; Lmo2.
DR   eggNOG; KOG0490; Eukaryota.
DR   GeneTree; ENSGT00940000160199; -.
DR   InParanoid; A0A0G2QC60; -.
DR   OrthoDB; 2875464at2759; -.
DR   TreeFam; TF351071; -.
DR   Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000009401; Expressed in spleen and 19 other cell types or tissues.
DR   ExpressionAtlas; A0A0G2QC60; baseline and differential.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR   GO; GO:0043425; F:bHLH transcription factor binding; ISO:RGD.
DR   GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR   GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR   GO; GO:0035162; P:embryonic hemopoiesis; ISO:RGD.
DR   GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   CDD; cd09384; LIM1_LMO2; 1.
DR   CDD; cd09385; LIM2_LMO2; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR45787; LD11652P; 1.
DR   PANTHER; PTHR45787:SF3; RHOMBOTIN-2; 1.
DR   Pfam; PF00412; LIM; 2.
DR   SMART; SM00132; LIM; 2.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE   4: Predicted;
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          90..152
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          154..216
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..62
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   220 AA;  24590 MW;  AB98B68E75ABEC82 CRC64;
     MEGSAVTVLE RGGASSPAER PSKRRRRSGG ARAPEGVRVQ AASQPRATKG APPPPGTPPP
     SPMSSAIERK SLDPSEEPVD EVLQIPPSLL TCGGCQQNIG DRYFLKAIDQ YWHEDCLSCD
     LCGCRLGEVG RRLYYKLGRK LCRRDYLRLF GQDGLCASCD KRIRAYEMTM RVKDKVYHLE
     CFKCAACQKH FCVGDRYLLI NSDIVCEQDI YEWTKINGII
//
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