ID RUFY2_MOUSE Reviewed; 606 AA. AC Q8R4C2; Q69ZH1; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 2. DT 27-MAR-2024, entry version 128. DE RecName: Full=RUN and FYVE domain-containing protein 2; DE AltName: Full=Leucine zipper FYVE-finger protein; DE Short=LZ-FYVE; GN Name=Rufy2; Synonyms=Kiaa1537; 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 [MRNA], DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION. RC TISSUE=Embryo; RX PubMed=11506704; DOI=10.1089/104454901750361460; RA Dunkelberg J.C., Gutierrez-Hartmann A.; RT "LZ-FYVE: a novel developmental stage-specific leucine zipper, FYVE-finger RT protein."; RL DNA Cell Biol. 20:403-412(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/cJ; TISSUE=Brain; RX PubMed=11877430; DOI=10.1074/jbc.m111933200; RA Yang J., Kim O., Wu J., Qiu Y.; RT "Interaction between tyrosine kinase Etk and a RUN-domain and FYVE-domain RT containing protein RUFY1. A possible role of Etk in regulation of vesicle RT trafficking."; RL J. Biol. Chem. 277:30219-30226(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). CC -!- SUBUNIT: Interacts with BMX. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11506704}. CC -!- DEVELOPMENTAL STAGE: Expressed only at embryonic stages. Present at 12 CC dpc in primordial lung, cartilage and otic capsule (at protein level). CC {ECO:0000269|PubMed:11506704}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD32473.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF484555; AAM18673.1; -; mRNA. DR EMBL; AK173195; BAD32473.1; ALT_INIT; mRNA. DR CCDS; CCDS48582.1; -. DR RefSeq; NP_081701.2; NM_027425.3. DR AlphaFoldDB; Q8R4C2; -. DR SMR; Q8R4C2; -. DR BioGRID; 214046; 1. DR STRING; 10090.ENSMUSP00000113429; -. DR iPTMnet; Q8R4C2; -. DR PhosphoSitePlus; Q8R4C2; -. DR MaxQB; Q8R4C2; -. DR PaxDb; 10090-ENSMUSP00000113429; -. DR ProteomicsDB; 256808; -. DR Pumba; Q8R4C2; -. DR Antibodypedia; 45205; 93 antibodies from 20 providers. DR DNASU; 70432; -. DR Ensembl; ENSMUST00000119567.8; ENSMUSP00000113429.2; ENSMUSG00000020070.19. DR GeneID; 70432; -. DR KEGG; mmu:70432; -. DR UCSC; uc007fjn.1; mouse. DR AGR; MGI:1917682; -. DR CTD; 55680; -. DR MGI; MGI:1917682; Rufy2. DR VEuPathDB; HostDB:ENSMUSG00000020070; -. DR eggNOG; KOG4381; Eukaryota. DR GeneTree; ENSGT00940000155595; -. DR HOGENOM; CLU_014576_3_1_1; -. DR InParanoid; Q8R4C2; -. DR OMA; KNDMISR; -. DR OrthoDB; 5385125at2759; -. DR PhylomeDB; Q8R4C2; -. DR TreeFam; TF323904; -. DR BioGRID-ORCS; 70432; 0 hits in 77 CRISPR screens. DR ChiTaRS; Rufy2; mouse. DR PRO; PR:Q8R4C2; -. DR Proteomes; UP000000589; Chromosome 10. DR RNAct; Q8R4C2; Protein. DR Bgee; ENSMUSG00000020070; Expressed in rostral migratory stream and 225 other cell types or tissues. DR ExpressionAtlas; Q8R4C2; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI. DR CDD; cd15759; FYVE_RUFY2; 1. DR CDD; cd17695; RUN_RUFY2; 1. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.58.900; -; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR047333; FYVE_RUFY2. DR InterPro; IPR047335; RUFY1-3. DR InterPro; IPR004012; Run_dom. DR InterPro; IPR037213; Run_dom_sf. DR InterPro; IPR047332; RUN_RUFY2. DR InterPro; IPR000306; Znf_FYVE. DR InterPro; IPR017455; Znf_FYVE-rel. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR45956:SF3; RUN AND FYVE DOMAIN-CONTAINING PROTEIN 2; 1. DR PANTHER; PTHR45956; RUN AND FYVE DOMAIN-CONTAINING PROTEIN 2-LIKE PROTEIN; 1. DR Pfam; PF01363; FYVE; 1. DR Pfam; PF02759; RUN; 1. DR SMART; SM00064; FYVE; 1. DR SMART; SM00593; RUN; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF140741; RUN domain-like; 1. DR PROSITE; PS50826; RUN; 1. DR PROSITE; PS50178; ZF_FYVE; 1. DR Genevisible; Q8R4C2; MM. PE 1: Evidence at protein level; KW Coiled coil; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger. FT CHAIN 1..606 FT /note="RUN and FYVE domain-containing protein 2" FT /id="PRO_0000245831" FT DOMAIN 37..169 FT /note="RUN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178" FT ZN_FING 540..598 FT /note="FYVE-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT COILED 210..267 FT /evidence="ECO:0000255" FT COILED 294..515 FT /evidence="ECO:0000255" FT BINDING 546 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 549 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 562 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 565 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 570 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 573 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 590 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 593 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT CONFLICT 208 FT /note="Y -> C (in Ref. 2; AAM18673)" FT /evidence="ECO:0000305" FT CONFLICT 435 FT /note="I -> V (in Ref. 2; AAM18673)" FT /evidence="ECO:0000305" SQ SEQUENCE 606 AA; 70093 MW; 741EE7EA1E0A4EF2 CRC64; MATKDPTAVE RANLLNMAKL SIKGLIESAL SFGRTLDSDY PPLQQFFVVM EHCLKHGLKG RKSFLSYNKT IWGPLELVEK LYPEAEEIGA SVRDLPGLKT PLGRARAWLR LALMQKKMAD YLRCLIIQRE LLSEFYEYHA LMMEEEGAVI VGLLVGLNVI DANLCVKGED LDSQVGVIDF SMYLKNEEEI GNKERNVQIA AILDQKNYVE ELNRQLNSTV SSLHSRVDSL EKSNTKLIEE LAIAKNNIIK LQEENHQLRS ENELILMRTR QHLEVTKVDV ETELQTYKHS RQGLDEMYND ARRQLRDESQ LRQDVENELS VQVGMKHEME LAMKLLEKDI HEKQDTLIGL RQQLEEVKAI NIEMYQRLQG SEDGLKEKNE IIARLEEKTN KITTAMRQLE QRLQQAEKAQ KEAEAEDEKY AQECLSQSDS LQRQISQKEQ QLVQLETDLK IEKEWRQTLQ EDLQKEKDVL SHLRHETQKV ISLKKEFLNL QDENQQLKRI YQEQEQALQE LGSKLCESKL KIDDIKEANK ALQGLVWLKD KDATHCKLCE KEFSLSKRKH HCRNCGEIFC NACSDNELPL PSSPKPVRVC DSCHAMLIQR CSSNMP //