ID   LYAR_MOUSE              Reviewed;         388 AA.
AC   Q08288; Q9D9X2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   14-OCT-2015, entry version 109.
DE   RecName: Full=Cell growth-regulating nucleolar protein;
DE   AltName: Full=Protein expressed in male leptotene and zygotene spermatocytes 264;
DE            Short=MLZ-264;
GN   Name=Lyar;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=8491376; DOI=10.1101/gad.7.5.735;
RA   Su L., Hershberger R.J., Weissman I.L.;
RT   "LYAR, a novel nucleolar protein with zinc finger DNA-binding motifs,
RT   is involved in cell growth regulation.";
RL   Genes Dev. 7:735-748(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=20339383; DOI=10.1038/jhg.2010.26;
RA   Kogo H., Kowa-Sugiyama H., Yamada K., Bolor H., Tsutsumi M., Ohye T.,
RA   Inagaki H., Taniguchi M., Toda T., Kurahashi H.;
RT   "Screening of genes involved in chromosome segregation during meiosis
RT   I: toward the identification of genes responsible for infertility in
RT   humans.";
RL   J. Hum. Genet. 55:293-299(2010).
RN   [5]
RP   STRUCTURE BY NMR OF 1-66, AND ZINC-BINDING SITES.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the N-terminal zinc finger domain of cell
RT   growth regulating nucleolar protein Lyar.";
RL   Submitted (JAN-2006) to the PDB data bank.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000269|PubMed:8491376}.
CC   -!- TISSUE SPECIFICITY: Very high levels in immature spermatocytes in
CC       testis. Expressed in ovary. {ECO:0000269|PubMed:20339383}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in testis and ovary at E15.5.
CC       {ECO:0000269|PubMed:20339383}.
CC   -!- SIMILARITY: Contains 2 C2HC-type zinc fingers. {ECO:0000305}.
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DR   EMBL; S60885; AAB26644.1; -; mRNA.
DR   EMBL; AK006373; BAB24554.1; -; mRNA.
DR   CCDS; CCDS19253.1; -.
DR   PIR; A40683; A40683.
DR   RefSeq; NP_079557.2; NM_025281.3.
DR   RefSeq; XP_006503822.1; XM_006503759.1.
DR   RefSeq; XP_006503823.1; XM_006503760.1.
DR   RefSeq; XP_006503824.1; XM_006503761.1.
DR   RefSeq; XP_006503825.1; XM_006503762.1.
DR   RefSeq; XP_006503826.1; XM_006503763.1.
DR   RefSeq; XP_006503827.1; XM_006503764.1.
DR   UniGene; Mm.28560; -.
DR   PDB; 1WJV; NMR; -; A=1-66.
DR   PDBsum; 1WJV; -.
DR   ProteinModelPortal; Q08288; -.
DR   SMR; Q08288; 1-67.
DR   BioGrid; 201254; 1.
DR   IntAct; Q08288; 3.
DR   MINT; MINT-4127850; -.
DR   STRING; 10090.ENSMUSP00000084791; -.
DR   PhosphoSite; Q08288; -.
DR   MaxQB; Q08288; -.
DR   PaxDb; Q08288; -.
DR   PRIDE; Q08288; -.
DR   Ensembl; ENSMUST00000087514; ENSMUSP00000084791; ENSMUSG00000067367.
DR   Ensembl; ENSMUST00000114106; ENSMUSP00000109741; ENSMUSG00000067367.
DR   GeneID; 17089; -.
DR   KEGG; mmu:17089; -.
DR   UCSC; uc008xgh.2; mouse.
DR   CTD; 55646; -.
DR   MGI; MGI:107470; Lyar.
DR   eggNOG; NOG253936; -.
DR   GeneTree; ENSGT00390000003477; -.
DR   HOGENOM; HOG000006633; -.
DR   HOVERGEN; HBG006298; -.
DR   InParanoid; Q08288; -.
DR   KO; K15263; -.
DR   OMA; APDNEIT; -.
DR   OrthoDB; EOG7PP58C; -.
DR   PhylomeDB; Q08288; -.
DR   TreeFam; TF314925; -.
DR   ChiTaRS; Lyar; mouse.
DR   EvolutionaryTrace; Q08288; -.
DR   NextBio; 291232; -.
DR   PRO; PR:Q08288; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; Q08288; -.
DR   CleanEx; MM_LYAR; -.
DR   ExpressionAtlas; Q08288; baseline and differential.
DR   Genevisible; Q08288; MM.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044822; F:poly(A) RNA binding; ISO:MGI.
DR   InterPro; IPR014898; Znf_C2H2_LYAR.
DR   Pfam; PF08790; zf-LYAR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Complete proteome; Isopeptide bond;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    388       Cell growth-regulating nucleolar protein.
FT                                /FTId=PRO_0000084529.
FT   ZN_FING       6     25       C2HC-type 1.
FT   ZN_FING      33     51       C2HC-type 2.
FT   COILED      174    216       {ECO:0000255}.
FT   COMPBIAS    182    344       Lys-rich.
FT   METAL         6      6       Zinc 1.
FT   METAL         9      9       Zinc 1.
FT   METAL        21     21       Zinc 1.
FT   METAL        25     25       Zinc 1.
FT   METAL        33     33       Zinc 2.
FT   METAL        36     36       Zinc 2.
FT   METAL        48     48       Zinc 2.
FT   METAL        51     51       Zinc 2.
FT   CROSSLNK    204    204       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9NX58}.
FT   CONFLICT     21     21       H -> Q (in Ref. 1; AAB26644).
FT                                {ECO:0000305}.
FT   CONFLICT    109    109       R -> I (in Ref. 1; AAB26644).
FT                                {ECO:0000305}.
FT   CONFLICT    234    238       EAAEA -> DGADG (in Ref. 1; AAB26644).
FT                                {ECO:0000305}.
FT   CONFLICT    267    267       A -> R (in Ref. 1; AAB26644).
FT                                {ECO:0000305}.
FT   CONFLICT    354    354       N -> K (in Ref. 2; BAB24554).
FT                                {ECO:0000305}.
FT   CONFLICT    356    359       HHTS -> TSHH (in Ref. 1; AAB26644).
FT                                {ECO:0000305}.
FT   STRAND        3      9       {ECO:0000244|PDB:1WJV}.
FT   STRAND       12     14       {ECO:0000244|PDB:1WJV}.
FT   HELIX        17     24       {ECO:0000244|PDB:1WJV}.
FT   STRAND       30     33       {ECO:0000244|PDB:1WJV}.
FT   TURN         34     37       {ECO:0000244|PDB:1WJV}.
FT   STRAND       38     41       {ECO:0000244|PDB:1WJV}.
FT   HELIX        42     44       {ECO:0000244|PDB:1WJV}.
FT   TURN         45     47       {ECO:0000244|PDB:1WJV}.
SQ   SEQUENCE   388 AA;  43736 MW;  D39A0CDC2257BE8C CRC64;
     MVFFTCNACG ESVKKIQVEK HVSNCRNCEC LSCIDCGKDF WGDDYKSHVK CISEGQKYGG
     KGYEAKTHKG DAKQQAWIQK INELIKKPNV SPKVRELLQQ ISAFDNVPRK KAKFQNWMKN
     SLKVHSDSVL EQVWDIFSEA SSSEQDQQQP PSHTAKPHAE MPITKVPSAK TNGTTEEQTE
     AKKNKRERKE ERQKNRKKEK KELKLENHQE NLRGQKPKKR KKNQEAGHEA AGEEAAEASG
     PPEKKKAQGG QASEEGADRN GGPGEDAAEG QTKTAAGKRK RPKHSGAESG YKKKKMKLPE
     QPEEGEAKDH EAPSKGKFNW KGTIKAVLKQ APDNEISVKK LKKKVIAQYH AVMNDHHTSE
     EELLAIFNRK ISRNPTFKVL KDRVKLLK
//