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NOA1_MOUSE
ID   NOA1_MOUSE              Reviewed;         693 AA.
AC   Q9JJG9; Q3T996; Q3U044; Q99JU4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Nitric oxide-associated protein 1;
GN   Name=Noa1; ORFNames=MNCb-4931;
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 MRNA].
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.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
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].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16380119; DOI=10.1016/j.febslet.2005.12.038;
RA   Zemojtel T., Kolanczyk M., Kossler N., Stricker S., Lurz R., Mikula I.,
RA   Duchniewicz M., Schuelke M., Ghafourifar P., Martasek P., Vingron M.,
RA   Mundlos S.;
RT   "Mammalian mitochondrial nitric oxide synthase: characterization of a novel
RT   candidate.";
RL   FEBS Lett. 580:455-462(2006).
RN   [5]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-353.
RX   PubMed=18456285; DOI=10.1016/j.lfs.2008.03.019;
RA   Parihar A., Parihar M.S., Chen Z., Ghafourifar P.;
RT   "mAtNOS1 induces apoptosis of human mammary adenocarcinoma cells.";
RL   Life Sci. 82:1077-1082(2008).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21118999; DOI=10.1091/mbc.e10-07-0643;
RA   Kolanczyk M., Pech M., Zemojtel T., Yamamoto H., Mikula I., Calvaruso M.A.,
RA   van den Brand M., Richter R., Fischer B., Ritz A., Kossler N., Thurisch B.,
RA   Spoerle R., Smeitink J., Kornak U., Chan D., Vingron M., Martasek P.,
RA   Lightowlers R.N., Nijtmans L., Schuelke M., Nierhaus K.H., Mundlos S.;
RT   "NOA1 is an essential GTPase required for mitochondrial protein
RT   synthesis.";
RL   Mol. Biol. Cell 22:1-11(2011).
CC   -!- FUNCTION: Involved in regulation of mitochondrial protein translation
CC       and respiration. Plays a role in mitochondria-mediated cell death. May
CC       act as a scaffolding protein or stabilizer of respiratory chain
CC       supercomplexes. Binds GTP. {ECO:0000269|PubMed:18456285,
CC       ECO:0000269|PubMed:21118999}.
CC   -!- SUBUNIT: Homodimer or multimer. Interacts with mitochondrial complex I,
CC       DAP3, MRPL12 and MRPS27. {ECO:0000269|PubMed:18456285}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:16380119, ECO:0000269|PubMed:18456285}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:16380119,
CC       ECO:0000269|PubMed:18456285}; Matrix side {ECO:0000269|PubMed:16380119,
CC       ECO:0000269|PubMed:18456285}.
CC   -!- TISSUE SPECIFICITY: Expressed in tissues associated with high
CC       mitochondria content including testes, heart, liver, brain and thymus.
CC       Also expressed in various bone cell lines.
CC       {ECO:0000269|PubMed:16380119}.
CC   -!- DEVELOPMENTAL STAGE: At 10.5 dpc, weak but widespread expression. By
CC       12.5 dpc prominently expressed in the liver and also detected in
CC       developing CNS and dorsal root ganglia. At 14.5 dpc, expression is
CC       intensified in bone. {ECO:0000269|PubMed:16380119}.
CC   -!- DISRUPTION PHENOTYPE: Mice display mid-gestation lethality associated
CC       with a severe developmental defect of the embryo and trophoblast.
CC       Primary embryonic fibroblasts isolated from mutant 9.5 dpc embryos show
CC       deficient mitochondrial synthesis and a global defect of oxidative
CC       phosphorylation. {ECO:0000269|PubMed:21118999}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. NOA1
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR   EMBL; AB041537; BAA95022.1; -; mRNA.
DR   EMBL; AK017793; BAB30935.1; -; mRNA.
DR   EMBL; AK157246; BAE34011.1; -; mRNA.
DR   EMBL; AK172681; BAE43128.1; -; mRNA.
DR   EMBL; BC005689; AAH05689.1; -; mRNA.
DR   EMBL; BC017154; AAH17154.1; -; mRNA.
DR   CCDS; CCDS19373.1; -.
DR   RefSeq; NP_062810.1; NM_019836.3.
DR   AlphaFoldDB; Q9JJG9; -.
DR   SMR; Q9JJG9; -.
DR   BioGRID; 207962; 3.
DR   STRING; 10090.ENSMUSP00000045948; -.
DR   iPTMnet; Q9JJG9; -.
DR   PhosphoSitePlus; Q9JJG9; -.
DR   EPD; Q9JJG9; -.
DR   jPOST; Q9JJG9; -.
DR   MaxQB; Q9JJG9; -.
DR   PaxDb; Q9JJG9; -.
DR   PeptideAtlas; Q9JJG9; -.
DR   PRIDE; Q9JJG9; -.
DR   ProteomicsDB; 252914; -.
DR   Antibodypedia; 44140; 127 antibodies from 24 providers.
DR   Ensembl; ENSMUST00000047860; ENSMUSP00000045948; ENSMUSG00000036285.
DR   GeneID; 56412; -.
DR   KEGG; mmu:56412; -.
DR   UCSC; uc008xwc.2; mouse.
DR   CTD; 84273; -.
DR   MGI; MGI:1914306; Noa1.
DR   VEuPathDB; HostDB:ENSMUSG00000036285; -.
DR   eggNOG; KOG1249; Eukaryota.
DR   GeneTree; ENSGT00390000001695; -.
DR   HOGENOM; CLU_014195_2_0_1; -.
DR   InParanoid; Q9JJG9; -.
DR   OMA; LLNSDYC; -.
DR   OrthoDB; 612803at2759; -.
DR   PhylomeDB; Q9JJG9; -.
DR   TreeFam; TF314460; -.
DR   BioGRID-ORCS; 56412; 12 hits in 72 CRISPR screens.
DR   ChiTaRS; Noa1; mouse.
DR   PRO; PR:Q9JJG9; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9JJG9; protein.
DR   Bgee; ENSMUSG00000036285; Expressed in ankle joint and 281 other tissues.
DR   Genevisible; Q9JJG9; MM.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISO:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0032543; P:mitochondrial translation; IMP:UniProtKB.
DR   GO; GO:0010941; P:regulation of cell death; IDA:UniProtKB.
DR   GO; GO:0043457; P:regulation of cellular respiration; IMP:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; GTP-binding; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..693
FT                   /note="Nitric oxide-associated protein 1"
FT                   /id="PRO_0000232511"
FT   DOMAIN          203..504
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   REGION          43..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         76
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC60"
FT   MUTAGEN         353
FT                   /note="K->R: Loss of ability to regulate activity of
FT                   mitochondrial respiratory chain complexes."
FT                   /evidence="ECO:0000269|PubMed:18456285"
FT   CONFLICT        8
FT                   /note="C -> R (in Ref. 2; BAE43128)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        259
FT                   /note="P -> T (in Ref. 2; BAE43128)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        563
FT                   /note="N -> S (in Ref. 2; BAE34011)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   693 AA;  77379 MW;  946AB1752263903C CRC64;
     MLPARLACGL LCGLRRGPAP AAACYGPARW LLEGKCEVPI RQRASSLGRR VPPSSTATED
     YAEGPDTEER FLFPEYVPER TPEEQVRELQ ELRELQQLQQ EKERERLQQR EERLQQKLRA
     GFRTLPVPEF PDASVPPSGI YCSGCGAELH CQHPGLPGYL PEEKFRDAAQ AEGGPARTVC
     QRCWLLVHHG RALRLQVSRD QYLELVSAAL RRPGPALVLY MVNLLDLPDA LLPDLPKLVG
     PKQLIVLGNK VDLLPQDAPG YLKRLRKRLW DDCIRAGLVV APGHQGPQYP AGDEPLEEIK
     NQNPSSRSRT VVKDVRLISA KTGYGVEEMI SALQRSWRYR GDVYLVGTTN AGKSTLFNTL
     LESDYCTAKG SEAIDRATIS PWPGTTLNLL KFPICNPTPY RMFKRQRRLQ EDATKAEEDL
     SEEEQSQLNQ LKKHGYIVGR VGRTFSYSRE QDEVPFEFDA DSLAFDMGSE PVVSVCKSTK
     QIELTPEDVK DAHWFYDTPG ITKESCILNL LTEKEINTVL PTHSIIPRTF VLKPGMVLFL
     GGIARIDFLQ GNQSAWFTVV ASNFLPVHIT SLDKADALYE KHAGHELLLV PMGGKERMAQ
     FPPLVAEDIT LKGGGKFEAV ADIKFSSAGW VAVTPYSEGT LHLRGHTPEG TALTVHPPVL
     PYIVNVKGQR MKKSVAYKTK KPPSLVHNLK KHR
 
 
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