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NMAT4_ARATH
ID   NMAT4_ARATH             Reviewed;         798 AA.
AC   Q9CA78;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Nuclear intron maturase 4, mitochondrial {ECO:0000303|PubMed:19946041};
DE            Short=AtnMat4 {ECO:0000303|PubMed:19946041};
DE            EC=3.1.-.-;
DE   AltName: Full=Nuclear intron maturase 2 b {ECO:0000303|PubMed:12527773};
DE            Short=AtnMat2b {ECO:0000303|PubMed:12527773};
DE   Flags: Precursor;
GN   Name=NMAT4 {ECO:0000303|PubMed:19946041};
GN   Synonyms=NMAT2B {ECO:0000303|PubMed:12527773};
GN   OrderedLocusNames=At1g74350 {ECO:0000312|Araport:AT1G74350};
GN   ORFNames=F1M20.3 {ECO:0000312|EMBL:AAG52355.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY.
RX   PubMed=12527773; DOI=10.1093/nar/gkg153;
RA   Mohr G., Lambowitz A.M.;
RT   "Putative proteins related to group II intron reverse
RT   transcriptase/maturases are encoded by nuclear genes in higher plants.";
RL   Nucleic Acids Res. 31:647-652(2003).
RN   [4]
RP   SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19946041; DOI=10.1261/rna.1776409;
RA   Keren I., Bezawork-Geleta A., Kolton M., Maayan I., Belausov E., Levy M.,
RA   Mett A., Gidoni D., Shaya F., Ostersetzer-Biran O.;
RT   "AtnMat2, a nuclear-encoded maturase required for splicing of group-II
RT   introns in Arabidopsis mitochondria.";
RL   RNA 15:2299-2311(2009).
RN   [5]
RP   REVIEW ON SPLICING FACTORS.
RC   STRAIN=cv. Columbia;
RX   PubMed=24600456; DOI=10.3389/fpls.2014.00035;
RA   Brown G.G., Colas des Francs-Small C., Ostersetzer-Biran O.;
RT   "Group II intron splicing factors in plant mitochondria.";
RL   Front. Plant Sci. 5:35-35(2014).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, ALTERNATIVE SPLICING, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=24506473; DOI=10.1111/tpj.12466;
RA   Cohen S., Zmudjak M., Colas des Francs-Small C., Malik S., Shaya F.,
RA   Keren I., Belausov E., Many Y., Brown G.G., Small I., Ostersetzer-Biran O.;
RT   "nMAT4, a maturase factor required for nad1 pre-mRNA processing and
RT   maturation, is essential for holocomplex I biogenesis in Arabidopsis
RT   mitochondria.";
RL   Plant J. 78:253-268(2014).
CC   -!- FUNCTION: Nuclear-encoded maturase required for splicing of group-II
CC       introns in mitochondria. Involved in NAD1 pre-mRNA processing and
CC       maturation of introns 1, 3 and 4. Necessary for mitochondrial
CC       biogenesis during early developmental stages. Essential for respiratory
CC       holocomplex I biogenesis in mitochondria.
CC       {ECO:0000269|PubMed:24506473}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC       {ECO:0000269|PubMed:19946041, ECO:0000269|PubMed:24506473}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Plastid, chloroplast
CC       {ECO:0000269|PubMed:19946041, ECO:0000269|PubMed:24506473}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1; Synonyms=long {ECO:0000303|PubMed:19946041}, nMAT4L
CC       {ECO:0000303|PubMed:24506473};
CC         IsoId=Q9CA78-1; Sequence=Displayed;
CC       Name=2; Synonyms=short {ECO:0000303|PubMed:19946041}, nMAT4S
CC       {ECO:0000303|PubMed:24506473};
CC         IsoId=Q9CA78-2; Sequence=VSP_058948;
CC   -!- DISRUPTION PHENOTYPE: Altered mitochondrial morphology. Impaired seed
CC       germination (e.g. many dark and wrinkled seeds in siliques), seedling
CC       establishment and development (e.g. abnormal primary root elongation
CC       and vegetative growth). Defects in the processing and maturation of
CC       various mitochondrial NAD1 introns. Modified respiration phenotypes
CC       associated with complex I defects. Seed-specific deficiency in the
CC       regulation of carbohydrate metabolism. Small plants requiring sucrose-
CC       supplemented medium to survive. {ECO:0000269|PubMed:24506473}.
CC   -!- SIMILARITY: Belongs to the plant nuclear intron maturase (nMat) family.
CC       {ECO:0000305}.
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DR   EMBL; AC011765; AAG52355.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35581.1; -; Genomic_DNA.
DR   PIR; B96772; B96772.
DR   RefSeq; NP_177575.1; NM_106095.2.
DR   AlphaFoldDB; Q9CA78; -.
DR   STRING; 3702.AT1G74350.1; -.
DR   PaxDb; Q9CA78; -.
DR   PeptideAtlas; Q9CA78; -.
DR   PRIDE; Q9CA78; -.
DR   ProteomicsDB; 251066; -. [Q9CA78-1]
DR   EnsemblPlants; AT1G74350.1; AT1G74350.1; AT1G74350.
DR   GeneID; 843776; -.
DR   Gramene; AT1G74350.1; AT1G74350.1; AT1G74350.
DR   KEGG; ath:AT1G74350; -.
DR   Araport; AT1G74350; -.
DR   TAIR; locus:2019140; AT1G74350.
DR   eggNOG; KOG1075; Eukaryota.
DR   HOGENOM; CLU_013547_0_0_1; -.
DR   InParanoid; Q9CA78; -.
DR   OrthoDB; 274919at2759; -.
DR   PhylomeDB; Q9CA78; -.
DR   PRO; PR:Q9CA78; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9CA78; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0000373; P:Group II intron splicing; IMP:UniProtKB.
DR   GO; GO:0006315; P:homing of group II introns; IBA:GO_Central.
DR   GO; GO:0090615; P:mitochondrial mRNA processing; IMP:UniProtKB.
DR   GO; GO:1900864; P:mitochondrial RNA modification; IMP:TAIR.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR   GO; GO:0032885; P:regulation of polysaccharide biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0009845; P:seed germination; IMP:TAIR.
DR   GO; GO:0090351; P:seedling development; IMP:TAIR.
DR   InterPro; IPR024937; Domain_X.
DR   InterPro; IPR000477; RT_dom.
DR   Pfam; PF01348; Intron_maturas2; 1.
DR   Pfam; PF00078; RVT_1; 1.
PE   3: Inferred from homology;
KW   Alternative initiation; Chloroplast; DNA-binding; Endonuclease; Hydrolase;
KW   Intron homing; Metal-binding; Mitochondrion; Nuclease; Plastid;
KW   Reference proteome; Transit peptide; Zinc; Zinc-finger.
FT   TRANSIT         1..16
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..798
FT                   /note="Nuclear intron maturase 4, mitochondrial"
FT                   /id="PRO_0000440122"
FT   ZN_FING         729..778
FT                   /note="THAP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT   REGION          578..665
FT                   /note="Intron maturase type-2"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         46..90
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_058948"
SQ   SEQUENCE   798 AA;  90268 MW;  EE646E421744A0D5 CRC64;
     MFRKRNLVLD LLRRCYIETL IPRGLWSRTI STFPKSALLA TDNAEMASKE TGMFSLAGEL
     ASLVEESSSH VDDDSKPRSR MELKRSLELR LKKRVKEQCI NGKFSDLLKK VIARPETLRD
     AYDCIRLNSN VSITERNGSV AFDSIAEELS SGVFDVASNT FSIVARDKTK EVLVLPSVAL
     KVVQEAIRIV LEVVFSPHFS KISHSCRSGR GRASALKYIN NNISRSDWCF TLSLNKKLDV
     SVFENLLSVM EEKVEDSSLS ILLRSMFEAR VLNLEFGGFP KGHGLPQEGV LSRVLMNIYL
     DRFDHEFYRI SMRHEALGLD SKTDEDSPGS KLRSWFRRQA GEQGLKSTTE QDVALRVYCC
     RFMDEIYFSV SGPKKVASDI RSEAIGFLRN SLHLDITDET DPSPCEATSG LRVLGTLVRK
     NVRESPTVKA VHKLKEKVRL FALQKEEAWT LGTVRIGKKW LGHGLKKVKE SEIKGLADSN
     STLSQISCHR KAGMETDHWY KILLRIWMED VLRTSADRSE EFVLSKHVVE PTVPQELRDA
     FYKFQNAAAA YVSSETANLE ALLPCPQSHD RPVFFGDVVA PTNAIGRRLY RYGLITAKGY
     ARSNSMLILL DTAQIIDWYS GLVRRWVIWY EGCSNFDEIK ALIDNQIRMS CIRTLAAKYR
     IHENEIEKRL DLELSTIPSA EDIEQEIQHE KLDSPAFDRD EHLTYGLSNS GLCLLSLARL
     VSESRPCNCF VIGCSMAAPA VYTLHAMERQ KFPGWKTGFS VCIPSSLNGR RIGLCKQHLK
     DLYIGQISLQ AVDFGAWR
 
 
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