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NFU1_MOUSE
ID   NFU1_MOUSE              Reviewed;         255 AA.
AC   Q9QZ23; Q3ULE0; Q6VNZ7; Q8CF80; Q9D1B7;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=NFU1 iron-sulfur cluster scaffold homolog, mitochondrial;
DE   AltName: Full=HIRA-interacting protein 5;
DE            Short=mHIRIP5;
DE   Flags: Precursor;
GN   Name=Nfu1; Synonyms=Hirip5;
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=Blastocyst, Kidney, and 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., 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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-255.
RX   PubMed=11342215; DOI=10.1016/s0167-4781(00)00300-6;
RA   Lorain S., Lecluse Y., Scamps C., Mattei M.-G., Lipinski M.;
RT   "Identification of human and mouse HIRA-interacting protein-5 (HIRIP5), two
RT   mammalian representatives in a family of phylogenetically conserved
RT   proteins with a role in the biogenesis of Fe/S proteins.";
RL   Biochim. Biophys. Acta 1517:376-383(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-255.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 11-255.
RC   STRAIN=ICR; TISSUE=Brain;
RX   PubMed=12915448; DOI=10.1093/hmg/ddg253;
RA   Ganesh S., Tsurutani N., Suzuki T., Ueda K., Agarwala K.L., Osada H.,
RA   Delgado-Escueta A.V., Yamakawa K.;
RT   "The Lafora disease gene product laforin interacts with HIRIP5, a
RT   phylogenetically conserved protein containing a NifU-like domain.";
RL   Hum. Mol. Genet. 12:2359-2368(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   STRUCTURE BY NMR OF 162-241.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RSGI RUH-018, a NIFU-like domain of HIRIP5 protein
RT   from mouse.";
RL   Submitted (SEP-2004) to the PDB data bank.
CC   -!- FUNCTION: Iron-sulfur cluster scaffold protein which can assemble [4Fe-
CC       4S] clusters and deliver them to target proteins.
CC       {ECO:0000250|UniProtKB:Q9UMS0}.
CC   -!- SUBUNIT: Monomer and homohexamer; the apo-NFU1 is a monomer, while the
CC       holo-NFU1 is a hexamer composed of a trimer of dimer that is probably
CC       linked by some 4Fe-4S cluster. Interacts with HIRA and EPM2A/laforin.
CC       Interacts with BOLA3. Interacts with HSPA9.
CC       {ECO:0000250|UniProtKB:Q9UMS0}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Cytoplasm, cytosol
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH18355.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC24985.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB57314.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK002244; BAC24985.1; ALT_FRAME; mRNA.
DR   EMBL; AK003730; BAB22965.1; -; mRNA.
DR   EMBL; AK145558; BAE26508.1; -; mRNA.
DR   EMBL; AJ132616; CAB57314.1; ALT_FRAME; mRNA.
DR   EMBL; BC018355; AAH18355.1; ALT_INIT; mRNA.
DR   EMBL; AY335195; AAQ73785.1; -; mRNA.
DR   CCDS; CCDS85088.1; -.
DR   RefSeq; NP_001164062.1; NM_001170591.1.
DR   RefSeq; NP_064429.2; NM_020045.3.
DR   RefSeq; XP_006506482.1; XM_006506419.1.
DR   RefSeq; XP_006506483.1; XM_006506420.1.
DR   PDB; 1VEH; NMR; -; A=163-241.
DR   PDBsum; 1VEH; -.
DR   AlphaFoldDB; Q9QZ23; -.
DR   BMRB; Q9QZ23; -.
DR   SMR; Q9QZ23; -.
DR   BioGRID; 208161; 2.
DR   IntAct; Q9QZ23; 1.
DR   STRING; 10090.ENSMUSP00000032060; -.
DR   PhosphoSitePlus; Q9QZ23; -.
DR   SwissPalm; Q9QZ23; -.
DR   EPD; Q9QZ23; -.
DR   jPOST; Q9QZ23; -.
DR   MaxQB; Q9QZ23; -.
DR   PaxDb; Q9QZ23; -.
DR   PeptideAtlas; Q9QZ23; -.
DR   PRIDE; Q9QZ23; -.
DR   ProteomicsDB; 252886; -.
DR   Antibodypedia; 48139; 46 antibodies from 18 providers.
DR   DNASU; 56748; -.
DR   Ensembl; ENSMUST00000117583; ENSMUSP00000113332; ENSMUSG00000029993.
DR   GeneID; 56748; -.
DR   KEGG; mmu:56748; -.
DR   UCSC; uc009csv.2; mouse.
DR   CTD; 27247; -.
DR   MGI; MGI:1913290; Nfu1.
DR   VEuPathDB; HostDB:ENSMUSG00000029993; -.
DR   eggNOG; KOG2358; Eukaryota.
DR   GeneTree; ENSGT00390000011296; -.
DR   InParanoid; Q9QZ23; -.
DR   OrthoDB; 1016782at2759; -.
DR   PhylomeDB; Q9QZ23; -.
DR   TreeFam; TF315076; -.
DR   BioGRID-ORCS; 56748; 4 hits in 72 CRISPR screens.
DR   ChiTaRS; Nfu1; mouse.
DR   EvolutionaryTrace; Q9QZ23; -.
DR   PRO; PR:Q9QZ23; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9QZ23; protein.
DR   Bgee; ENSMUSG00000029993; Expressed in embryonic brain and 252 other tissues.
DR   ExpressionAtlas; Q9QZ23; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR   GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central.
DR   Gene3D; 3.30.1370.70; -; 1.
DR   Gene3D; 3.30.300.130; -; 1.
DR   InterPro; IPR034904; FSCA_dom_sf.
DR   InterPro; IPR014824; Nfu/NifU_N.
DR   InterPro; IPR036498; Nfu/NifU_N_sf.
DR   InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
DR   Pfam; PF08712; Nfu_N; 1.
DR   Pfam; PF01106; NifU; 1.
DR   SMART; SM00932; Nfu_N; 1.
DR   SUPFAM; SSF110836; SSF110836; 1.
DR   SUPFAM; SSF117916; SSF117916; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..255
FT                   /note="NFU1 iron-sulfur cluster scaffold homolog,
FT                   mitochondrial"
FT                   /id="PRO_0000166192"
FT   REGION          173..241
FT                   /note="NifU"
FT   BINDING         210
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UMS0"
FT   BINDING         213
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UMS0"
FT   CONFLICT        11..12
FT                   /note="AV -> TS (in Ref. 4; AAQ73785)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        19
FT                   /note="R -> K (in Ref. 2; CAB57314)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="V -> A (in Ref. 2; CAB57314, 3; AAH18355 and 4;
FT                   AAQ73785)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        48
FT                   /note="A -> H (in Ref. 2; CAB57314)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="S -> SS (in Ref. 1; BAC24985/BAE26508)"
FT                   /evidence="ECO:0000305"
FT   HELIX           168..179
FT                   /evidence="ECO:0007829|PDB:1VEH"
FT   HELIX           182..188
FT                   /evidence="ECO:0007829|PDB:1VEH"
FT   STRAND          194..198
FT                   /evidence="ECO:0007829|PDB:1VEH"
FT   STRAND          201..204
FT                   /evidence="ECO:0007829|PDB:1VEH"
FT   HELIX           214..219
FT                   /evidence="ECO:0007829|PDB:1VEH"
FT   HELIX           221..231
FT                   /evidence="ECO:0007829|PDB:1VEH"
FT   STRAND          238..240
FT                   /evidence="ECO:0007829|PDB:1VEH"
SQ   SEQUENCE   255 AA;  28568 MW;  E7DA6A0333E2EB5E CRC64;
     MAAAERAWGA AVGVVRLCRR FCHVATPHTF KKQPLHQYVR RPLFPLRAPL CNTVRFMFIQ
     TQDTPNPNSL KFIPGKPVLE TRTMDFPTPA AAFRSPLARQ LFRIEGVKSV FFGPDFITVT
     KENEELDWNL LKPDIYATIM DFFASGLPLV TEETPPPPGE AGSEEDDEVV AMIKELLDTR
     IRPTVQEDGG DVIYRGFEDG IVRLKLQGSC TSCPSSIITL KSGIQNMLQF YIPEVEGVEQ
     VMDDDESDEK EANSS
 
 
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