RSAD1_MOUSE
ID RSAD1_MOUSE Reviewed; 442 AA.
AC Q5SUV1; B2RTE1; Q6PHM8;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Radical S-adenosyl methionine domain-containing protein 1, mitochondrial;
DE AltName: Full=Putative heme chaperone;
DE Flags: Precursor;
GN Name=Rsad1;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: May be a heme chaperone, appears to bind heme. Homologous
CC bacterial proteins do not have oxygen-independent coproporphyrinogen-
CC III oxidase activity (By similarity). Binds 1 [4Fe-4S] cluster. The
CC cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-
CC L-methionine (By similarity). {ECO:0000250|UniProtKB:P32131,
CC ECO:0000250|UniProtKB:Q9HA92}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01266};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- MISCELLANEOUS: Might carry two S-adenosyl-L-methionine binding sites
CC with only one binding to the iron-sulfur cluster.
CC {ECO:0000250|UniProtKB:P32131}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. HemW subfamily. {ECO:0000305}.
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DR EMBL; AL645809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056485; AAH56485.1; -; mRNA.
DR EMBL; BC139274; AAI39275.1; -; mRNA.
DR EMBL; BC139276; AAI39277.1; -; mRNA.
DR CCDS; CCDS25258.1; -.
DR RefSeq; NP_001013399.1; NM_001013381.2.
DR RefSeq; XP_011247294.1; XM_011248992.2.
DR AlphaFoldDB; Q5SUV1; -.
DR SMR; Q5SUV1; -.
DR STRING; 10090.ENSMUSP00000037361; -.
DR PhosphoSitePlus; Q5SUV1; -.
DR EPD; Q5SUV1; -.
DR PaxDb; Q5SUV1; -.
DR PRIDE; Q5SUV1; -.
DR ProteomicsDB; 262737; -.
DR Antibodypedia; 18086; 134 antibodies from 23 providers.
DR DNASU; 237926; -.
DR Ensembl; ENSMUST00000040487; ENSMUSP00000037361; ENSMUSG00000039096.
DR GeneID; 237926; -.
DR KEGG; mmu:237926; -.
DR UCSC; uc007kza.2; mouse.
DR CTD; 55316; -.
DR MGI; MGI:3039628; Rsad1.
DR VEuPathDB; HostDB:ENSMUSG00000039096; -.
DR eggNOG; ENOG502QRH0; Eukaryota.
DR GeneTree; ENSGT00390000011216; -.
DR HOGENOM; CLU_027579_0_0_1; -.
DR InParanoid; Q5SUV1; -.
DR OMA; HIPWCVR; -.
DR OrthoDB; 1201842at2759; -.
DR PhylomeDB; Q5SUV1; -.
DR TreeFam; TF332416; -.
DR BioGRID-ORCS; 237926; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q5SUV1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SUV1; protein.
DR Bgee; ENSMUSG00000039096; Expressed in interventricular septum and 207 other tissues.
DR Genevisible; Q5SUV1; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR010723; HemN_C.
DR InterPro; IPR004559; HemW-like.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR13932; PTHR13932; 1.
DR Pfam; PF06969; HemN_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00562; HemN-like__clustered_with_heat; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00539; hemN_rel; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Chaperone; Heme; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Reference proteome; S-adenosyl-L-methionine; Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..442
FT /note="Radical S-adenosyl methionine domain-containing
FT protein 1, mitochondrial"
FT /id="PRO_0000284610"
FT DOMAIN 34..270
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 43
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 99..100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 158
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
SQ SEQUENCE 442 AA; 48665 MW; 999B006D092D7FA3 CRC64;
MVPSGVRTGR WVAAARAAQR RPRVDSLGQP PSPESASTRA ALYVHWPYCE KRCSYCNFNK
YIPRGVEEGT VRNCLVTEAR TLLRLSGVQR VESVFFGGGT PSLASPHTVA AVLEAVAQEV
YLPADSEVTL EANPTSAPGP RLAAFGAAGV NRLSIGLQSL DDAELQLLGR THSASDALRT
LAEARLLFPG RVSVDLMLGL PAQKVEPWLQ QLQKLLYHCD DHLSLYQLTL ERGTSLFAQV
QQGTLPAPDP DLAAEMYQEG RTVLRDAGFR QYEVSNFARN GALSTHNWTY WQCGQYLGIG
PGAHGRFVPQ GTGGHTREAR IQTLEPDNWM KEVTLFGHGT RKCVRLGKLE LLEEVLAMGL
RTDVGVTHQH WQQFEPQLTL WDVFGASKEV EELLAQGLLL LDYRGLRCSW EGLAVLDSLL
LTLLPQLQEA WQHRPSSPVS GG
