RSAD1_HUMAN
ID RSAD1_HUMAN Reviewed; 442 AA.
AC Q9HA92; B4DMW0; Q53HV8; Q86VC4; Q9BRY7; Q9NUS7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Radical S-adenosyl methionine domain-containing protein 1, mitochondrial;
DE AltName: Full=Putative heme chaperone {ECO:0000303|PubMed:29282292};
DE Flags: Precursor;
GN Name=RSAD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Embryo, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS THR-119
RP AND SER-126.
RC TISSUE=Blood, and Colon;
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 [5]
RP PUTATIVE FUNCTION AS A HEME CHAPERONE, AND POSSIBLE HEME-BINDING.
RX PubMed=29282292; DOI=10.1074/jbc.ra117.000229;
RA Haskamp V., Karrie S., Mingers T., Barthels S., Alberge F., Magalon A.,
RA Mueller K., Bill E., Lubitz W., Kleeberg K., Schweyen P., Broering M.,
RA Jahn M., Jahn D.;
RT "The radical SAM protein HemW is a heme chaperone.";
RL J. Biol. Chem. 293:2558-2572(2018).
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 (Probable). Binds 1 [4Fe-4S] cluster. The cluster
CC is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC methionine (By similarity). {ECO:0000250|UniProtKB:P32131,
CC ECO:0000305|PubMed:29282292}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HA92-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HA92-2; Sequence=VSP_056130, VSP_056131, VSP_056132;
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; AK002026; BAA92043.1; -; mRNA.
DR EMBL; AK022105; BAB13962.1; -; mRNA.
DR EMBL; AK297655; BAG60022.1; -; mRNA.
DR EMBL; AK222472; BAD96192.1; -; mRNA.
DR EMBL; AC021491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005854; AAH05854.4; -; mRNA.
DR EMBL; BC050538; AAH50538.1; -; mRNA.
DR CCDS; CCDS11569.1; -. [Q9HA92-1]
DR RefSeq; NP_060816.1; NM_018346.2. [Q9HA92-1]
DR AlphaFoldDB; Q9HA92; -.
DR SMR; Q9HA92; -.
DR BioGRID; 120598; 81.
DR IntAct; Q9HA92; 9.
DR STRING; 9606.ENSP00000258955; -.
DR iPTMnet; Q9HA92; -.
DR PhosphoSitePlus; Q9HA92; -.
DR BioMuta; RSAD1; -.
DR DMDM; 145566941; -.
DR EPD; Q9HA92; -.
DR jPOST; Q9HA92; -.
DR MassIVE; Q9HA92; -.
DR MaxQB; Q9HA92; -.
DR PaxDb; Q9HA92; -.
DR PeptideAtlas; Q9HA92; -.
DR PRIDE; Q9HA92; -.
DR ProteomicsDB; 4646; -.
DR ProteomicsDB; 81387; -. [Q9HA92-1]
DR Antibodypedia; 18086; 134 antibodies from 23 providers.
DR DNASU; 55316; -.
DR Ensembl; ENST00000258955.7; ENSP00000258955.2; ENSG00000136444.10. [Q9HA92-1]
DR Ensembl; ENST00000515221.2; ENSP00000424558.2; ENSG00000136444.10. [Q9HA92-2]
DR GeneID; 55316; -.
DR KEGG; hsa:55316; -.
DR MANE-Select; ENST00000258955.7; ENSP00000258955.2; NM_018346.3; NP_060816.1.
DR UCSC; uc002iqw.2; human. [Q9HA92-1]
DR CTD; 55316; -.
DR DisGeNET; 55316; -.
DR GeneCards; RSAD1; -.
DR HGNC; HGNC:25634; RSAD1.
DR HPA; ENSG00000136444; Low tissue specificity.
DR neXtProt; NX_Q9HA92; -.
DR OpenTargets; ENSG00000136444; -.
DR PharmGKB; PA134945325; -.
DR VEuPathDB; HostDB:ENSG00000136444; -.
DR eggNOG; ENOG502QRH0; Eukaryota.
DR GeneTree; ENSGT00390000011216; -.
DR HOGENOM; CLU_027579_0_0_1; -.
DR InParanoid; Q9HA92; -.
DR OMA; HIPWCVR; -.
DR OrthoDB; 1201842at2759; -.
DR PhylomeDB; Q9HA92; -.
DR TreeFam; TF332416; -.
DR PathwayCommons; Q9HA92; -.
DR SignaLink; Q9HA92; -.
DR BioGRID-ORCS; 55316; 104 hits in 1083 CRISPR screens.
DR ChiTaRS; RSAD1; human.
DR GenomeRNAi; 55316; -.
DR Pharos; Q9HA92; Tdark.
DR PRO; PR:Q9HA92; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9HA92; protein.
DR Bgee; ENSG00000136444; Expressed in right hemisphere of cerebellum and 195 other tissues.
DR ExpressionAtlas; Q9HA92; baseline and differential.
DR Genevisible; Q9HA92; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
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 SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00539; hemN_rel; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Alternative splicing; Chaperone; Heme; Iron; Iron-sulfur;
KW Metal-binding; Mitochondrion; Reference proteome; S-adenosyl-L-methionine;
KW 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_0000284609"
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"
FT VAR_SEQ 46..158
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056130"
FT VAR_SEQ 282..307
FT /note="ALSTHNWTYWQCGQYLGVGPGAHGRF -> PMDDLCPRGLEATPGRLGSRHW
FT SLTT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056131"
FT VAR_SEQ 308..441
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056132"
FT VARIANT 119
FT /note="A -> T (in dbSNP:rs2290862)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031777"
FT VARIANT 126
FT /note="L -> S (in dbSNP:rs2290861)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031778"
FT VARIANT 354
FT /note="E -> Q (in dbSNP:rs9891176)"
FT /id="VAR_061126"
FT CONFLICT 186
FT /note="R -> G (in Ref. 1; BAB13962)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="Q -> R (in Ref. 2; BAD96192)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="Y -> C (in Ref. 1; BAB13962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 48714 MW; A450E02F3AE2D554 CRC64;
MALPGARARG WAAAARAAQR RRRVENAGGS PSPEPAGRRA ALYVHWPYCE KRCSYCNFNK
YIPRRLEEAA MQKCLVTEAQ TLLRLSGVQR VESVFFGGGT PSLASPHTVA AVLEAVAQAA
HLPADLEVTL EANPTSAPGS RLAEFGAAGV NRLSIGLQSL DDTELRLLGR THSACDALRT
LAEARRLFPG RVSVDLMLGL PAQQVGPWLG QLQELLHHCD DHLSLYQLSL ERGTALFAQV
QRGALPAPDP ELAAEMYQRG RAVLREAGFH QYEVSNFARN GALSTHNWTY WQCGQYLGVG
PGAHGRFMPQ GAGGHTREAR IQTLEPDNWM KEVMLFGHGT RKRVPLGRLE LLEEVLALGL
RTDVGITHQH WQQFEPQLTL WDVFGANKEV QELLERGLLQ LDHRGLRCSW EGLAVLDSLL
LTLLPQLQEA WQQRTPSPVP GG
