CAF17_HUMAN
ID CAF17_HUMAN Reviewed; 356 AA.
AC Q5T440;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Putative transferase CAF17, mitochondrial;
DE EC=2.1.-.-;
DE AltName: Full=Iron-sulfur cluster assembly factor homolog;
DE Flags: Precursor;
GN Name=IBA57; Synonyms=C1orf69;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=22323289; DOI=10.1091/mbc.e11-09-0772;
RA Sheftel A.D., Wilbrecht C., Stehling O., Niggemeyer B., Elsasser H.P.,
RA Muhlenhoff U., Lill R.;
RT "The human mitochondrial ISCA1, ISCA2, and IBA57 proteins are required for
RT [4Fe-4S] protein maturation.";
RL Mol. Biol. Cell 23:1157-1166(2012).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [5]
RP INVOLVEMENT IN SPG74.
RX PubMed=25609768; DOI=10.1212/wnl.0000000000001270;
RA Lossos A., Stuempfig C., Stevanin G., Gaussen M., Zimmerman B.E.,
RA Mundwiller E., Asulin M., Chamma L., Sheffer R., Misk A., Dotan S.,
RA Gomori J.M., Ponger P., Brice A., Lerer I., Meiner V., Lill R.;
RT "Fe/S protein assembly gene IBA57 mutation causes hereditary spastic
RT paraplegia.";
RL Neurology 84:659-667(2015).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [7]
RP VARIANT MMDS3 PRO-314, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23462291; DOI=10.1093/hmg/ddt107;
RA Ajit Bolar N., Vanlander A.V., Wilbrecht C., Van der Aa N., Smet J.,
RA De Paepe B., Vandeweyer G., Kooy F., Eyskens F., De Latter E., Delanghe G.,
RA Govaert P., Leroy J.G., Loeys B., Lill R., Van Laer L., Van Coster R.;
RT "Mutation of the iron-sulfur cluster assembly gene IBA57 causes severe
RT myopathy and encephalopathy.";
RL Hum. Mol. Genet. 22:2590-2602(2013).
CC -!- FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins
CC functioning late in the iron-sulfur cluster assembly pathway.
CC {ECO:0000269|PubMed:23462291}.
CC -!- INTERACTION:
CC Q5T440; Q86U28: ISCA2; NbExp=4; IntAct=EBI-10714899, EBI-10258659;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22323289,
CC ECO:0000269|PubMed:23462291}.
CC -!- TISSUE SPECIFICITY: Expressed in skin fibroblasts and skeletal muscle
CC (at protein level). {ECO:0000269|PubMed:23462291}.
CC -!- DISEASE: Multiple mitochondrial dysfunctions syndrome 3 (MMDS3)
CC [MIM:615330]: A severe disorder of systemic energy metabolism,
CC resulting in weakness, respiratory failure, lack of neurologic
CC development, lactic acidosis, hyperglycinemia and early death. Some
CC patients show failure to thrive, pulmonary hypertension, hypotonia and
CC irritability. Biochemical features include severe combined deficiency
CC of the 2-oxoacid dehydrogenases, defective lipoic acid synthesis and
CC reduction in activity of mitochondrial respiratory chain complexes.
CC {ECO:0000269|PubMed:23462291}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Spastic paraplegia 74, autosomal recessive (SPG74)
CC [MIM:616451]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body. SPG74 is characterized
CC by a combination of spastic paraplegia, optic atrophy, and peripheral
CC neuropathy with childhood-onset and slow progression into late
CC adulthood. {ECO:0000269|PubMed:25609768}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the GcvT family. CAF17 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL359510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS31046.1; -.
DR RefSeq; NP_001010867.1; NM_001010867.3.
DR PDB; 6GEU; X-ray; 1.55 A; A=43-356.
DR PDB; 6QE3; X-ray; 1.75 A; A=44-352.
DR PDB; 6QE4; X-ray; 2.30 A; A=31-356.
DR PDBsum; 6GEU; -.
DR PDBsum; 6QE3; -.
DR PDBsum; 6QE4; -.
DR AlphaFoldDB; Q5T440; -.
DR SASBDB; Q5T440; -.
DR SMR; Q5T440; -.
DR BioGRID; 128310; 81.
DR IntAct; Q5T440; 21.
DR MINT; Q5T440; -.
DR STRING; 9606.ENSP00000355672; -.
DR iPTMnet; Q5T440; -.
DR PhosphoSitePlus; Q5T440; -.
DR BioMuta; IBA57; -.
DR DMDM; 74744873; -.
DR EPD; Q5T440; -.
DR jPOST; Q5T440; -.
DR MassIVE; Q5T440; -.
DR MaxQB; Q5T440; -.
DR PaxDb; Q5T440; -.
DR PeptideAtlas; Q5T440; -.
DR PRIDE; Q5T440; -.
DR ProteomicsDB; 64428; -.
DR Antibodypedia; 52265; 78 antibodies from 13 providers.
DR DNASU; 200205; -.
DR Ensembl; ENST00000366711.4; ENSP00000355672.3; ENSG00000181873.13.
DR GeneID; 200205; -.
DR KEGG; hsa:200205; -.
DR MANE-Select; ENST00000366711.4; ENSP00000355672.3; NM_001010867.4; NP_001010867.1.
DR UCSC; uc001hsl.5; human.
DR CTD; 200205; -.
DR DisGeNET; 200205; -.
DR GeneCards; IBA57; -.
DR HGNC; HGNC:27302; IBA57.
DR HPA; ENSG00000181873; Low tissue specificity.
DR MalaCards; IBA57; -.
DR MIM; 615316; gene.
DR MIM; 615330; phenotype.
DR MIM; 616451; phenotype.
DR neXtProt; NX_Q5T440; -.
DR OpenTargets; ENSG00000181873; -.
DR Orphanet; 468661; Autosomal recessive spastic paraplegia type 74.
DR Orphanet; 363424; Multiple mitochondrial dysfunctions syndrome type 3.
DR PharmGKB; PA142672519; -.
DR VEuPathDB; HostDB:ENSG00000181873; -.
DR eggNOG; KOG2929; Eukaryota.
DR GeneTree; ENSGT00390000006465; -.
DR HOGENOM; CLU_007884_7_1_1; -.
DR InParanoid; Q5T440; -.
DR OMA; MDRLHGV; -.
DR OrthoDB; 1342242at2759; -.
DR PhylomeDB; Q5T440; -.
DR TreeFam; TF105983; -.
DR PathwayCommons; Q5T440; -.
DR SignaLink; Q5T440; -.
DR BioGRID-ORCS; 200205; 151 hits in 1077 CRISPR screens.
DR ChiTaRS; IBA57; human.
DR GenomeRNAi; 200205; -.
DR Pharos; Q5T440; Tbio.
DR PRO; PR:Q5T440; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5T440; protein.
DR Bgee; ENSG00000181873; Expressed in pancreatic ductal cell and 169 other tissues.
DR Genevisible; Q5T440; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR Gene3D; 3.30.1360.120; -; 1.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR InterPro; IPR045179; YgfZ/GcvT.
DR InterPro; IPR017703; YgfZ/GcvT_CS.
DR PANTHER; PTHR22602; PTHR22602; 1.
DR TIGRFAMs; TIGR03317; ygfZ_signature; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; Heme biosynthesis;
KW Hereditary spastic paraplegia; Mitochondrion; Neurodegeneration;
KW Primary mitochondrial disease; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..356
FT /note="Putative transferase CAF17, mitochondrial"
FT /id="PRO_0000278633"
FT MOD_RES 309
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CAK1"
FT MOD_RES 309
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CAK1"
FT VARIANT 211
FT /note="G -> S (in dbSNP:rs2298014)"
FT /id="VAR_030794"
FT VARIANT 314
FT /note="Q -> P (in MMDS3; loss of stability and consequently
FT decrease in various mitochondrial 4Fe-4S proteins and in
FT proteins covalently linked to lipoic acid;
FT dbSNP:rs587777016)"
FT /evidence="ECO:0000269|PubMed:23462291"
FT /id="VAR_069821"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:6GEU"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 106..129
FT /evidence="ECO:0007829|PDB:6GEU"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6GEU"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:6GEU"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:6QE3"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:6GEU"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:6GEU"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:6GEU"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:6GEU"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:6GEU"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:6GEU"
FT TURN 242..246
FT /evidence="ECO:0007829|PDB:6GEU"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:6GEU"
FT HELIX 263..272
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 276..284
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 306..314
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:6GEU"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:6GEU"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:6QE4"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:6GEU"
SQ SEQUENCE 356 AA; 38155 MW; 199A04DAB6840807 CRC64;
MATAALLRGA TPGRGGPVWR WRLRAAPRCR LAHSSCSPGG DPTAGAAWAC FRLDGRTLLR
VRGPDAAPFL LGLLTNELPL PSPAAAGAPP AARAGYAHFL NVQGRTLYDV ILYGLQEHSE
VSGFLLECDS SVQGALQKHL ALYRIRRKVT VEPHPELRVW AVLPSSPEAC GAASLQERAG
AAAILIRDPR TARMGWRLLT QDEGPALVPG GRLGDLWDYH QHRYLQGVPE GVRDLPPGVA
LPLESNLAFM NGVSFTKGCY IGQELTARTH HMGVIRKRLF PVRFLDPLPT SGITPGATVL
TASGQTVGKF RAGQGNVGLA LLWSEKIKGP LHIRASEGAQ VALAASVPDW WPTVSK
