SUCHY_HUMAN
ID SUCHY_HUMAN Reviewed; 445 AA.
AC Q9HAC7; A4D1W5; B4DR73; Q4KMW4; Q4KMW8; Q4KMZ0; Q8TE00; Q8TEY1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Succinate--hydroxymethylglutarate CoA-transferase;
DE EC=2.8.3.13;
DE AltName: Full=Dermal papilla-derived protein 13;
DE AltName: Full=SuccinylCoA:glutarate-CoA transferase;
DE Flags: Precursor;
GN Name=SUGCT; Synonyms=C7orf10, DERP13;
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).
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-78, AND TISSUE SPECIFICITY.
RX PubMed=11829489; DOI=10.1006/geno.2002.6695;
RA Nakabayashi K., Fernandez B.A., Teshima I., Shuman C., Proud V.K.,
RA Curry C.J., Chitayat D., Grebe T., Ming J., Oshimura M., Meguro M.,
RA Mitsuya K., Deb-Rinker P., Herbrick J.A., Weksberg R., Scherer S.W.;
RT "Molecular genetic studies of human chromosome 7 in Russell-Silver
RT syndrome.";
RL Genomics 79:186-196(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-445 (ISOFORM 1).
RC TISSUE=Hair follicle dermal papilla;
RA Ikeda A., Yamashita M., Yoshimoto M.;
RT "Molecular cloning of a dermal papiila derived gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF
RP VARIANT GA3 TRP-336.
RX PubMed=23893049; DOI=10.1007/s10545-013-9632-0;
RA Marlaire S., Van Schaftingen E., Veiga-da-Cunha M.;
RT "C7orf10 encodes succinate-hydroxymethylglutarate CoA-transferase, the
RT enzyme that converts glutarate to glutaryl-CoA.";
RL J. Inherit. Metab. Dis. 37:13-19(2014).
RN [9]
RP VARIANT GA3 TRP-336.
RX PubMed=18926513; DOI=10.1016/j.ajhg.2008.09.018;
RA Sherman E.A., Strauss K.A., Tortorelli S., Bennett M.J., Knerr I.,
RA Morton D.H., Puffenberger E.G.;
RT "Genetic mapping of glutaric aciduria, type 3, to chromosome 7 and
RT identification of mutations in C7orf10.";
RL Am. J. Hum. Genet. 83:604-609(2008).
CC -!- FUNCTION: Catalyzes the succinyl-CoA-dependent conversion of glutarate
CC to glutaryl-CoA. Can use different dicarboxylic acids as CoA acceptors,
CC the preferred ones are glutarate, succinate, adipate, and 3-
CC hydroxymethylglutarate. {ECO:0000269|PubMed:23893049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-3-methylglutarate + succinyl-CoA = (3S)-hydroxy-3-
CC methylglutaryl-CoA + succinate; Xref=Rhea:RHEA:12284,
CC ChEBI:CHEBI:17325, ChEBI:CHEBI:30031, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57292; EC=2.8.3.13;
CC Evidence={ECO:0000269|PubMed:23893049};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23893049}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9HAC7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HAC7-2; Sequence=VSP_014721, VSP_014722;
CC Name=3;
CC IsoId=Q9HAC7-3; Sequence=VSP_014722;
CC Name=4;
CC IsoId=Q9HAC7-4; Sequence=VSP_043291;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney. Intermediate expression
CC in liver, skeletal muscle and pancreas. Little to no expression
CC detected in other tissues examined. {ECO:0000269|PubMed:11829489}.
CC -!- DISEASE: Glutaric aciduria 3 (GA3) [MIM:231690]: A metabolic disorder
CC due to peroxisomal glutaryl-CoA oxidase deficiency and characterized by
CC the excretion of abnormal quantities of glutaric acid but low 3-
CC hydroxyglutaric acid. {ECO:0000269|PubMed:18926513,
CC ECO:0000269|PubMed:23893049}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AK021870; BAB13922.1; -; mRNA.
DR EMBL; AK299133; BAG61185.1; -; mRNA.
DR EMBL; AC004988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236951; EAL24000.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW94136.1; -; Genomic_DNA.
DR EMBL; BC098117; AAH98117.1; -; mRNA.
DR EMBL; BC098261; AAH98261.1; -; mRNA.
DR EMBL; BC098310; AAH98310.1; -; mRNA.
DR EMBL; BC098318; AAH98318.1; -; mRNA.
DR EMBL; AF397013; AAL76418.1; -; mRNA.
DR EMBL; AB014767; BAB87807.1; -; mRNA.
DR RefSeq; NP_001180240.1; NM_001193311.1.
DR RefSeq; NP_001180241.1; NM_001193312.1.
DR RefSeq; NP_001180242.1; NM_001193313.1.
DR RefSeq; NP_079004.1; NM_024728.2.
DR AlphaFoldDB; Q9HAC7; -.
DR SMR; Q9HAC7; -.
DR BioGRID; 122883; 21.
DR IntAct; Q9HAC7; 30.
DR STRING; 9606.ENSP00000338475; -.
DR iPTMnet; Q9HAC7; -.
DR PhosphoSitePlus; Q9HAC7; -.
DR BioMuta; SUGCT; -.
DR DMDM; 71152390; -.
DR EPD; Q9HAC7; -.
DR jPOST; Q9HAC7; -.
DR MassIVE; Q9HAC7; -.
DR MaxQB; Q9HAC7; -.
DR PeptideAtlas; Q9HAC7; -.
DR PRIDE; Q9HAC7; -.
DR ProteomicsDB; 81391; -. [Q9HAC7-1]
DR ProteomicsDB; 81392; -. [Q9HAC7-2]
DR ProteomicsDB; 81393; -. [Q9HAC7-3]
DR ProteomicsDB; 81394; -. [Q9HAC7-4]
DR Antibodypedia; 49926; 128 antibodies from 20 providers.
DR DNASU; 79783; -.
DR Ensembl; ENST00000335693.9; ENSP00000338475.5; ENSG00000175600.16.
DR Ensembl; ENST00000401647.7; ENSP00000385222.3; ENSG00000175600.16.
DR Ensembl; ENST00000628514.3; ENSP00000486291.2; ENSG00000175600.16.
DR GeneID; 79783; -.
DR KEGG; hsa:79783; -.
DR UCSC; uc003thn.3; human. [Q9HAC7-1]
DR CTD; 79783; -.
DR DisGeNET; 79783; -.
DR GeneCards; SUGCT; -.
DR HGNC; HGNC:16001; SUGCT.
DR HPA; ENSG00000175600; Tissue enhanced (kidney, liver).
DR MalaCards; SUGCT; -.
DR MIM; 231690; phenotype.
DR MIM; 609187; gene.
DR neXtProt; NX_Q9HAC7; -.
DR Orphanet; 35706; Glutaric acidemia type 3.
DR PharmGKB; PA25942; -.
DR VEuPathDB; HostDB:ENSG00000175600; -.
DR eggNOG; KOG3957; Eukaryota.
DR HOGENOM; CLU_033975_0_2_1; -.
DR InParanoid; Q9HAC7; -.
DR OrthoDB; 983223at2759; -.
DR PhylomeDB; Q9HAC7; -.
DR TreeFam; TF314188; -.
DR BioCyc; MetaCyc:ENSG00000175600-MON; -.
DR BRENDA; 2.8.3.13; 2681.
DR PathwayCommons; Q9HAC7; -.
DR SignaLink; Q9HAC7; -.
DR BioGRID-ORCS; 79783; 8 hits in 1067 CRISPR screens.
DR ChiTaRS; SUGCT; human.
DR GenomeRNAi; 79783; -.
DR Pharos; Q9HAC7; Tbio.
DR PRO; PR:Q9HAC7; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9HAC7; protein.
DR Bgee; ENSG00000175600; Expressed in right adrenal gland cortex and 120 other tissues.
DR ExpressionAtlas; Q9HAC7; baseline and differential.
DR Genevisible; Q9HAC7; HS.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0047369; F:succinate-hydroxymethylglutarate CoA-transferase activity; IDA:UniProtKB.
DR Gene3D; 3.30.1540.10; -; 1.
DR Gene3D; 3.40.50.10540; -; 1.
DR InterPro; IPR003673; CoA-Trfase_fam_III.
DR InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR Pfam; PF02515; CoA_transf_3; 1.
DR SUPFAM; SSF89796; SSF89796; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant; Glutaricaciduria;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 39..445
FT /note="Succinate--hydroxymethylglutarate CoA-transferase"
FT /id="PRO_0000194726"
FT ACT_SITE 212
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT MOD_RES 401
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7TNE1"
FT VAR_SEQ 126..162
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014721"
FT VAR_SEQ 200..247
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043291"
FT VAR_SEQ 370
FT /note="Q -> QNAVSGFQSLLHSLAHGPFLHLQGSAR (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_014722"
FT VARIANT 336
FT /note="R -> W (in GA3; inactive enzyme; healthy individuals
FT who have abnormal quantities of glutaric acid but low 3-
FT hydroxyglutaric acid; dbSNP:rs137852860)"
FT /evidence="ECO:0000269|PubMed:18926513,
FT ECO:0000269|PubMed:23893049"
FT /id="VAR_054852"
FT CONFLICT 99
FT /note="E -> G (in Ref. 7; BAB87807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 48462 MW; D1FE42D75787692A CRC64;
MPSETHAMLA TLARVAALRR TCLFSGRGGG RGLWTGRPQS DMNNIKPLEG VKILDLTRVL
AGPFATMNLG DLGAEVIKVE RPGAGDDTRT WGPPFVGTES TYYLSVNRNK KSIAVNIKDP
KGVKIIKELA AVCDVFVENY VPGKLSAMGL GYEDIDEIAP HIIYCSITGY GQTGPISQRA
GYDAVASAVS GLMHITGPEN GDPVRPGVAM TDLATGLYAY GAIMAGLIQK YKTGKGLFID
CNLLSSQVAC LSHIAANYLI GQKEAKRWGT AHGSIVPYQA FKTKDGYIVV GAGNNQQFAT
VCKILDLPEL IDNSKYKTNH LRVHNRKELI KILSERFEEE LTSKWLYLFE GSGVPYGPIN
NMKNVFAEPQ VLHNGLVMEM EHPTVGKISV PGPAVRYSKF KMSEARPPPL LGQHTTHILK
EVLRYDDRAI GELLSAGVVD QHETH
