FTCD_MOUSE
ID FTCD_MOUSE Reviewed; 541 AA.
AC Q91XD4;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Formimidoyltransferase-cyclodeaminase;
DE AltName: Full=Formiminotransferase-cyclodeaminase;
DE Short=FTCD;
DE Includes:
DE RecName: Full=Glutamate formimidoyltransferase;
DE EC=2.1.2.5;
DE AltName: Full=Glutamate formiminotransferase;
DE AltName: Full=Glutamate formyltransferase;
DE Includes:
DE RecName: Full=Formimidoyltetrahydrofolate cyclodeaminase;
DE EC=4.3.1.4;
DE AltName: Full=Formiminotetrahydrofolate cyclodeaminase;
GN Name=Ftcd;
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 TISSUE=Liver;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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).
CC -!- FUNCTION: Folate-dependent enzyme, that displays both transferase and
CC deaminase activity. Serves to channel one-carbon units from
CC formiminoglutamate to the folate pool (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Binds and promotes bundling of vimentin filaments originating
CC from the Golgi. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-formimidoyltetrahydrofolate + L-glutamate = (6S)-5,6,7,8-
CC tetrahydrofolate + N-formimidoyl-L-glutamate; Xref=Rhea:RHEA:15097,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57453, ChEBI:CHEBI:57456,
CC ChEBI:CHEBI:58928; EC=2.1.2.5;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5-formyl-5,6,7,8-tetrahydrofolate + L-glutamate = (6S)-
CC 5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-glutamate;
CC Xref=Rhea:RHEA:23240, ChEBI:CHEBI:15378, ChEBI:CHEBI:17684,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57453, ChEBI:CHEBI:57457; EC=2.1.2.5;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-formimidoyltetrahydrofolate + 2 H(+) = 5,10-
CC methenyltetrahydrofolate + NH4(+); Xref=Rhea:RHEA:22736,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57455,
CC ChEBI:CHEBI:57456; EC=4.3.1.4;
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; L-glutamate from N-formimidoyl-L-glutamate (transferase
CC route): step 1/1.
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- SUBUNIT: Homooctamer, including four polyglutamate binding sites. The
CC subunits are arranged as a tetramer of dimers, and form a planar ring-
CC shaped structure (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}. Note=More abundantly located around the mother
CC centriole. {ECO:0000250}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC cyclodeaminase/cyclohydrolase family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC formiminotransferase family. {ECO:0000305}.
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DR EMBL; BC010813; AAH10813.1; -; mRNA.
DR EMBL; BC024078; AAH24078.1; -; mRNA.
DR CCDS; CCDS23950.1; -.
DR RefSeq; NP_543121.1; NM_080845.2.
DR AlphaFoldDB; Q91XD4; -.
DR SMR; Q91XD4; -.
DR BioGRID; 199754; 1.
DR IntAct; Q91XD4; 1.
DR STRING; 10090.ENSMUSP00000001183; -.
DR iPTMnet; Q91XD4; -.
DR PhosphoSitePlus; Q91XD4; -.
DR SwissPalm; Q91XD4; -.
DR jPOST; Q91XD4; -.
DR MaxQB; Q91XD4; -.
DR PaxDb; Q91XD4; -.
DR PeptideAtlas; Q91XD4; -.
DR PRIDE; Q91XD4; -.
DR ProteomicsDB; 267529; -.
DR Antibodypedia; 4293; 652 antibodies from 39 providers.
DR DNASU; 14317; -.
DR Ensembl; ENSMUST00000001183; ENSMUSP00000001183; ENSMUSG00000001155.
DR GeneID; 14317; -.
DR KEGG; mmu:14317; -.
DR UCSC; uc007fut.2; mouse.
DR CTD; 10841; -.
DR MGI; MGI:1339962; Ftcd.
DR VEuPathDB; HostDB:ENSMUSG00000001155; -.
DR eggNOG; ENOG502QQBY; Eukaryota.
DR GeneTree; ENSGT00390000005581; -.
DR HOGENOM; CLU_040037_1_0_1; -.
DR InParanoid; Q91XD4; -.
DR OMA; VGQPECV; -.
DR OrthoDB; 1063278at2759; -.
DR PhylomeDB; Q91XD4; -.
DR TreeFam; TF333892; -.
DR Reactome; R-MMU-70921; Histidine catabolism.
DR UniPathway; UPA00193; -.
DR UniPathway; UPA00379; UER00555.
DR BioGRID-ORCS; 14317; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q91XD4; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q91XD4; protein.
DR Bgee; ENSMUSG00000001155; Expressed in left lobe of liver and 44 other tissues.
DR Genevisible; Q91XD4; MM.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0030412; F:formimidoyltetrahydrofolate cyclodeaminase activity; ISO:MGI.
DR GO; GO:0030409; F:glutamate formimidoyltransferase activity; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:MGI.
DR GO; GO:0006548; P:histidine catabolic process; TAS:MGI.
DR GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.120.680; -; 1.
DR Gene3D; 3.30.70.670; -; 1.
DR Gene3D; 3.30.990.10; -; 1.
DR InterPro; IPR007044; Cyclodeamin/CycHdrlase.
DR InterPro; IPR013802; Formiminotransferase_C.
DR InterPro; IPR037070; Formiminotransferase_C_sf.
DR InterPro; IPR004227; Formiminotransferase_cat.
DR InterPro; IPR012886; Formiminotransferase_N.
DR InterPro; IPR037064; Formiminotransferase_N_sf.
DR InterPro; IPR022384; FormiminoTrfase_cat_dom_sf.
DR InterPro; IPR036178; Formintransfe-cycloase-like_sf.
DR Pfam; PF02971; FTCD; 1.
DR Pfam; PF04961; FTCD_C; 1.
DR Pfam; PF07837; FTCD_N; 1.
DR SMART; SM01221; FTCD; 1.
DR SMART; SM01222; FTCD_N; 1.
DR SUPFAM; SSF101262; SSF101262; 1.
DR SUPFAM; SSF55116; SSF55116; 2.
DR TIGRFAMs; TIGR02024; FtcD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Folate-binding; Golgi apparatus;
KW Histidine metabolism; Lyase; Multifunctional enzyme; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..541
FT /note="Formimidoyltransferase-cyclodeaminase"
FT /id="PRO_0000087360"
FT REGION 1..181
FT /note="Formiminotransferase N-subdomain"
FT /evidence="ECO:0000250"
FT REGION 182..326
FT /note="Formiminotransferase C-subdomain"
FT /evidence="ECO:0000250"
FT REGION 327..334
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 335..541
FT /note="Cyclodeaminase/cyclohydrolase"
FT /evidence="ECO:0000250"
FT ACT_SITE 82
FT /note="For formimidoyltransferase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 412
FT /note="For cyclodeaminase activity"
FT /evidence="ECO:0000250"
FT BINDING 163..172
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88618"
SQ SEQUENCE 541 AA; 58939 MW; 988DDAC3847F5BC3 CRC64;
MSQLVECVPN FSEGNNQEVI DAISRAISQT PGCVLLDVDA GPSTNRTVYT FVGQPECVVE
GALHAARTAS QLIDMSKHKG EHPRMGALDV CPFIPVRGVS MEECVLCAKA FGQRLAEELN
VPVYLYGEAA QTPSRQTLPA IRAGEYEALP EKLKQAEWVP DFGPSSFVPS WGATVTGARK
FLIAFNINLL STKEQAHRIA LNLREQGRGK DQPGRLKKVQ GIGWYLEEKN LAQVSTNLLD
FEVTALHTVF EEARREAQEL NLPVVGSQLV GLVPLKALLD AAAFYCDKEK LFVLEEEHRI
RLVVNRLGLD SLAPFDPKER IIEYLVPDSG PEQSLLDTSL RGFVREVGAR SAAPGGGSVA
AAVAALGAAL ASMVGQMTYG RRQFDHLDST MRRLIPPFHA ASAQLTSLVD ADARAFAACL
EAIKLPKNTP EERDRRACAL QEGLRQAVAV PLKLAETVSQ LWPALQELAH CGNLSCLSDL
QVAAKALETG VFGAYFNVLI NLKDMTDDVF KEKTHHRISS LLQEAKTQAA LVLGSLEARK
E
