ID C1TC_MOUSE Reviewed; 935 AA. AC Q922D8; Q8R013; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 4. DT 24-JAN-2024, entry version 172. DE RecName: Full=C-1-tetrahydrofolate synthase, cytoplasmic {ECO:0000305|PubMed:15611115}; DE Short=C1-THF synthase; DE Includes: DE RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000305|PubMed:15611115}; DE EC=1.5.1.5 {ECO:0000269|PubMed:15611115}; DE Includes: DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000250|UniProtKB:P11586}; DE EC=3.5.4.9 {ECO:0000250|UniProtKB:P11586}; DE Includes: DE RecName: Full=Formyltetrahydrofolate synthetase {ECO:0000305|PubMed:15611115}; DE EC=6.3.4.3 {ECO:0000269|PubMed:15611115}; DE Contains: DE RecName: Full=C-1-tetrahydrofolate synthase, cytoplasmic, N-terminally processed; GN Name=Mthfd1; 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 [GENOMIC DNA / MRNA]. RC STRAIN=129/SvJ; RX PubMed=12061812; DOI=10.1016/s0003-9861(02)00203-5; RA Patel H., Christensen K.E., Mejia N., MacKenzie R.E.; RT "Mammalian mitochondrial methylenetetrahydrofolate dehydrogenase- RT cyclohydrolase derived from a trifunctional methylenetetrahydrofolate RT dehydrogenase-cyclohydrolase-synthetase."; RL Arch. Biochem. Biophys. 403:145-148(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP PROTEIN SEQUENCE OF 2-17; 27-56; 59-66; 75-83; 123-134; 138-173; 176-198; RP 205-223; 251-262; 314-324; 330-352; 355-362; 371-402; 464-473; 488-495; RP 505-517; 521-532; 543-553; 658-679; 687-702; 706-733; 747-772; 776-784; RP 805-819; 833-848 AND 855-889, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [5] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION. RX PubMed=15611115; DOI=10.1074/jbc.m409380200; RA Christensen K.E., Patel H., Kuzmanov U., Mejia N.R., MacKenzie R.E.; RT "Disruption of the mthfd1 gene reveals a monofunctional 10- RT formyltetrahydrofolate synthetase in mammalian mitochondria."; RL J. Biol. Chem. 280:7597-7602(2005). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; 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: Trifunctional enzyme that catalyzes the interconversion of CC three forms of one-carbon-substituted tetrahydrofolate: (6R)-5,10- CC methylene-5,6,7,8-tetrahydrofolate, 5,10-methenyltetrahydrofolate and CC (6S)-10-formyltetrahydrofolate. These derivatives of tetrahydrofolate CC are differentially required in nucleotide and amino acid biosynthesis, CC (6S)-10-formyltetrahydrofolate being required for purine biosynthesis CC while (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate is used for serine CC and methionine biosynthesis for instance. CC {ECO:0000269|PubMed:15611115}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)- CC 5,10-methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812, CC ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.5.1.5; CC Evidence={ECO:0000269|PubMed:15611115}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10- CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455, CC ChEBI:CHEBI:195366; EC=3.5.4.9; CC Evidence={ECO:0000250|UniProtKB:P11586}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-10- CC formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57453, ChEBI:CHEBI:195366, ChEBI:CHEBI:456216; CC EC=6.3.4.3; Evidence={ECO:0000269|PubMed:15611115}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000269|PubMed:15611115}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11586}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:15611115}. CC -!- DOMAIN: The N-terminal methylenetetrahydrofolate dehydrogenase and CC methenyltetrahydrofolate cyclohydrolase (D/C) domain carries both the CC methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate CC cyclohydrolase activities. {ECO:0000250|UniProtKB:P11586}. CC -!- DOMAIN: The larger C-terminal formyltetrahydrofolate synthetase domain CC carries a third formyltetrahydrofolate synthetase activity. CC {ECO:0000250|UniProtKB:P11586}. CC -!- SIMILARITY: In the N-terminal section; belongs to the tetrahydrofolate CC dehydrogenase/cyclohydrolase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC formate--tetrahydrofolate ligase family. {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; AF364579; AAL99692.1; -; mRNA. DR EMBL; AF364591; AAL99693.1; -; Genomic_DNA. DR EMBL; AF364580; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364581; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364582; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364583; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364584; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364585; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364586; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364587; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364588; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364589; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364590; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AK088700; BAC40513.1; -; mRNA. DR EMBL; BC008523; AAH08523.1; -; mRNA. DR CCDS; CCDS25990.1; -. DR RefSeq; NP_620084.2; NM_138745.2. DR AlphaFoldDB; Q922D8; -. DR SMR; Q922D8; -. DR BioGRID; 223871; 23. DR IntAct; Q922D8; 4. DR MINT; Q922D8; -. DR STRING; 10090.ENSMUSP00000021443; -. DR ChEMBL; CHEMBL3137; -. DR GlyGen; Q922D8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q922D8; -. DR PhosphoSitePlus; Q922D8; -. DR SwissPalm; Q922D8; -. DR REPRODUCTION-2DPAGE; Q922D8; -. DR EPD; Q922D8; -. DR jPOST; Q922D8; -. DR MaxQB; Q922D8; -. DR PaxDb; 10090-ENSMUSP00000021443; -. DR PeptideAtlas; Q922D8; -. DR ProteomicsDB; 273855; -. DR Pumba; Q922D8; -. DR Antibodypedia; 52; 190 antibodies from 30 providers. DR DNASU; 108156; -. DR Ensembl; ENSMUST00000021443.7; ENSMUSP00000021443.6; ENSMUSG00000021048.8. DR GeneID; 108156; -. DR KEGG; mmu:108156; -. DR UCSC; uc007nxz.2; mouse. DR AGR; MGI:1342005; -. DR CTD; 4522; -. DR MGI; MGI:1342005; Mthfd1. DR VEuPathDB; HostDB:ENSMUSG00000021048; -. DR eggNOG; KOG4230; Eukaryota. DR GeneTree; ENSGT00940000154746; -. DR HOGENOM; CLU_003601_2_0_1; -. DR InParanoid; Q922D8; -. DR OMA; QPIMFRR; -. DR OrthoDB; 651667at2759; -. DR PhylomeDB; Q922D8; -. DR TreeFam; TF300623; -. DR BRENDA; 6.3.4.3; 3474. DR Reactome; R-MMU-196757; Metabolism of folate and pterines. DR UniPathway; UPA00193; -. DR BioGRID-ORCS; 108156; 23 hits in 79 CRISPR screens. DR ChiTaRS; Mthfd1; mouse. DR PRO; PR:Q922D8; -. DR Proteomes; UP000000589; Chromosome 12. DR RNAct; Q922D8; Protein. DR Bgee; ENSMUSG00000021048; Expressed in paneth cell and 286 other cell types or tissues. DR ExpressionAtlas; Q922D8; baseline and differential. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IMP:UniProtKB. DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; ISS:UniProtKB. DR GO; GO:0004487; F:methylenetetrahydrofolate dehydrogenase (NAD+) activity; IDA:BHF-UCL. DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IMP:UniProtKB. DR GO; GO:0004486; F:methylenetetrahydrofolate dehydrogenase [NAD(P)+] activity; ISO:MGI. DR GO; GO:0009257; P:10-formyltetrahydrofolate biosynthetic process; IMP:BHF-UCL. DR GO; GO:0007507; P:heart development; IMP:BHF-UCL. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009086; P:methionine biosynthetic process; ISO:MGI. DR GO; GO:0006555; P:methionine metabolic process; IMP:BHF-UCL. DR GO; GO:0001843; P:neural tube closure; IMP:BHF-UCL. DR GO; GO:0001780; P:neutrophil homeostasis; IMP:BHF-UCL. DR GO; GO:0006730; P:one-carbon metabolic process; ISO:MGI. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:BHF-UCL. DR GO; GO:0009152; P:purine ribonucleotide biosynthetic process; IMP:UniProtKB. DR GO; GO:0009070; P:serine family amino acid biosynthetic process; ISO:MGI. DR GO; GO:0009069; P:serine family amino acid metabolic process; IMP:BHF-UCL. DR GO; GO:0061053; P:somite development; IMP:BHF-UCL. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IMP:BHF-UCL. DR GO; GO:0019346; P:transsulfuration; IMP:BHF-UCL. DR CDD; cd00477; FTHFS; 1. DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1. DR Gene3D; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 1. DR Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1. DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR HAMAP; MF_01543; FTHFS; 1. DR HAMAP; MF_01576; THF_DHG_CYH; 1. DR InterPro; IPR046346; Aminoacid_DH-like_N_sf. DR InterPro; IPR000559; Formate_THF_ligase. DR InterPro; IPR020628; Formate_THF_ligase_CS. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000672; THF_DH/CycHdrlase. DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom. DR InterPro; IPR020867; THF_DH/CycHdrlase_CS. DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom. DR PANTHER; PTHR48099:SF1; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC; 1. DR PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1. DR Pfam; PF01268; FTHFS; 1. DR Pfam; PF00763; THF_DHG_CYH; 1. DR Pfam; PF02882; THF_DHG_CYH_C; 1. DR PRINTS; PR00085; THFDHDRGNASE. DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00721; FTHFS_1; 1. DR PROSITE; PS00722; FTHFS_2; 1. DR PROSITE; PS00766; THF_DHG_CYH_1; 1. DR PROSITE; PS00767; THF_DHG_CYH_2; 1. DR Genevisible; Q922D8; MM. PE 1: Evidence at protein level; KW Acetylation; Amino-acid biosynthesis; ATP-binding; Cytoplasm; KW Direct protein sequencing; Histidine biosynthesis; Hydrolase; Ligase; KW Methionine biosynthesis; Multifunctional enzyme; NADP; Nucleotide-binding; KW One-carbon metabolism; Oxidoreductase; Phosphoprotein; Purine biosynthesis; KW Reference proteome. FT CHAIN 1..935 FT /note="C-1-tetrahydrofolate synthase, cytoplasmic" FT /id="PRO_0000199322" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000250|UniProtKB:P11586" FT CHAIN 2..935 FT /note="C-1-tetrahydrofolate synthase, cytoplasmic, N- FT terminally processed" FT /id="PRO_0000423281" FT REGION 2..291 FT /note="Methylenetetrahydrofolate dehydrogenase and FT methenyltetrahydrofolate cyclohydrolase (D/C) domain" FT /evidence="ECO:0000250|UniProtKB:P11586" FT REGION 310..935 FT /note="Formyltetrahydrofolate synthetase domain" FT /evidence="ECO:0000250|UniProtKB:P11586" FT ACT_SITE 56 FT /evidence="ECO:0000250|UniProtKB:P11586" FT BINDING 52..56 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11586" FT BINDING 99..101 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11586" FT BINDING 172..174 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11586" FT BINDING 197 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11586" FT BINDING 272..276 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11586" FT BINDING 380..387 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P11586" FT MOD_RES 318 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11586" FT MOD_RES 413 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11586" FT MOD_RES 490 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11586" FT CONFLICT 365 FT /note="H -> Y (in Ref. 3; AAH08523)" FT /evidence="ECO:0000305" FT CONFLICT 610 FT /note="A -> T (in Ref. 3; AAH08523)" FT /evidence="ECO:0000305" SQ SEQUENCE 935 AA; 101200 MW; 0EB92D58C78DDEB5 CRC64; MAPAGILNGK LVSAQIRDRL KNQVTRMQEQ VPGFTPGLAI LQVGDRDDSN LYINVKLKAA EEIGIKATHI KLPRTSTESE VLKYVISLNE DASVHGFIVQ LPLDSENSIN TEAVINAIAP EKDVDGLTSV SAGKLARGDL NDCFIPCTPK GCLELIKEAG VQIAGRHAVV VGRSKIVGAP MHDLLLWNNA TVTTCHSKTA NLDKEVNKGD ILVVATGQPE MVKGEWIKPG AVVIDCGINY VPDDTKPNGR KVVGDVAYDE AKERASFITP VPGGVGPMTV AMLMQSTVES AQRFLQKFKP GKWTIQYNKL NLKTPVPSDI AISRSCKPKL IGNLAREIGL LTEEVELYGE TKAKVLLSAL DRLKHQPDGK YVVVTGITPT PLGEGKSTTT IGLVQALGAH LRQNVFACVR QPSQGPTFGI KGGAAGGGYS QVIPMEEFNL HLTGDIHAIT AANNLVAAAI DARIFHELTQ TDKALFNRLV PSVNGIRKFS DIQIRRLRRL GIEKTDPTTL TDDEINRFAR LDIDPETITW QRVLDTNDRF LRKITIGQSP TEKGHTRTAQ FDISVASEIM AVLALTSSLE DMRERLGRMV VASSKKGEPI SCEDLGVSGA LTVLMKDAIK PNLMQTLEGT PVFVHAGPFA NIAHGNSSII ADRIALKLVG PEGFVVTEAG FGADIGMEKF FNIKCRYSGL QPHVVVLVAT VRALKMHGGG PTVTAGLPLP KAYTEEDLDL VEKGFSNLRK QIENARMFGV PVVVAVNVFK TDTDAELDLV SRLSREHGAF DAVKCTHWAE GGQGALALAQ AVQRASQAPS SFQLLYDLKL SIEDKIRIIA QRIYGADDIE LLPEAQNKAE IYTKQGFGNL PICMAKTHLS LSHNPEQKGV PTGFVLPIRD IRASVGAGFL YPLVGTMSTM PGLPTRPCFY DIDLDPETEQ VNGLF //