ID GCST_HUMAN Reviewed; 403 AA. AC P48728; A8K3I5; B4DE61; B4DJQ0; E9PBG1; Q96IG6; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 15-MAR-2017, entry version 161. DE RecName: Full=Aminomethyltransferase, mitochondrial {ECO:0000305}; DE EC=2.1.2.10 {ECO:0000269|PubMed:16051266}; DE AltName: Full=Glycine cleavage system T protein {ECO:0000303|PubMed:7916605}; DE Short=GCVT; DE Flags: Precursor; GN Name=AMT {ECO:0000312|HGNC:HGNC:473}; Synonyms=GCST; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=7916605; DOI=10.1006/bbrc.1993.1480; RA Hayasaka K., Nanao K., Takada G., Okamura-Ikeda K., Motokawa Y.; RT "Isolation and sequence determination of cDNA encoding human T-protein RT of the glycine cleavage system."; RL Biochem. Biophys. Res. Commun. 192:766-771(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8188235; DOI=10.1006/geno.1994.1007; RA Nanao K., Takada G., Takahashi E., Seki N., Komatsu Y., RA Okamura-Ikeda K., Motokawa Y., Hayasaka K.; RT "Structure and chromosomal localization of the aminomethyltransferase RT gene (AMT)."; RL Genomics 19:27-30(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Cerebellum, Heart, and Thalamus; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-386 (ISOFORM 4). RC TISSUE=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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-403 ALONE AND IN COMPLEX RP WITH 5-METHYLTETRAHYDROFOLATE, SUBSTRATE-BINDING SITES, CATALYTIC RP ACTIVITY, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, CHARACTERIZATION OF RP VARIANTS NKH ILE-145; ASP-269 AND HIS-320, AND MUTAGENESIS OF ASP-129. RX PubMed=16051266; DOI=10.1016/j.jmb.2005.06.056; RA Okamura-Ikeda K., Hosaka H., Yoshimura M., Yamashita E., Toma S., RA Nakagawa A., Fujiwara K., Motokawa Y., Taniguchi H.; RT "Crystal structure of human T-protein of glycine cleavage system at RT 2.0 A resolution and its implication for understanding non-ketotic RT hyperglycinemia."; RL J. Mol. Biol. 351:1146-1159(2005). RN [9] RP VARIANTS NKH ARG-47; ASP-269 AND HIS-320, AND INVOLVEMENT IN NKH. RX PubMed=8005589; DOI=10.1007/BF00201565; RA Nanao K., Okamura-Ikeda K., Motokawa Y., Danks D.M., Baumgartner E.R., RA Takada G., Hayasaka K.; RT "Identification of the mutations in the T-protein gene causing typical RT and atypical nonketotic hyperglycinemia."; RL Hum. Genet. 93:655-658(1994). RN [10] RP VARIANT NKH ARG-42. RX PubMed=9600239; DOI=10.1007/s004390050716; RA Kure S., Mandel H., Rolland M.-O., Sakata Y., Shinka T., Drugan A., RA Boneh A., Tada K., Matsubara Y., Narisawa K.; RT "A missense mutation (His42Arg) in the T-protein gene from a large RT Israeli-Arab kindred with nonketotic hyperglycinemia."; RL Hum. Genet. 102:430-434(1998). RN [11] RP VARIANT NKH HIS-276. RX PubMed=9621520; DOI=10.1007/s100380050055; RA Kure S., Shinka T., Sakata Y., Osamu N., Takayanagi M., Tada K., RA Matsubara Y., Narisawa K.; RT "A one-base deletion (183delC) and a missense mutation (D276H) in the RT T-protein gene from a Japanese family with nonketotic RT hyperglycinemia."; RL J. Hum. Genet. 43:135-137(1998). RN [12] RP VARIANTS NKH LYS-211 AND HIS-320. RX PubMed=10873393; DOI=10.1006/mgme.2000.3000; RA Toone J.R., Applegarth D.A., Coulter-Mackie M.B., James E.R.; RT "Biochemical and molecular investigations of patients with nonketotic RT hyperglycinemia."; RL Mol. Genet. Metab. 70:116-121(2000). RN [13] RP VARIANTS NKH ILE-145 AND HIS-320. RX PubMed=11286506; DOI=10.1006/mgme.2001.3158; RA Toone J.R., Applegarth D.A., Coulter-Mackie M.B., James E.R.; RT "Recurrent mutations in P- and T-proteins of the glycine cleavage RT complex and a novel T-protein mutation (N145I): a strategy for the RT molecular investigation of patients with nonketotic hyperglycinemia RT (NKH)."; RL Mol. Genet. Metab. 72:322-325(2001). RN [14] RP VARIANT NKH CYS-265. RX PubMed=26371980; DOI=10.1016/j.ejpn.2015.08.008; RA Belcastro V., Barbarini M., Barca S., Mauro I.; RT "A novel AMT gene mutation in a newborn with nonketotic RT hyperglycinemia and early myoclonic encephalopathy."; RL Eur. J. Paediatr. Neurol. 20:192-195(2016). CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. {ECO:0000269|PubMed:16051266}. CC -!- CATALYTIC ACTIVITY: [Protein]-S(8)-aminomethyldihydrolipoyllysine CC + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10- CC methylenetetrahydrofolate + NH(3). {ECO:0000269|PubMed:16051266}. CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H. {ECO:0000305|PubMed:16051266}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:16051266}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=P48728-1; Sequence=Displayed; CC Name=2; CC IsoId=P48728-2; Sequence=VSP_042557; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=P48728-3; Sequence=VSP_043288; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=P48728-4; Sequence=VSP_045418; CC Note=No experimental confirmation available.; CC -!- DISEASE: Non-ketotic hyperglycinemia (NKH) [MIM:605899]: Autosomal CC recessive disease characterized by accumulation of a large amount CC of glycine in body fluid and by severe neurological symptoms. CC {ECO:0000269|PubMed:10873393, ECO:0000269|PubMed:11286506, CC ECO:0000269|PubMed:16051266, ECO:0000269|PubMed:26371980, CC ECO:0000269|PubMed:8005589, ECO:0000269|PubMed:9600239, CC ECO:0000269|PubMed:9621520}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the GcvT 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; D13811; BAA02967.1; -; mRNA. DR EMBL; D14686; BAA03512.1; -; Genomic_DNA. DR EMBL; AK290600; BAF83289.1; -; mRNA. DR EMBL; AK293481; BAG56972.1; -; mRNA. DR EMBL; AK296177; BAG58912.1; -; mRNA. DR EMBL; AC104452; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64984.1; -; Genomic_DNA. DR EMBL; BC007546; AAH07546.2; -; mRNA. DR CCDS; CCDS2797.1; -. [P48728-1] DR CCDS; CCDS54583.1; -. [P48728-2] DR CCDS; CCDS54584.1; -. [P48728-3] DR CCDS; CCDS54585.1; -. [P48728-4] DR PIR; I54192; I54192. DR RefSeq; NP_000472.2; NM_000481.3. [P48728-1] DR RefSeq; NP_001158182.1; NM_001164710.1. [P48728-3] DR RefSeq; NP_001158183.1; NM_001164711.1. [P48728-2] DR RefSeq; NP_001158184.1; NM_001164712.1. [P48728-4] DR UniGene; Hs.102; -. DR PDB; 1WSR; X-ray; 2.00 A; A/B=29-403. DR PDB; 1WSV; X-ray; 2.60 A; A/B=29-403. DR PDBsum; 1WSR; -. DR PDBsum; 1WSV; -. DR ProteinModelPortal; P48728; -. DR SMR; P48728; -. DR BioGrid; 106772; 2. DR IntAct; P48728; 1. DR STRING; 9606.ENSP00000273588; -. DR DrugBank; DB04789; 5-methyltetrahydrofolic acid. DR DrugBank; DB00157; NADH. DR DrugBank; DB00116; Tetrahydrofolic acid. DR iPTMnet; P48728; -. DR PhosphoSitePlus; P48728; -. DR BioMuta; AMT; -. DR DMDM; 1346122; -. DR EPD; P48728; -. DR MaxQB; P48728; -. DR PaxDb; P48728; -. DR PeptideAtlas; P48728; -. DR PRIDE; P48728; -. DR Ensembl; ENST00000273588; ENSP00000273588; ENSG00000145020. [P48728-1] DR Ensembl; ENST00000395338; ENSP00000378747; ENSG00000145020. [P48728-4] DR Ensembl; ENST00000458307; ENSP00000415619; ENSG00000145020. [P48728-3] DR Ensembl; ENST00000636522; ENSP00000489758; ENSG00000145020. [P48728-2] DR GeneID; 275; -. DR KEGG; hsa:275; -. DR UCSC; uc003cww.4; human. [P48728-1] DR CTD; 275; -. DR DisGeNET; 275; -. DR GeneCards; AMT; -. DR GeneReviews; AMT; -. DR HGNC; HGNC:473; AMT. DR HPA; HPA005566; -. DR MalaCards; AMT; -. DR MIM; 238310; gene. DR MIM; 605899; phenotype. DR neXtProt; NX_P48728; -. DR OpenTargets; ENSG00000145020; -. DR Orphanet; 289863; Atypical glycine encephalopathy. DR Orphanet; 289860; Infantile glycine encephalopathy. DR Orphanet; 289857; Neonatal glycine encephalopathy. DR PharmGKB; PA24780; -. DR eggNOG; KOG2770; Eukaryota. DR eggNOG; COG0404; LUCA. DR GeneTree; ENSGT00530000063120; -. DR HOGENOM; HOG000239380; -. DR HOVERGEN; HBG005822; -. DR InParanoid; P48728; -. DR KO; K00605; -. DR OMA; HSPILNM; -. DR OrthoDB; EOG091G07Z1; -. DR PhylomeDB; P48728; -. DR TreeFam; TF313026; -. DR BioCyc; MetaCyc:HS07223-MONOMER; -. DR BRENDA; 2.1.2.10; 2681. DR Reactome; R-HSA-6783984; Glycine degradation. DR SABIO-RK; P48728; -. DR ChiTaRS; AMT; human. DR EvolutionaryTrace; P48728; -. DR GenomeRNAi; 275; -. DR PRO; PR:P48728; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000145020; -. DR CleanEx; HS_AMT; -. DR ExpressionAtlas; P48728; baseline and differential. DR Genevisible; P48728; HS. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IC:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0004047; F:aminomethyltransferase activity; IMP:UniProtKB. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0006546; P:glycine catabolic process; TAS:ProtInc. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IMP:UniProtKB. DR GO; GO:0046487; P:glyoxylate metabolic process; TAS:Reactome. DR Gene3D; 2.40.30.110; -; 1. DR Gene3D; 3.30.1360.120; -; 2. DR InterPro; IPR006223; GCS_T. DR InterPro; IPR028896; GCST/DmdA. DR InterPro; IPR013977; GCV_T_C. DR InterPro; IPR006222; GCV_T_N. DR InterPro; IPR029043; GcvT/YgfZ_C. DR InterPro; IPR027266; TrmE/GcvT_dom1. DR Pfam; PF01571; GCV_T; 1. DR Pfam; PF08669; GCV_T_C; 1. DR PIRSF; PIRSF006487; GcvT; 1. DR SUPFAM; SSF101790; SSF101790; 1. DR TIGRFAMs; TIGR00528; gcvT; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Aminotransferase; KW Complete proteome; Disease mutation; Mitochondrion; KW Reference proteome; Transferase; Transit peptide. FT TRANSIT 1 28 Mitochondrion. FT {ECO:0000250|UniProtKB:P25285}. FT CHAIN 29 403 Aminomethyltransferase, mitochondrial. FT /FTId=PRO_0000010755. FT BINDING 232 232 Substrate. {ECO:0000269|PubMed:16051266}. FT BINDING 261 261 Substrate. {ECO:0000269|PubMed:16051266}. FT BINDING 399 399 Substrate. {ECO:0000269|PubMed:16051266}. FT VAR_SEQ 30 85 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_042557. FT VAR_SEQ 113 156 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043288. FT VAR_SEQ 380 403 VRRKQQMAVVSKMPFVPTNYYTLK -> LPSGPCF (in FT isoform 4). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_045418. FT VARIANT 42 42 H -> R (in NKH; dbSNP:rs121964983). FT {ECO:0000269|PubMed:9600239}. FT /FTId=VAR_007951. FT VARIANT 47 47 G -> R (in NKH; dbSNP:rs121964982). FT {ECO:0000269|PubMed:8005589}. FT /FTId=VAR_007952. FT VARIANT 145 145 N -> I (in NKH; loss of FT aminomethyltransferase activity; FT dbSNP:rs386833682). FT {ECO:0000269|PubMed:11286506, FT ECO:0000269|PubMed:16051266}. FT /FTId=VAR_016847. FT VARIANT 211 211 E -> K (in NKH; dbSNP:rs116192290). FT {ECO:0000269|PubMed:10873393}. FT /FTId=VAR_016848. FT VARIANT 265 265 R -> C (in NKH; dbSNP:rs779483959). FT {ECO:0000269|PubMed:26371980}. FT /FTId=VAR_074107. FT VARIANT 269 269 G -> D (in NKH; decreased FT aminomethyltransferase activity; FT dbSNP:rs121964981). FT {ECO:0000269|PubMed:16051266, FT ECO:0000269|PubMed:8005589}. FT /FTId=VAR_007953. FT VARIANT 276 276 D -> H (in NKH; dbSNP:rs121964984). FT {ECO:0000269|PubMed:9621520}. FT /FTId=VAR_007954. FT VARIANT 320 320 R -> H (in NKH; loss of FT aminomethyltransferase activity; FT dbSNP:rs121964985). FT {ECO:0000269|PubMed:10873393, FT ECO:0000269|PubMed:11286506, FT ECO:0000269|PubMed:16051266, FT ECO:0000269|PubMed:8005589}. FT /FTId=VAR_007955. FT MUTAGEN 129 129 D->A,N: Loss of aminomethyltransferase FT activity. {ECO:0000269|PubMed:16051266}. FT CONFLICT 95 95 V -> C (in Ref. 2; BAA03512). FT {ECO:0000305}. FT HELIX 39 44 {ECO:0000244|PDB:1WSR}. FT STRAND 48 52 {ECO:0000244|PDB:1WSR}. FT STRAND 55 60 {ECO:0000244|PDB:1WSR}. FT HELIX 65 74 {ECO:0000244|PDB:1WSR}. FT STRAND 75 80 {ECO:0000244|PDB:1WSR}. FT STRAND 84 91 {ECO:0000244|PDB:1WSR}. FT HELIX 94 101 {ECO:0000244|PDB:1WSR}. FT STRAND 102 104 {ECO:0000244|PDB:1WSR}. FT STRAND 113 120 {ECO:0000244|PDB:1WSR}. FT STRAND 126 134 {ECO:0000244|PDB:1WSR}. FT STRAND 138 144 {ECO:0000244|PDB:1WSR}. FT HELIX 146 148 {ECO:0000244|PDB:1WSR}. FT HELIX 149 165 {ECO:0000244|PDB:1WSR}. FT STRAND 171 174 {ECO:0000244|PDB:1WSR}. FT STRAND 178 184 {ECO:0000244|PDB:1WSR}. FT HELIX 187 192 {ECO:0000244|PDB:1WSR}. FT HELIX 199 201 {ECO:0000244|PDB:1WSR}. FT STRAND 206 212 {ECO:0000244|PDB:1WSR}. FT STRAND 215 222 {ECO:0000244|PDB:1WSR}. FT STRAND 225 235 {ECO:0000244|PDB:1WSR}. FT HELIX 237 248 {ECO:0000244|PDB:1WSR}. FT STRAND 253 255 {ECO:0000244|PDB:1WSR}. FT HELIX 258 267 {ECO:0000244|PDB:1WSR}. FT TURN 273 275 {ECO:0000244|PDB:1WSR}. FT TURN 283 287 {ECO:0000244|PDB:1WSR}. FT HELIX 289 291 {ECO:0000244|PDB:1WSR}. FT HELIX 294 299 {ECO:0000244|PDB:1WSR}. FT HELIX 305 312 {ECO:0000244|PDB:1WSR}. FT STRAND 319 328 {ECO:0000244|PDB:1WSR}. FT STRAND 335 337 {ECO:0000244|PDB:1WSR}. FT STRAND 343 353 {ECO:0000244|PDB:1WSR}. FT TURN 354 357 {ECO:0000244|PDB:1WSR}. FT STRAND 358 365 {ECO:0000244|PDB:1WSR}. FT HELIX 367 369 {ECO:0000244|PDB:1WSR}. FT STRAND 375 380 {ECO:0000244|PDB:1WSR}. FT STRAND 383 390 {ECO:0000244|PDB:1WSR}. SQ SEQUENCE 403 AA; 43946 MW; 218DC9EEADFA9102 CRC64; MQRAVSVVAR LGFRLQAFPP ALCRPLSCAQ EVLRRTPLYD FHLAHGGKMV AFAGWSLPVQ YRDSHTDSHL HTRQHCSLFD VSHMLQTKIL GSDRVKLMES LVVGDIAELR PNQGTLSLFT NEAGGILDDL IVTNTSEGHL YVVSNAGCWE KDLALMQDKV RELQNQGRDV GLEVLDNALL ALQGPTAAQV LQAGVADDLR KLPFMTSAVM EVFGVSGCRV TRCGYTGEDG VEISVPVAGA VHLATAILKN PEVKLAGLAA RDSLRLEAGL CLYGNDIDEH TTPVEGSLSW TLGKRRRAAM DFPGAKVIVP QLKGRVQRRR VGLMCEGAPM RAHSPILNME GTKIGTVTSG CPSPSLKKNV AMGYVPCEYS RPGTMLLVEV RRKQQMAVVS KMPFVPTNYY TLK //