ENOF1_HUMAN
ID ENOF1_HUMAN Reviewed; 443 AA.
AC Q7L5Y1; A6NMP3; A8K9R5; B3KSL6; B3KXE4; D3DUH0; Q15407; Q15594; Q15595;
AC Q6ZS08; Q9HAS5; Q9HAS6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Mitochondrial enolase superfamily member 1;
DE EC=4.2.1.68 {ECO:0000269|PubMed:24697329};
DE AltName: Full=Antisense RNA to thymidylate synthase;
DE Short=rTS;
DE AltName: Full=L-fuconate dehydratase;
GN Name=ENOSF1; Synonyms=RTS, TYMSAS;
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 [GENOMIC DNA / MRNA] (ISOFORM 2), AND VARIANT THR-145.
RC TISSUE=Cervix carcinoma;
RX PubMed=8493092; DOI=10.1093/nar/21.8.1747;
RA Dolnick B.J.;
RT "Cloning and characterization of a naturally occurring antisense RNA to
RT human thymidylate synthase mRNA.";
RL Nucleic Acids Res. 21:1747-1752(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 23-443 (ISOFORM 3), AND VARIANT THR-145.
RC TISSUE=Cervix carcinoma;
RX PubMed=8764108;
RA Dolnick B.J., Black A.R.;
RT "Alternate splicing of the rTS gene product and its overexpression in a 5-
RT fluorouracil-resistant cell line.";
RL Cancer Res. 56:3207-3210(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5; 6 AND 7), AND
RP VARIANT THR-145.
RC TISSUE=Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-145.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [7]
RP ORIGINALLY PROPOSED FUNCTION.
RX PubMed=8869746; DOI=10.1016/0065-2571(95)00009-7;
RA Dolnick B.J., Black A.R., Winkler P.M., Schindler K., Hsueh C.-T.;
RT "rTS gene expression is associated with altered cell sensitivity to
RT thymidylate synthase inhibitors.";
RL Adv. Enzyme Regul. 36:165-180(1996).
RN [8]
RP ORIGINALLY PROPOSED FUNCTION.
RX PubMed=12084460; DOI=10.1016/s0925-4439(02)00081-9;
RA Chu J., Dolnick B.J.;
RT "Natural antisense (rTSalpha) RNA induces site-specific cleavage of
RT thymidylate synthase mRNA.";
RL Biochim. Biophys. Acta 1587:183-193(2002).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=16162288; DOI=10.1186/1471-2164-6-125;
RA Liang P., Nair J.R., Song L., McGuire J.J., Dolnick B.J.;
RT "Comparative genomic analysis reveals a novel mitochondrial isoform of
RT human rTS protein and unusual phylogenetic distribution of the rTS gene.";
RL BMC Genomics 6:125-125(2005).
RN [10]
RP PHOSPHORYLATION AT SER-148, AND SUMOYLATION.
RX PubMed=15994970; DOI=10.1158/0008-5472.can-05-0431;
RA Dolnick R., Wu Q., Angelino N.J., Stephanie L.V., Chow K.-C., Sufrin J.R.,
RA Dolnick B.J.;
RT "Enhancement of 5-fluorouracil sensitivity by an rTS signaling mimic in
RT H630 colon cancer cells.";
RL Cancer Res. 65:5917-5924(2005).
RN [11]
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 [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-440 IN COMPLEX WITH MAGNESIUM,
RP CATALYTIC ACTIVITY, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF 1-MET--HIS-27.
RX PubMed=24697329; DOI=10.1021/bi500349e;
RA Wichelecki D.J., Froese D.S., Kopec J., Muniz J.R., Yue W.W., Gerlt J.A.;
RT "Enzymatic and structural characterization of rTSgamma provides insights
RT into the function of rTSbeta.";
RL Biochemistry 53:2732-2738(2014).
CC -!- FUNCTION: Plays a role in the catabolism of L-fucose, a sugar that is
CC part of the carbohydrates that are attached to cellular glycoproteins.
CC Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by
CC the abstraction of the 2-proton to generate an enediolate intermediate
CC that is stabilized by the magnesium ion (PubMed:24697329).
CC {ECO:0000269|PubMed:24697329}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H2O;
CC Xref=Rhea:RHEA:22772, ChEBI:CHEBI:15377, ChEBI:CHEBI:21291,
CC ChEBI:CHEBI:37448; EC=4.2.1.68;
CC Evidence={ECO:0000269|PubMed:24697329};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24697329};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:24697329};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for L-fuconate {ECO:0000269|PubMed:24697329};
CC KM=3.0 mM for L-galactonate {ECO:0000269|PubMed:24697329};
CC KM=2.0 mM for D-arabinonate {ECO:0000269|PubMed:24697329};
CC KM=4.0 mM for L-arabinonate {ECO:0000269|PubMed:24697329};
CC KM=0.4 mM for D-ribonate {ECO:0000269|PubMed:24697329};
CC Note=kcat is 0.5 sec(-1) for L-fuconate. kcat is 0.3 sec(-1) for L-
CC galactonate. kcat is 0.3 sec(-1) for L-arabinonate. kcat is 0.04
CC sec(-1) for D-arabinonate. kcat is 0.002 sec(-1) for D-ribonate.;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16162288}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=rTSgamma;
CC IsoId=Q7L5Y1-1; Sequence=Displayed;
CC Name=2; Synonyms=rTSalpha;
CC IsoId=Q7L5Y1-2; Sequence=VSP_033311, VSP_033313;
CC Name=3;
CC IsoId=Q7L5Y1-3; Sequence=VSP_033312, VSP_033314;
CC Name=4;
CC IsoId=Q7L5Y1-4; Sequence=VSP_047153, VSP_047154;
CC Name=5;
CC IsoId=Q7L5Y1-5; Sequence=VSP_055243, VSP_047154;
CC Name=6;
CC IsoId=Q7L5Y1-6; Sequence=VSP_055242;
CC Name=7;
CC IsoId=Q7L5Y1-7; Sequence=VSP_055241;
CC -!- PTM: Could be sumoylated. {ECO:0000269|PubMed:15994970}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. ENOSF1 subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:8493092) identified as a gene coding
CC for an antisense RNA to thymidylate synthase, and was proposed to down-
CC regulate TYMS activity (PubMed:8869746), possibly by promoting the
CC degradation of TYMS mRNA via an antisense RNA-based mechanism
CC (PubMed:12084460). {ECO:0000305|PubMed:12084460,
CC ECO:0000305|PubMed:8493092, ECO:0000305|PubMed:8869746}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG29537.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA47471.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF305057; AAG29536.1; -; Genomic_DNA.
DR EMBL; X67098; CAA47472.1; -; mRNA.
DR EMBL; AF305057; AAG29537.1; ALT_INIT; Genomic_DNA.
DR EMBL; X67098; CAA47471.1; ALT_INIT; mRNA.
DR EMBL; X89602; CAA61761.1; -; mRNA.
DR EMBL; AK127818; BAC87148.1; -; mRNA.
DR EMBL; AK093873; BAG52778.1; -; mRNA.
DR EMBL; AK127219; BAG54456.1; -; mRNA.
DR EMBL; AK292780; BAF85469.1; -; mRNA.
DR EMBL; AP001178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471113; EAX01713.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01714.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01715.1; -; Genomic_DNA.
DR EMBL; BC001285; AAH01285.2; -; mRNA.
DR CCDS; CCDS11822.1; -. [Q7L5Y1-1]
DR CCDS; CCDS45821.1; -. [Q7L5Y1-2]
DR RefSeq; NP_001119595.1; NM_001126123.3.
DR RefSeq; NP_001305688.1; NM_001318759.1.
DR RefSeq; NP_001305689.1; NM_001318760.1. [Q7L5Y1-6]
DR RefSeq; NP_059982.2; NM_017512.5. [Q7L5Y1-1]
DR RefSeq; NP_974487.1; NM_202758.3.
DR RefSeq; XP_016881324.1; XM_017025835.1.
DR RefSeq; XP_016881325.1; XM_017025836.1.
DR PDB; 4A35; X-ray; 1.74 A; A=1-440.
DR PDBsum; 4A35; -.
DR AlphaFoldDB; Q7L5Y1; -.
DR SMR; Q7L5Y1; -.
DR BioGRID; 120716; 12.
DR IntAct; Q7L5Y1; 3.
DR STRING; 9606.ENSP00000345974; -.
DR GlyGen; Q7L5Y1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7L5Y1; -.
DR PhosphoSitePlus; Q7L5Y1; -.
DR BioMuta; ENOSF1; -.
DR DMDM; 74739173; -.
DR EPD; Q7L5Y1; -.
DR jPOST; Q7L5Y1; -.
DR MassIVE; Q7L5Y1; -.
DR MaxQB; Q7L5Y1; -.
DR PaxDb; Q7L5Y1; -.
DR PeptideAtlas; Q7L5Y1; -.
DR PRIDE; Q7L5Y1; -.
DR ProteomicsDB; 1550; -.
DR ProteomicsDB; 3646; -.
DR ProteomicsDB; 68814; -. [Q7L5Y1-1]
DR ProteomicsDB; 68815; -. [Q7L5Y1-2]
DR ProteomicsDB; 68816; -. [Q7L5Y1-3]
DR Antibodypedia; 21907; 157 antibodies from 23 providers.
DR DNASU; 55556; -.
DR Ensembl; ENST00000383578.7; ENSP00000373072.3; ENSG00000132199.20. [Q7L5Y1-2]
DR Ensembl; ENST00000647584.2; ENSP00000497230.2; ENSG00000132199.20. [Q7L5Y1-1]
DR GeneID; 55556; -.
DR KEGG; hsa:55556; -.
DR MANE-Select; ENST00000647584.2; ENSP00000497230.2; NM_017512.7; NP_059982.2.
DR UCSC; uc002kkt.4; human. [Q7L5Y1-1]
DR CTD; 55556; -.
DR DisGeNET; 55556; -.
DR GeneCards; ENOSF1; -.
DR HGNC; HGNC:30365; ENOSF1.
DR HPA; ENSG00000132199; Low tissue specificity.
DR MIM; 607427; gene.
DR neXtProt; NX_Q7L5Y1; -.
DR OpenTargets; ENSG00000132199; -.
DR PharmGKB; PA134897613; -.
DR VEuPathDB; HostDB:ENSG00000132199; -.
DR eggNOG; ENOG502QU7C; Eukaryota.
DR GeneTree; ENSGT00390000014290; -.
DR HOGENOM; CLU_030273_2_2_1; -.
DR InParanoid; Q7L5Y1; -.
DR OMA; SGAIDVC; -.
DR OrthoDB; 933480at2759; -.
DR PhylomeDB; Q7L5Y1; -.
DR TreeFam; TF300529; -.
DR PathwayCommons; Q7L5Y1; -.
DR SignaLink; Q7L5Y1; -.
DR BioGRID-ORCS; 55556; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; ENOSF1; human.
DR GenomeRNAi; 55556; -.
DR Pharos; Q7L5Y1; Tbio.
DR PRO; PR:Q7L5Y1; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q7L5Y1; protein.
DR Bgee; ENSG00000132199; Expressed in right uterine tube and 204 other tissues.
DR ExpressionAtlas; Q7L5Y1; baseline and differential.
DR Genevisible; Q7L5Y1; HS.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0050023; F:L-fuconate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR GO; GO:0044275; P:cellular carbohydrate catabolic process; IDA:UniProtKB.
DR CDD; cd03324; rTSbeta_L-fuconate_dehydratase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR034610; L-fuconate_dehydratase.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDF00111; L-fuconate_dehydratase; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isomerase; Lyase; Magnesium;
KW Metal-binding; Mitochondrion; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..443
FT /note="Mitochondrial enolase superfamily member 1"
FT /id="PRO_0000331652"
FT ACT_SITE 222
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT ACT_SITE 355
FT /evidence="ECO:0000255"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24697329"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24697329"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24697329"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 355..357
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8P3K2"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15994970"
FT VAR_SEQ 1..230
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055241"
FT VAR_SEQ 1..181
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055242"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8493092"
FT /id="VSP_033311"
FT VAR_SEQ 1..24
FT /note="MVRGRISRLSVRDVRFPTSLGGHG -> MVSADAMVSADAMVSADAMVSADA
FT MVSADAMVSADAMVSADAMVS (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047153"
FT VAR_SEQ 1..24
FT /note="MVRGRISRLSVRDVRFPTSLGGHG -> MVSADAMVSADAMVSADAMVSADA
FT MVSADAMVSADAMVSADAMVSADAMVSADAMVSADAMVSADAMVS (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055243"
FT VAR_SEQ 65..117
FT /note="VVCAVNALAHHVLNKDLKDIVGDFRGFYRQLTSDGQLRWIGPEKGVVHLATA
FT A -> DWSRKGRGAPGDSGRPKRGVGLVGQAGGKACLEVTCGHGSQDAGILHRFQVHH
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8764108"
FT /id="VSP_033312"
FT VAR_SEQ 103
FT /note="W -> MQKMESRGVELPSLWEKALKL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8493092"
FT /id="VSP_033313"
FT VAR_SEQ 118..443
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8764108"
FT /id="VSP_033314"
FT VAR_SEQ 293..306
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047154"
FT VARIANT 31
FT /note="D -> E (in dbSNP:rs34724061)"
FT /id="VAR_042933"
FT VARIANT 145
FT /note="M -> T (in dbSNP:rs2612086)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:8493092, ECO:0000269|PubMed:8764108,
FT ECO:0000269|Ref.5"
FT /id="VAR_042934"
FT VARIANT 428
FT /note="Y -> S (in dbSNP:rs2847620)"
FT /id="VAR_042935"
FT MUTAGEN 1..27
FT /note="Missing: Impairs protein solubility. Abolishes
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:24697329"
FT STRAND 5..15
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4A35"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:4A35"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:4A35"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:4A35"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 109..130
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:4A35"
FT TURN 153..158
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:4A35"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:4A35"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:4A35"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 227..241
FT /evidence="ECO:0007829|PDB:4A35"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:4A35"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 284..294
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:4A35"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:4A35"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:4A35"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 334..347
FT /evidence="ECO:0007829|PDB:4A35"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 361..375
FT /evidence="ECO:0007829|PDB:4A35"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:4A35"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:4A35"
FT STRAND 400..407
FT /evidence="ECO:0007829|PDB:4A35"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 420..426
FT /evidence="ECO:0007829|PDB:4A35"
FT TURN 428..430
FT /evidence="ECO:0007829|PDB:4A35"
FT HELIX 432..437
FT /evidence="ECO:0007829|PDB:4A35"
SQ SEQUENCE 443 AA; 49786 MW; 82BEDAC229D1A729 CRC64;
MVRGRISRLS VRDVRFPTSL GGHGADAMHT DPDYSAAYVV IETDAEDGIK GCGITFTLGK
GTEVVVCAVN ALAHHVLNKD LKDIVGDFRG FYRQLTSDGQ LRWIGPEKGV VHLATAAVLN
AVWDLWAKQE GKPVWKLLVD MDPRMLVSCI DFRYITDVLT EEDALEILQK GQIGKKEREK
QMLAQGYPAY TTSCAWLGYS DDTLKQLCAQ ALKDGWTRFK VKVGADLQDD MRRCQIIRDM
IGPEKTLMMD ANQRWDVPEA VEWMSKLAKF KPLWIEEPTS PDDILGHATI SKALVPLGIG
IATGEQCHNR VIFKQLLQAK ALQFLQIDSC RLGSVNENLS VLLMAKKFEI PVCPHAGGVG
LCELVQHLII FDYISVSASL ENRVCEYVDH LHEHFKYPVM IQRASYMPPK DPGYSTEMKE
ESVKKHQYPD GEVWKKLLPA QEN
