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Methionine synthase reductase (MSR) (EC 1.16.1.8)

 MTRR_HUMAN              Reviewed;         698 AA.
Q9UBK8; O60471; Q32MA9; Q7Z4M8;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
16-JAN-2019, sequence version 4.
13-FEB-2019, entry version 184.
RecName: Full=Methionine synthase reductase;
Short=MSR;
EC=1.16.1.8 {ECO:0000269|PubMed:17892308};
Name=MTRR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B), AND
VARIANT LEU-175.
PubMed=10564814; DOI=10.1016/S0378-1119(99)00431-X;
Leclerc D., Odievre M.-H., Wu Q., Wilson A., Huizenga J., Rozen R.,
Scherer S.W., Gravel R.A.;
"Molecular cloning, expression and physical mapping of the human
methionine synthase reductase gene.";
Gene 240:75-88(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), VARIANT LEU-175, AND VARIANT
HMAE LEU-576 DEL.
PubMed=9501215; DOI=10.1073/pnas.95.6.3059;
Leclerc D., Wilson A., Dumas R., Gafuik C., Song D., Watkins D.,
Heng H.H.Q., Rommens J.M., Scherer S.W., Rosenblatt D.S., Gravel R.A.;
"Cloning and mapping of a cDNA for methionine synthase reductase, a
flavoprotein defective in patients with homocystinuria.";
Proc. Natl. Acad. Sci. U.S.A. 95:3059-3064(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION (ISOFORM A).
PubMed=18221906; DOI=10.1016/j.ymgme.2007.11.019;
Froese D.S., Wu X., Zhang J., Dumas R., Schoel W.M., Amrein M.,
Gravel R.A.;
"Restricted role for methionine synthase reductase defined by
subcellular localization.";
Mol. Genet. Metab. 94:68-77(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-189, VARIANT
[LARGE SCALE ANALYSIS] LEU-175, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 165-698 IN COMPLEX WITH FAD
AND NADP, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY,
AND FUNCTION.
PubMed=17892308; DOI=10.1021/bi701209p;
Wolthers K.R., Lou X., Toogood H.S., Leys D., Scrutton N.S.;
"Mechanism of coenzyme binding to human methionine synthase reductase
revealed through the crystal structure of the FNR-like module and
isothermal titration calorimetry.";
Biochemistry 46:11833-11844(2007).
[11]
VARIANTS HMAE VAL-54 DEL; MET-56; THR-129; ARG-405; ARG-487 AND
ARG-554, AND VARIANT VAL-333.
PubMed=10484769; DOI=10.1093/hmg/8.11.2009;
Wilson A., Leclerc D., Rosenblatt D.S., Gravel R.A.;
"Molecular basis for methionine synthase reductase deficiency in
patients belonging to the cblE complementation group of disorders in
folate/cobalamin metabolism.";
Hum. Mol. Genet. 8:2009-2016(1999).
[12]
INVOLVEMENT IN SUSCEPTIBILITY TO NTDFS, AND VARIANT MET-22.
PubMed=10444342; DOI=10.1006/mgme.1999.2879;
Wilson A., Platt R., Wu Q., Leclerc D., Christensen B., Yang H.,
Gravel R.A., Rozen R.;
"A common variant in methionine synthase reductase combined with low
cobalamin (vitamin B12) increases risk for spina bifida.";
Mol. Genet. Metab. 67:317-323(1999).
[13]
INVOLVEMENT IN SUSCEPTIBILITY TO NTDFS, AND VARIANT MET-22.
PubMed=12375236; DOI=10.1086/344209;
Doolin M.-T., Barbaux S., McDonnell M., Hoess K., Whitehead A.S.,
Mitchell L.E.;
"Maternal genetic effects, exerted by genes involved in homocysteine
remethylation, influence the risk of spina bifida.";
Am. J. Hum. Genet. 71:1222-1226(2002).
[14]
VARIANTS MET-22; LEU-175 AND ARG-350.
PubMed=15979034; DOI=10.1016/j.ymgme.2005.02.003;
O'Leary V.B., Mills J.L., Pangilinan F., Kirke P.N., Cox C.,
Conley M., Weiler A., Peng K., Shane B., Scott J.M.,
Parle-McDermott A., Molloy A.M., Brody L.C.;
"Analysis of methionine synthase reductase polymorphisms for neural
tube defects risk association.";
Mol. Genet. Metab. 85:220-227(2005).
-!- FUNCTION: Involved in the reductive regeneration of cob(I)alamin
(vitamin B12) cofactor required for the maintenance of methionine
synthase in a functional state. Necessary for utilization of
methylgroups from the folate cycle, thereby affecting
transgenerational epigenetic inheritance. Folate pathway donates
methyl groups necessary for cellular methylation and affects
different pathways such as DNA methylation, possibly explaining
the transgenerational epigenetic inheritance effects.
{ECO:0000269|PubMed:17892308}.
-!- CATALYTIC ACTIVITY:
Reaction=2 [methionine synthase]-methylcob(III)alamin + H(+) +
NADP(+) + 2 S-adenosyl-L-homocysteine = 2 [methionine synthase]-
cob(II)alamin + NADPH + 2 S-adenosyl-L-methionine;
Xref=Rhea:RHEA:23908, Rhea:RHEA-COMP:14714, Rhea:RHEA-
COMP:14715, ChEBI:CHEBI:15378, ChEBI:CHEBI:16304,
ChEBI:CHEBI:28115, ChEBI:CHEBI:57783, ChEBI:CHEBI:57856,
ChEBI:CHEBI:58349, ChEBI:CHEBI:59789; EC=1.16.1.8;
Evidence={ECO:0000269|PubMed:17892308};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:17892308};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:17892308};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.89 uM for NADPH {ECO:0000269|PubMed:17892308};
KM=3540 uM for NADH {ECO:0000269|PubMed:17892308};
-!- INTERACTION:
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-10319161, EBI-10172181;
-!- SUBCELLULAR LOCATION: Isoform B: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform A: Cytoplasm
{ECO:0000269|PubMed:18221906}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=B;
IsoId=Q9UBK8-2; Sequence=Displayed;
Name=A;
IsoId=Q9UBK8-1; Sequence=VSP_060027;
-!- TISSUE SPECIFICITY: Found in all tissues tested, particularly
abundant in skeletal muscle.
-!- DISEASE: Homocystinuria-megaloblastic anemia, cblE complementation
type (HMAE) [MIM:236270]: An autosomal recessive inborn error of
metabolism resulting from defects in the cobalamin-dependent
pathway that converts homocysteine to methionine. It causes
delayed psychomotor development, megaloblastic anemia,
homocystinuria, and hypomethioninemia. Cells from patients with
HMAE fail to incorporate methyltetrahydrofolate into methionine in
whole cells, but cell extracts show normal methionine synthase
activity in the presence of a reducing agent.
{ECO:0000269|PubMed:10484769, ECO:0000269|PubMed:9501215}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Neural tube defects, folate-sensitive (NTDFS)
[MIM:601634]: The most common NTDs are open spina bifida
(myelomeningocele) and anencephaly. {ECO:0000269|PubMed:10444342,
ECO:0000269|PubMed:12375236}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The hidden things
- Issue 166 of December 2014;
URL="https://web.expasy.org/spotlight/back_issues/166/";
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EMBL; AF121213; AAF17303.1; -; Genomic_DNA.
EMBL; AF121202; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121203; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121204; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121205; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121206; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121207; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121208; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121209; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121210; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121211; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121212; AAF17303.1; JOINED; Genomic_DNA.
EMBL; AF121214; AAF16876.1; -; mRNA.
EMBL; AF121213; AAF17304.1; -; Genomic_DNA.
EMBL; AF121202; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121203; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121204; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121205; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121206; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121207; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121208; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121209; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121210; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121211; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF121212; AAF17304.1; JOINED; Genomic_DNA.
EMBL; AF025794; AAC39667.1; -; mRNA.
EMBL; AC010346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC025174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC054816; AAH54816.2; -; mRNA.
EMBL; BC109216; AAI09217.1; -; mRNA.
CCDS; CCDS3874.1; -. [Q9UBK8-2]
CCDS; CCDS47190.1; -. [Q9UBK8-2]
RefSeq; NP_002445.2; NM_002454.2. [Q9UBK8-2]
RefSeq; NP_076915.2; NM_024010.2. [Q9UBK8-2]
UniGene; Hs.481551; -.
PDB; 2QTL; X-ray; 1.90 A; A=165-698.
PDB; 2QTZ; X-ray; 1.90 A; A=165-698.
PDBsum; 2QTL; -.
PDBsum; 2QTZ; -.
ProteinModelPortal; Q9UBK8; -.
SMR; Q9UBK8; -.
BioGrid; 110645; 14.
DIP; DIP-61183N; -.
IntAct; Q9UBK8; 8.
STRING; 9606.ENSP00000264668; -.
DrugBank; DB00115; Cyanocobalamin.
DrugBank; DB00200; Hydroxocobalamin.
DrugBank; DB00134; L-Methionine.
iPTMnet; Q9UBK8; -.
PhosphoSitePlus; Q9UBK8; -.
SwissPalm; Q9UBK8; -.
BioMuta; MTRR; -.
DMDM; 296439300; -.
EPD; Q9UBK8; -.
jPOST; Q9UBK8; -.
MaxQB; Q9UBK8; -.
PaxDb; Q9UBK8; -.
PeptideAtlas; Q9UBK8; -.
PRIDE; Q9UBK8; -.
ProteomicsDB; 83984; -.
ProteomicsDB; 83985; -. [Q9UBK8-2]
Ensembl; ENST00000264668; ENSP00000264668; ENSG00000124275. [Q9UBK8-1]
Ensembl; ENST00000440940; ENSP00000402510; ENSG00000124275. [Q9UBK8-2]
GeneID; 4552; -.
KEGG; hsa:4552; -.
UCSC; uc003jed.4; human. [Q9UBK8-2]
CTD; 4552; -.
DisGeNET; 4552; -.
EuPathDB; HostDB:ENSG00000124275.14; -.
GeneCards; MTRR; -.
GeneReviews; MTRR; -.
H-InvDB; HIX0031952; -.
HGNC; HGNC:7473; MTRR.
HPA; HPA038113; -.
MalaCards; MTRR; -.
MIM; 236270; phenotype.
MIM; 601634; phenotype.
MIM; 602568; gene.
neXtProt; NX_Q9UBK8; -.
OpenTargets; ENSG00000124275; -.
Orphanet; 2169; Methylcobalamin deficiency type cblE.
PharmGKB; PA31277; -.
eggNOG; KOG1158; Eukaryota.
eggNOG; COG0369; LUCA.
GeneTree; ENSGT00940000155822; -.
HOGENOM; HOG000007485; -.
HOVERGEN; HBG108376; -.
InParanoid; Q9UBK8; -.
KO; K00597; -.
OMA; ELVVDPW; -.
OrthoDB; 1436007at2759; -.
PhylomeDB; Q9UBK8; -.
TreeFam; TF105716; -.
BioCyc; MetaCyc:HS04756-MONOMER; -.
BRENDA; 1.16.1.8; 2681.
Reactome; R-HSA-156581; Methylation.
Reactome; R-HSA-1614635; Sulfur amino acid metabolism.
Reactome; R-HSA-196741; Cobalamin (Cbl, vitamin B12) transport and metabolism.
Reactome; R-HSA-3359467; Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
Reactome; R-HSA-3359469; Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
SABIO-RK; Q9UBK8; -.
EvolutionaryTrace; Q9UBK8; -.
GeneWiki; MTRR_(gene); -.
GenomeRNAi; 4552; -.
PRO; PR:Q9UBK8; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000124275; Expressed in 223 organ(s), highest expression level in corpus callosum.
ExpressionAtlas; Q9UBK8; baseline and differential.
Genevisible; Q9UBK8; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0030586; F:[methionine synthase] reductase activity; IDA:BHF-UCL.
GO; GO:0050444; F:aquacobalamin reductase (NADPH) activity; IDA:CACAO.
GO; GO:0071949; F:FAD binding; IDA:BHF-UCL.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
GO; GO:0010181; F:FMN binding; IDA:BHF-UCL.
GO; GO:0050661; F:NADP binding; TAS:UniProtKB.
GO; GO:0070402; F:NADPH binding; IDA:BHF-UCL.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:BHF-UCL.
GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
GO; GO:0016723; F:oxidoreductase activity, oxidizing metal ions, NAD or NADP as acceptor; IDA:UniProtKB.
GO; GO:0009235; P:cobalamin metabolic process; TAS:Reactome.
GO; GO:0006306; P:DNA methylation; ISS:UniProtKB.
GO; GO:0046655; P:folic acid metabolic process; IDA:BHF-UCL.
GO; GO:0043418; P:homocysteine catabolic process; IDA:BHF-UCL.
GO; GO:0050667; P:homocysteine metabolic process; IBA:GO_Central.
GO; GO:0009086; P:methionine biosynthetic process; IDA:BHF-UCL.
GO; GO:0006555; P:methionine metabolic process; TAS:UniProtKB.
GO; GO:1904042; P:negative regulation of cystathionine beta-synthase activity; IDA:BHF-UCL.
GO; GO:0055114; P:oxidation-reduction process; TAS:UniProtKB.
GO; GO:0033353; P:S-adenosylmethionine cycle; ISS:BHF-UCL.
Gene3D; 1.20.990.10; -; 1.
Gene3D; 3.40.50.360; -; 1.
Gene3D; 3.40.50.80; -; 1.
InterPro; IPR003097; CysJ-like_FAD-binding.
InterPro; IPR017927; FAD-bd_FR_type.
InterPro; IPR001094; Flavdoxin-like.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR029039; Flavoprotein-like_sf.
InterPro; IPR039261; FNR_nucleotide-bd.
InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00667; FAD_binding_1; 1.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00175; NAD_binding_1; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF52343; SSF52343; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Amino-acid biosynthesis;
Complete proteome; Cytoplasm; Disease mutation; FAD; Flavoprotein;
FMN; Methionine biosynthesis; NADP; Oxidoreductase; Phosphoprotein;
Polymorphism; Reference proteome; S-adenosyl-L-methionine.
CHAIN 1 698 Methionine synthase reductase.
/FTId=PRO_0000021785.
DOMAIN 5 147 Flavodoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
DOMAIN 271 533 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 93 124 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
NP_BIND 451 454 FAD. {ECO:0000269|PubMed:17892308}.
NP_BIND 487 490 FAD. {ECO:0000269|PubMed:17892308}.
NP_BIND 610 611 NADP. {ECO:0000269|PubMed:17892308}.
NP_BIND 624 626 NADP. {ECO:0000269|PubMed:17892308}.
REGION 166 247 Hinge.
BINDING 291 291 NADP. {ECO:0000269|PubMed:17892308}.
BINDING 659 659 NADP. {ECO:0000269|PubMed:17892308}.
BINDING 697 697 FAD. {ECO:0000269|PubMed:17892308}.
MOD_RES 171 171 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 189 189 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 1 M -> MGAASVRAGARLVEVALCSFTVTCLEVM (in
isoform A). {ECO:0000303|PubMed:10564814,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9501215}.
/FTId=VSP_060027.
VARIANT 22 22 I -> M (polymorphism; may increase risk
for spina bifida; dbSNP:rs1801394).
{ECO:0000269|PubMed:10444342,
ECO:0000269|PubMed:12375236,
ECO:0000269|PubMed:15979034}.
/FTId=VAR_012836.
VARIANT 54 54 Missing (in HMAE).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_012837.
VARIANT 56 56 V -> M (in HMAE; dbSNP:rs761061866).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_012838.
VARIANT 129 129 A -> T (in HMAE).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_012839.
VARIANT 175 175 S -> L (in dbSNP:rs1532268).
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10564814,
ECO:0000269|PubMed:15979034,
ECO:0000269|PubMed:9501215}.
/FTId=VAR_034595.
VARIANT 257 257 S -> T (in dbSNP:rs2303080).
/FTId=VAR_034596.
VARIANT 333 333 L -> V (in dbSNP:rs10064631).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_012840.
VARIANT 350 350 K -> R (in dbSNP:rs162036).
{ECO:0000269|PubMed:15979034}.
/FTId=VAR_034597.
VARIANT 405 405 C -> R (in HMAE).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_012841.
VARIANT 415 415 R -> C (in dbSNP:rs2287780).
/FTId=VAR_034598.
VARIANT 450 450 P -> R (in dbSNP:rs16879334).
/FTId=VAR_034599.
VARIANT 487 487 G -> R (in HMAE; dbSNP:rs137853061).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_012842.
VARIANT 515 515 A -> V (in dbSNP:rs16879355).
/FTId=VAR_056947.
VARIANT 554 554 G -> R (in HMAE).
{ECO:0000269|PubMed:10484769}.
/FTId=VAR_015731.
VARIANT 576 576 Missing (in HMAE).
{ECO:0000269|PubMed:9501215}.
/FTId=VAR_012843.
VARIANT 595 595 H -> Y (in dbSNP:rs10380).
/FTId=VAR_014944.
HELIX 235 237 {ECO:0000244|PDB:2QTL}.
STRAND 250 255 {ECO:0000244|PDB:2QTL}.
STRAND 274 283 {ECO:0000244|PDB:2QTL}.
STRAND 293 299 {ECO:0000244|PDB:2QTL}.
STRAND 312 316 {ECO:0000244|PDB:2QTL}.
HELIX 321 330 {ECO:0000244|PDB:2QTL}.
HELIX 334 336 {ECO:0000244|PDB:2QTL}.
STRAND 339 345 {ECO:0000244|PDB:2QTL}.
HELIX 366 372 {ECO:0000244|PDB:2QTL}.
HELIX 382 389 {ECO:0000244|PDB:2QTL}.
HELIX 395 405 {ECO:0000244|PDB:2QTL}.
HELIX 410 416 {ECO:0000244|PDB:2QTL}.
TURN 417 421 {ECO:0000244|PDB:2QTL}.
HELIX 424 430 {ECO:0000244|PDB:2QTL}.
HELIX 438 444 {ECO:0000244|PDB:2QTL}.
STRAND 451 454 {ECO:0000244|PDB:2QTL}.
TURN 459 461 {ECO:0000244|PDB:2QTL}.
STRAND 465 471 {ECO:0000244|PDB:2QTL}.
STRAND 474 476 {ECO:0000244|PDB:2QTL}.
STRAND 483 486 {ECO:0000244|PDB:2QTL}.
HELIX 488 496 {ECO:0000244|PDB:2QTL}.
TURN 497 500 {ECO:0000244|PDB:2QTL}.
STRAND 519 524 {ECO:0000244|PDB:2QTL}.
STRAND 540 543 {ECO:0000244|PDB:2QTL}.
HELIX 546 549 {ECO:0000244|PDB:2QTL}.
HELIX 550 565 {ECO:0000244|PDB:2QTL}.
STRAND 574 581 {ECO:0000244|PDB:2QTL}.
TURN 583 585 {ECO:0000244|PDB:2QTL}.
HELIX 590 598 {ECO:0000244|PDB:2QTL}.
STRAND 604 612 {ECO:0000244|PDB:2QTL}.
HELIX 625 631 {ECO:0000244|PDB:2QTL}.
HELIX 633 642 {ECO:0000244|PDB:2QTL}.
STRAND 646 652 {ECO:0000244|PDB:2QTL}.
HELIX 654 672 {ECO:0000244|PDB:2QTL}.
HELIX 676 688 {ECO:0000244|PDB:2QTL}.
STRAND 691 696 {ECO:0000244|PDB:2QTL}.
SEQUENCE 698 AA; 77674 MW; D4B394F0B24A07E5 CRC64;
MRRFLLLYAT QQGQAKAIAE EICEQAVVHG FSADLHCISE SDKYDLKTET APLVVVVSTT
GTGDPPDTAR KFVKEIQNQT LPVDFFAHLR YGLLGLGDSE YTYFCNGGKI IDKRLQELGA
RHFYDTGHAD DCVGLELVVE PWIAGLWPAL RKHFRSSRGQ EEISGALPVA SPASSRTDLV
KSELLHIESQ VELLRFDDSG RKDSEVLKQN AVNSNQSNVV IEDFESSLTR SVPPLSQASL
NIPGLPPEYL QVHLQESLGQ EESQVSVTSA DPVFQVPISK AVQLTTNDAI KTTLLVELDI
SNTDFSYQPG DAFSVICPNS DSEVQSLLQR LQLEDKREHC VLLKIKADTK KKGATLPQHI
PAGCSLQFIF TWCLEIRAIP KKAFLRALVD YTSDSAEKRR LQELCSKQGA ADYSRFVRDA
CACLLDLLLA FPSCQPPLSL LLEHLPKLQP RPYSCASSSL FHPGKLHFVF NIVEFLSTAT
TEVLRKGVCT GWLALLVASV LQPNIHASHE DSGKALAPKI SISPRTTNSF HLPDDPSIPI
IMVGPGTGIA PFIGFLQHRE KLQEQHPDGN FGAMWLFFGC RHKDRDYLFR KELRHFLKHG
ILTHLKVSFS RDAPVGEEEA PAKYVQDNIQ LHGQQVARIL LQENGHIYVC GDAKNMAKDV
HDALVQIISK EVGVEKLEAM KTLATLKEEK RYLQDIWS


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