MOC2B_HUMAN
ID MOC2B_HUMAN Reviewed; 188 AA.
AC O96007; Q6IAI3;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Molybdopterin synthase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_03052};
DE EC=2.8.1.12 {ECO:0000255|HAMAP-Rule:MF_03052};
DE AltName: Full=MOCO1-B;
DE AltName: Full=Molybdenum cofactor synthesis protein 2 large subunit {ECO:0000255|HAMAP-Rule:MF_03052};
DE AltName: Full=Molybdenum cofactor synthesis protein 2B {ECO:0000255|HAMAP-Rule:MF_03052};
DE Short=MOCS2B {ECO:0000255|HAMAP-Rule:MF_03052};
DE AltName: Full=Molybdopterin-synthase large subunit;
DE Short=MPT synthase large subunit;
GN Name=MOCS2 {ECO:0000255|HAMAP-Rule:MF_03052}; Synonyms=MCBPE, MOCO1;
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 [MRNA], IDENTIFICATION OF BICISTRONIC GENE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10053003; DOI=10.1086/302295;
RA Stallmeyer B., Drugeon G., Reiss J., Haenni A.L., Mendel R.R.;
RT "Human molybdopterin synthase gene: identification of a bicistronic
RT transcript with overlapping reading frames.";
RL Am. J. Hum. Genet. 64:698-705(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9889283; DOI=10.1093/nar/27.3.854;
RA Sloan J., Kinghorn J.R., Unkles S.E.;
RT "The two subunits of human molybdopterin synthase: evidence for a
RT bicistronic messenger RNA with overlapping reading frames.";
RL Nucleic Acids Res. 27:854-858(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal gland;
RA Huang C., Huang Q., Wu T., Peng Y., Gu Y., Zhang L., Jiang C., Li Y.,
RA Han Z., Wang Y., Chen Z., Fu G.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum;
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 [8]
RP ENZYME ACTIVITY, FUNCTION, AND SUBUNIT.
RX PubMed=12732628; DOI=10.1074/jbc.m303092200;
RA Leimkuehler S., Freuer A., Araujo J.A., Rajagopalan K.V., Mendel R.R.;
RT "Mechanistic studies of human molybdopterin synthase reaction and
RT characterization of mutants identified in group B patients of molybdenum
RT cofactor deficiency.";
RL J. Biol. Chem. 278:26127-26134(2003).
RN [9]
RP ENZYME ACTIVITY, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15073332; DOI=10.1073/pnas.0308191101;
RA Matthies A., Rajagopalan K.V., Mendel R.R., Leimkuehler S.;
RT "Evidence for the physiological role of a rhodanese-like protein for the
RT biosynthesis of the molybdenum cofactor in humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5946-5951(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP 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 [18]
RP VARIANT MOCODB LYS-168.
RX PubMed=10053004; DOI=10.1086/302296;
RA Reiss J., Dorche C., Stallmeyer B., Mendel R.R., Cohen N., Zabot M.-T.;
RT "Human molybdopterin synthase gene: genomic structure and mutations in
RT molybdenum cofactor deficiency type B.";
RL Am. J. Hum. Genet. 64:706-711(1999).
RN [19]
RP INVOLVEMENT IN MOCODB.
RX PubMed=16021469; DOI=10.1007/s00439-005-1341-9;
RA Leimkuehler S., Charcosset M., Latour P., Dorche C., Kleppe S., Scaglia F.,
RA Szymczak I., Schupp P., Hahnewald R., Reiss J.;
RT "Ten novel mutations in the molybdenum cofactor genes MOCS1 and MOCS2 and
RT in vitro characterization of a MOCS2 mutation that abolishes the binding
RT ability of molybdopterin synthase.";
RL Hum. Genet. 117:565-570(2005).
RN [20]
RP INVOLVEMENT IN MOCODB.
RX PubMed=16737835; DOI=10.1016/j.ymgme.2006.04.008;
RA Hahnewald R., Leimkuehler S., Vilaseca A., Acquaviva-Bourdain C., Lenz U.,
RA Reiss J.;
RT "A novel MOCS2 mutation reveals coordinated expression of the small and
RT large subunit of molybdopterin synthase.";
RL Mol. Genet. Metab. 89:210-213(2006).
CC -!- FUNCTION: Catalytic subunit of the molybdopterin synthase complex, a
CC complex that catalyzes the conversion of precursor Z into
CC molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms
CC from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene
CC group. {ECO:0000255|HAMAP-Rule:MF_03052, ECO:0000269|PubMed:12732628,
CC ECO:0000269|PubMed:15073332}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2
CC [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly +
CC 4 H(+) + molybdopterin; Xref=Rhea:RHEA:26333, Rhea:RHEA-COMP:12160,
CC Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58698, ChEBI:CHEBI:59648, ChEBI:CHEBI:90619,
CC ChEBI:CHEBI:90778; EC=2.8.1.12; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03052, ECO:0000269|PubMed:12732628,
CC ECO:0000269|PubMed:15073332};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03052}.
CC -!- SUBUNIT: Heterotetramer; composed of 2 small (MOCS2A) and 2 large
CC (MOCS2B) subunits. {ECO:0000255|HAMAP-Rule:MF_03052}.
CC -!- INTERACTION:
CC O96007; O96033: MOCS2; NbExp=2; IntAct=EBI-723640, EBI-9056334;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-
CC Rule:MF_03052, ECO:0000269|PubMed:15073332}.
CC -!- TISSUE SPECIFICITY: Highest levels are found in heart and skeletal
CC muscle. Lower levels are present in brain, kidney and pancreas. Very
CC low levels are found in lung and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:10053003}.
CC -!- DISEASE: Molybdenum cofactor deficiency, complementation group B
CC (MOCODB) [MIM:252160]: An autosomal recessive metabolic disorder
CC characterized by neonatal onset of intractable seizures, opisthotonus,
CC and facial dysmorphism associated with hypouricemia and elevated
CC urinary sulfite levels. Affected individuals show severe neurologic
CC damage and often die in early childhood. {ECO:0000269|PubMed:10053004,
CC ECO:0000269|PubMed:16021469, ECO:0000269|PubMed:16737835}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the small subunit (MOCS2A) from an overlapping reading
CC frame. Expression of these 2 proteins are related since a mutation that
CC removes the start codon of the small subunit (MOCS2A) also impairs
CC expression of the large subunit (MOCS2B).
CC -!- SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03052}.
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DR EMBL; AF091871; AAD14599.1; -; mRNA.
DR EMBL; AF117815; AAD13297.1; -; mRNA.
DR EMBL; AF155659; AAF67478.1; -; mRNA.
DR EMBL; AK312887; BAG35735.1; -; mRNA.
DR EMBL; CR457172; CAG33453.1; -; mRNA.
DR EMBL; CH471123; EAW54874.1; -; Genomic_DNA.
DR EMBL; BC046097; AAH46097.1; -; mRNA.
DR CCDS; CCDS3958.1; -.
DR PIR; B59370; B59370.
DR RefSeq; NP_004522.1; NM_004531.4.
DR PDB; 4AP8; X-ray; 2.78 A; A/B/C/D=38-172.
DR PDB; 5MPO; X-ray; 2.43 A; C/D=27-179.
DR PDBsum; 4AP8; -.
DR PDBsum; 5MPO; -.
DR AlphaFoldDB; O96007; -.
DR SMR; O96007; -.
DR BioGRID; 110481; 15.
DR ComplexPortal; CPX-6341; Molybdopterin synthase complex.
DR CORUM; O96007; -.
DR IntAct; O96007; 6.
DR STRING; 9606.ENSP00000380157; -.
DR DrugBank; DB16628; Fosdenopterin.
DR GlyGen; O96007; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O96007; -.
DR PhosphoSitePlus; O96007; -.
DR BioMuta; MOCS2; -.
DR EPD; O96007; -.
DR jPOST; O96007; -.
DR MassIVE; O96007; -.
DR MaxQB; O96007; -.
DR PaxDb; O96007; -.
DR PeptideAtlas; O96007; -.
DR PRIDE; O96007; -.
DR ProteomicsDB; 51186; -.
DR Antibodypedia; 23330; 160 antibodies from 23 providers.
DR DNASU; 4338; -.
DR Ensembl; ENST00000396954.8; ENSP00000380157.3; ENSG00000164172.20.
DR GeneID; 4338; -.
DR KEGG; hsa:4338; -.
DR MANE-Select; ENST00000396954.8; ENSP00000380157.3; NM_004531.5; NP_004522.1.
DR UCSC; uc003joz.5; human.
DR CTD; 4338; -.
DR DisGeNET; 4338; -.
DR GeneCards; MOCS2; -.
DR GeneReviews; MOCS2; -.
DR HGNC; HGNC:7193; MOCS2.
DR HPA; ENSG00000164172; Low tissue specificity.
DR MalaCards; MOCS2; -.
DR MIM; 252160; phenotype.
DR MIM; 603708; gene.
DR neXtProt; NX_O96007; -.
DR OpenTargets; ENSG00000164172; -.
DR Orphanet; 308393; Sulfite oxidase deficiency due to molybdenum cofactor deficiency type B.
DR PharmGKB; PA30903; -.
DR VEuPathDB; HostDB:ENSG00000164172; -.
DR eggNOG; KOG3307; Eukaryota.
DR GeneTree; ENSGT00510000047669; -.
DR HOGENOM; CLU_089568_0_1_1; -.
DR InParanoid; O96007; -.
DR OMA; WPLQRVS; -.
DR OrthoDB; 1419096at2759; -.
DR PhylomeDB; O96007; -.
DR TreeFam; TF314334; -.
DR BioCyc; MetaCyc:HS09033-MON; -.
DR BRENDA; 2.8.1.12; 2681.
DR PathwayCommons; O96007; -.
DR Reactome; R-HSA-947581; Molybdenum cofactor biosynthesis.
DR SignaLink; O96007; -.
DR UniPathway; UPA00344; -.
DR BioGRID-ORCS; 4338; 20 hits in 1078 CRISPR screens.
DR ChiTaRS; MOCS2; human.
DR GeneWiki; MOCS2; -.
DR GenomeRNAi; 4338; -.
DR Pharos; O96007; Tbio.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O96007; protein.
DR Bgee; ENSG00000164172; Expressed in anterior cingulate cortex and 199 other tissues.
DR ExpressionAtlas; O96007; baseline and differential.
DR Genevisible; O96007; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0019008; C:molybdopterin synthase complex; IPI:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0030366; F:molybdopterin synthase activity; TAS:Reactome.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; TAS:Reactome.
DR CDD; cd00756; MoaE; 1.
DR Gene3D; 3.90.1170.40; -; 1.
DR HAMAP; MF_03052; MOC2B; 1.
DR InterPro; IPR036563; MoaE_sf.
DR InterPro; IPR028888; MOCS2B_euk.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR Pfam; PF02391; MoaE; 1.
DR SUPFAM; SSF54690; SSF54690; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; Molybdenum cofactor biosynthesis;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..188
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000163111"
FT BINDING 143..144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT BINDING 166..168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VARIANT 50
FT /note="T -> A (in dbSNP:rs2233213)"
FT /id="VAR_050091"
FT VARIANT 77
FT /note="T -> A (in dbSNP:rs2233215)"
FT /id="VAR_050092"
FT VARIANT 123
FT /note="H -> Y (in dbSNP:rs2233218)"
FT /id="VAR_050093"
FT VARIANT 168
FT /note="E -> K (in MOCODB; dbSNP:rs121908605)"
FT /evidence="ECO:0000269|PubMed:10053004"
FT /id="VAR_012765"
FT VARIANT 187
FT /note="N -> S (in dbSNP:rs2233221)"
FT /id="VAR_050094"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:5MPO"
FT HELIX 56..63
FT /evidence="ECO:0007829|PDB:5MPO"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:5MPO"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5MPO"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:5MPO"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:5MPO"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:5MPO"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:5MPO"
FT STRAND 132..143
FT /evidence="ECO:0007829|PDB:5MPO"
FT HELIX 144..161
FT /evidence="ECO:0007829|PDB:5MPO"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:5MPO"
SQ SEQUENCE 188 AA; 20944 MW; F405256D85621146 CRC64;
MSSLEISSSC FSLETKLPLS PPLVEDSAFE PSRKDMDEVE EKSKDVINFT AEKLSVDEVS
QLVISPLCGA ISLFVGTTRN NFEGKKVISL EYEAYLPMAE NEVRKICSDI RQKWPVKHIA
VFHRLGLVPV SEASIIIAVS SAHRAASLEA VSYAIDTLKA KVPIWKKEIY EESSTWKGNK
ECFWASNS
