MOCOS_HUMAN
ID MOCOS_HUMAN Reviewed; 888 AA.
AC Q96EN8; Q53GP5; Q8N3A4; Q9NWM7;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Molybdenum cofactor sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MCS {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MOS {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=hMCS;
DE EC=2.8.1.9 {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03050};
GN Name=MOCOS {ECO:0000255|HAMAP-Rule:MF_03050};
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], INVOLVEMENT IN XAN2, AND VARIANTS ARG-225 AND
RP ASN-703.
RX PubMed=11302742; DOI=10.1006/bbrc.2001.4719;
RA Ichida K., Matsumura T., Sakuma R., Hosoya T., Nishino T.;
RT "Mutation of human molybdenum cofactor sulfurase gene is responsible to
RT classical xanthinuria type II.";
RL Biochem. Biophys. Res. Commun. 282:1194-1200(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-170; GLY-184;
RP ARG-225; MET-358 AND ASN-703.
RC TISSUE=Liver;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-170; GLY-184;
RP ARG-225 AND MET-358.
RC TISSUE=Lung;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 95-888, AND VARIANTS ILE-170
RP GLY-184; ARG-225 AND MET-358.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16973608; DOI=10.1074/jbc.m607697200;
RA Havemeyer A., Bittner F., Wollers S., Mendel R., Kunze T., Clement B.;
RT "Identification of the missing component in the mitochondrial benzamidoxime
RT prodrug converting system as a novel molybdenum enzyme.";
RL J. Biol. Chem. 281:34796-34802(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-530, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-530, AND
RP IDENTIFICATION BY 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 [9]
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-528 AND SER-530, AND
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, 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 [12]
RP VARIANT XAN2 ILE-294.
RA Finckh U., Haddad M., Lukacs Z., Wagener C., Gal A.;
RT "Classical xanthinuria type 2 associated with a missense mutation in HMCS,
RT the gene encoding molybdenum cofactor sulfurase.";
RL (In) EUREGIO congress of clinical chemistry and laboratory medicine,
RL pp.36-37, Aachen (2003).
RN [13]
RP VARIANT XAN2 PRO-57.
RX PubMed=14624414; DOI=10.1016/s0026-0495(03)00272-5;
RA Yamamoto T., Moriwaki Y., Takahashi S., Tsutsumi Z., Tuneyoshi K.,
RA Matsui K., Cheng J., Hada T.;
RT "Identification of a new point mutation in the human molybdenum cofactor
RT sulferase gene that is responsible for xanthinuria type II.";
RL Metabolism 52:1501-1504(2003).
RN [14]
RP VARIANT XAN2 CYS-776.
RX PubMed=17368066; DOI=10.1016/j.ymgme.2007.02.005;
RA Peretz H., Naamati M.S., Levartovsky D., Lagziel A., Shani E., Horn I.,
RA Shalev H., Landau D.;
RT "Identification and characterization of the first mutation (Arg776Cys) in
RT the C-terminal domain of the human molybdenum cofactor sulfurase (HMCS)
RT associated with type II classical xanthinuria.";
RL Mol. Genet. Metab. 91:23-29(2007).
CC -!- FUNCTION: Sulfurates the molybdenum cofactor. Sulfation of molybdenum
CC is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase
CC (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and
CC 1 sulfur atom in active form. In vitro, the C-terminal domain is able
CC to reduce N-hydroxylated prodrugs, such as benzamidoxime.
CC {ECO:0000255|HAMAP-Rule:MF_03050, ECO:0000269|PubMed:16973608}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine +
CC thio-Mo-molybdopterin; Xref=Rhea:RHEA:42636, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:71302, ChEBI:CHEBI:82685; EC=2.8.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03050};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03050};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for benzamidoxime {ECO:0000269|PubMed:16973608};
CC Vmax=0.24 nmol/min/mg enzyme {ECO:0000269|PubMed:16973608};
CC -!- INTERACTION:
CC Q96EN8; Q96BM9: ARL8A; NbExp=3; IntAct=EBI-1220583, EBI-4401082;
CC Q96EN8; Q9NVD7: PARVA; NbExp=5; IntAct=EBI-1220583, EBI-747655;
CC -!- DISEASE: Xanthinuria 2 (XAN2) [MIM:603592]: A disorder characterized by
CC excretion of very large amounts of xanthine in the urine and a tendency
CC to form xanthine stones. Uric acid is strikingly diminished in serum
CC and urine. In addition, XAN2 patients cannot metabolize allopurinol
CC into oxypurinol due to dual deficiency of xanthine dehydrogenase and
CC aldehyde oxidase. {ECO:0000269|PubMed:11302742,
CC ECO:0000269|PubMed:14624414, ECO:0000269|PubMed:17368066,
CC ECO:0000269|Ref.12}. Note=The disease is caused by variants affecting
CC the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. MOCOS subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03050}.
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DR EMBL; AK000740; BAA91353.1; -; mRNA.
DR EMBL; AK222886; BAD96606.1; -; mRNA.
DR EMBL; AC023043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012079; AAH12079.1; -; mRNA.
DR EMBL; AL834481; CAD39140.1; -; mRNA.
DR CCDS; CCDS11919.1; -.
DR PIR; JC7680; JC7680.
DR RefSeq; NP_060417.2; NM_017947.2.
DR AlphaFoldDB; Q96EN8; -.
DR SMR; Q96EN8; -.
DR BioGRID; 120363; 39.
DR IntAct; Q96EN8; 26.
DR MINT; Q96EN8; -.
DR STRING; 9606.ENSP00000261326; -.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR GlyGen; Q96EN8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96EN8; -.
DR PhosphoSitePlus; Q96EN8; -.
DR BioMuta; MOCOS; -.
DR DMDM; 296438294; -.
DR CPTAC; CPTAC-979; -.
DR EPD; Q96EN8; -.
DR jPOST; Q96EN8; -.
DR MassIVE; Q96EN8; -.
DR MaxQB; Q96EN8; -.
DR PaxDb; Q96EN8; -.
DR PeptideAtlas; Q96EN8; -.
DR PRIDE; Q96EN8; -.
DR ProteomicsDB; 76426; -.
DR Antibodypedia; 41960; 54 antibodies from 19 providers.
DR DNASU; 55034; -.
DR Ensembl; ENST00000261326.6; ENSP00000261326.4; ENSG00000075643.6.
DR GeneID; 55034; -.
DR KEGG; hsa:55034; -.
DR MANE-Select; ENST00000261326.6; ENSP00000261326.4; NM_017947.4; NP_060417.4.
DR UCSC; uc002kzq.5; human.
DR CTD; 55034; -.
DR DisGeNET; 55034; -.
DR GeneCards; MOCOS; -.
DR HGNC; HGNC:18234; MOCOS.
DR HPA; ENSG00000075643; Tissue enhanced (adrenal gland, liver).
DR MalaCards; MOCOS; -.
DR MIM; 603592; phenotype.
DR MIM; 613274; gene.
DR neXtProt; NX_Q96EN8; -.
DR OpenTargets; ENSG00000075643; -.
DR Orphanet; 93602; Xanthinuria type II.
DR PharmGKB; PA134964534; -.
DR VEuPathDB; HostDB:ENSG00000075643; -.
DR eggNOG; KOG2142; Eukaryota.
DR GeneTree; ENSGT00940000157051; -.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; Q96EN8; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
DR PhylomeDB; Q96EN8; -.
DR TreeFam; TF105761; -.
DR PathwayCommons; Q96EN8; -.
DR Reactome; R-HSA-947581; Molybdenum cofactor biosynthesis.
DR SABIO-RK; Q96EN8; -.
DR SignaLink; Q96EN8; -.
DR BioGRID-ORCS; 55034; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; MOCOS; human.
DR GeneWiki; MOCOS; -.
DR GenomeRNAi; 55034; -.
DR Pharos; Q96EN8; Tbio.
DR PRO; PR:Q96EN8; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q96EN8; protein.
DR Bgee; ENSG00000075643; Expressed in secondary oocyte and 120 other tissues.
DR Genevisible; Q96EN8; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; IMP:UniProtKB.
DR GO; GO:0102867; F:molybdenum cofactor sulfurtransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; TAS:Reactome.
DR GO; GO:0043545; P:molybdopterin cofactor metabolic process; IMP:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR HAMAP; MF_03050; MOCOS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR028886; MoCo_sulfurase.
DR InterPro; IPR005303; MOSC_N.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 1: Evidence at protein level;
KW Disease variant; Molybdenum cofactor biosynthesis; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..888
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000249952"
FT DOMAIN 706..867
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 424
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 264
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT VARIANT 57
FT /note="A -> P (in XAN2; dbSNP:rs886037854)"
FT /evidence="ECO:0000269|PubMed:14624414"
FT /id="VAR_027528"
FT VARIANT 120
FT /note="S -> N (in dbSNP:rs3744900)"
FT /id="VAR_027529"
FT VARIANT 170
FT /note="T -> I (in dbSNP:rs623053)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_027530"
FT VARIANT 184
FT /note="S -> G (in dbSNP:rs540967)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_027531"
FT VARIANT 225
FT /note="H -> R (in dbSNP:rs623558)"
FT /evidence="ECO:0000269|PubMed:11302742,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_027532"
FT VARIANT 294
FT /note="T -> I (in XAN2; dbSNP:rs577279030)"
FT /evidence="ECO:0000269|Ref.12"
FT /id="VAR_027533"
FT VARIANT 358
FT /note="V -> M (in dbSNP:rs678560)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_027534"
FT VARIANT 495
FT /note="D -> N (in dbSNP:rs8088347)"
FT /id="VAR_027535"
FT VARIANT 541
FT /note="V -> L (in dbSNP:rs672924)"
FT /id="VAR_027536"
FT VARIANT 703
FT /note="H -> N (in dbSNP:rs594445)"
FT /evidence="ECO:0000269|PubMed:11302742,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_027537"
FT VARIANT 776
FT /note="R -> C (in XAN2; dbSNP:rs750896617)"
FT /evidence="ECO:0000269|PubMed:17368066"
FT /id="VAR_045899"
FT VARIANT 867
FT /note="V -> A (in dbSNP:rs1057251)"
FT /id="VAR_027538"
FT CONFLICT 119
FT /note="G -> E (in Ref. 2; BAD96606)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="K -> E (in Ref. 2; BAD96606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 888 AA; 98120 MW; 07DB9457516E8C06 CRC64;
MAGAAAESGR ELWTFAGSRD PSAPRLAYGY GPGSLRELRA REFSRLAGTV YLDHAGATLF
SQSQLESFTS DLMENTYGNP HSQNISSKLT HDTVEQVRYR ILAHFHTTAE DYTVIFTAGS
TAALKLVAEA FPWVSQGPES SGSRFCYLTD SHTSVVGMRN VTMAINVIST PVRPEDLWSA
EERSASASNP DCQLPHLFCY PAQSNFSGVR YPLSWIEEVK SGRLHPVSTP GKWFVLLDAA
SYVSTSPLDL SAHQADFVPI SFYKIFGFPT GLGALLVHNR AAPLLRKTYF GGGTASAYLA
GEDFYIPRQS VAQRFEDGTI SFLDVIALKH GFDTLERLTG GMENIKQHTF TLAQYTYVAL
SSLQYPNGAP VVRIYSDSEF SSPEVQGPII NFNVLDDKGN IIGYSQVDKM ASLYNIHLRT
GCFCNTGACQ RHLGISNEMV RKHFQAGHVC GDNMDLIDGQ PTGSVRISFG YMSTLDDVQA
FLRFIIDTRL HSSGDWPVPQ AHADTGETGA PSADSQADVI PAVMGRRSLS PQEDALTGSR
VWNNSSTVNA VPVAPPVCDV ARTQPTPSEK AAGVLEGALG PHVVTNLYLY PIKSCAAFEV
TRWPVGNQGL LYDRSWMVVN HNGVCLSQKQ EPRLCLIQPF IDLRQRIMVI KAKGMEPIEV
PLEENSERTQ IRQSRVCADR VSTYDCGEKI SSWLSTFFGR PCHLIKQSSN SQRNAKKKHG
KDQLPGTMAT LSLVNEAQYL LINTSSILEL HRQLNTSDEN GKEELFSLKD LSLRFRANII
INGKRAFEEE KWDEISIGSL RFQVLGPCHR CQMICIDQQT GQRNQHVFQK LSESRETKVN
FGMYLMHASL DLSSPCFLSV GSQVLPVLKE NVEGHDLPAS EKHQDVTS
