MOXD1_HUMAN
ID MOXD1_HUMAN Reviewed; 613 AA.
AC Q6UVY6; Q5THU6; Q8NC97; Q8WV49; Q9H4M6; Q9Y4U3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=DBH-like monooxygenase protein 1;
DE EC=1.14.17.-;
DE AltName: Full=Monooxygenase X;
DE Flags: Precursor;
GN Name=MOXD1; Synonyms=MOX; ORFNames=UNQ2493/PRO5780;
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] (ISOFORM 2), TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Fibroblast;
RX PubMed=9751809; DOI=10.1016/s0378-1119(98)00344-8;
RA Chambers K.J., Tonkin L.A., Chang E., Shelton D.N., Linskens M.H.,
RA Funk W.D.;
RT "Identification and cloning of a sequence homologue of dopamine beta-
RT hydroxylase.";
RL Gene 218:111-120(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-539.
RC TISSUE=Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-613 (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-613.
RC TISSUE=Brain;
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 [8]
RP IDENTIFICATION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15337741; DOI=10.1074/jbc.m407486200;
RA Xin X., Mains R.E., Eipper B.A.;
RT "Monooxygenase X, a member of the copper-dependent monooxygenase family
RT localized to the endoplasmic reticulum.";
RL J. Biol. Chem. 279:48159-48167(2004).
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC Q6UVY6; O76003: GLRX3; NbExp=7; IntAct=EBI-7134667, EBI-374781;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=Q6UVY6-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q6UVY6-2; Sequence=VSP_028288, VSP_028289;
CC -!- TISSUE SPECIFICITY: Highly expressed in lung, kidney, brain and spinal
CC cord. {ECO:0000269|PubMed:15337741, ECO:0000269|PubMed:9751809}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver and fetal brain.
CC {ECO:0000269|PubMed:15337741}.
CC -!- INDUCTION: By replicative senescence. {ECO:0000269|PubMed:9751809}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major.
CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC monooxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11263.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY007239; AAG09636.1; -; mRNA.
DR EMBL; AY359094; AAQ89452.1; -; mRNA.
DR EMBL; AL357034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL023578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48033.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48034.1; -; Genomic_DNA.
DR EMBL; BC018756; AAH18756.1; -; mRNA.
DR EMBL; AK074879; BAC11263.1; ALT_INIT; mRNA.
DR EMBL; AL080058; CAB45692.1; -; mRNA.
DR CCDS; CCDS5152.2; -. [Q6UVY6-1]
DR PIR; T12460; T12460.
DR RefSeq; NP_056344.2; NM_015529.3. [Q6UVY6-1]
DR AlphaFoldDB; Q6UVY6; -.
DR SMR; Q6UVY6; -.
DR BioGRID; 117478; 40.
DR IntAct; Q6UVY6; 21.
DR MINT; Q6UVY6; -.
DR STRING; 9606.ENSP00000356940; -.
DR GlyGen; Q6UVY6; 4 sites.
DR iPTMnet; Q6UVY6; -.
DR PhosphoSitePlus; Q6UVY6; -.
DR BioMuta; MOXD1; -.
DR DMDM; 74749373; -.
DR EPD; Q6UVY6; -.
DR jPOST; Q6UVY6; -.
DR MassIVE; Q6UVY6; -.
DR MaxQB; Q6UVY6; -.
DR PaxDb; Q6UVY6; -.
DR PeptideAtlas; Q6UVY6; -.
DR PRIDE; Q6UVY6; -.
DR ProteomicsDB; 67438; -. [Q6UVY6-1]
DR ProteomicsDB; 67439; -. [Q6UVY6-2]
DR Antibodypedia; 32922; 144 antibodies from 22 providers.
DR DNASU; 26002; -.
DR Ensembl; ENST00000336749.3; ENSP00000336998.3; ENSG00000079931.15. [Q6UVY6-2]
DR Ensembl; ENST00000367963.8; ENSP00000356940.3; ENSG00000079931.15. [Q6UVY6-1]
DR GeneID; 26002; -.
DR KEGG; hsa:26002; -.
DR MANE-Select; ENST00000367963.8; ENSP00000356940.3; NM_015529.4; NP_056344.2.
DR UCSC; uc003qde.4; human. [Q6UVY6-1]
DR CTD; 26002; -.
DR DisGeNET; 26002; -.
DR GeneCards; MOXD1; -.
DR HGNC; HGNC:21063; MOXD1.
DR HPA; ENSG00000079931; Tissue enhanced (endometrium, smooth muscle).
DR MIM; 609000; gene.
DR neXtProt; NX_Q6UVY6; -.
DR OpenTargets; ENSG00000079931; -.
DR PharmGKB; PA134979178; -.
DR VEuPathDB; HostDB:ENSG00000079931; -.
DR eggNOG; KOG3568; Eukaryota.
DR GeneTree; ENSGT00530000063085; -.
DR HOGENOM; CLU_017939_4_1_1; -.
DR InParanoid; Q6UVY6; -.
DR OMA; SMDTLYW; -.
DR OrthoDB; 1472750at2759; -.
DR PhylomeDB; Q6UVY6; -.
DR TreeFam; TF320698; -.
DR PathwayCommons; Q6UVY6; -.
DR SignaLink; Q6UVY6; -.
DR BioGRID-ORCS; 26002; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; MOXD1; human.
DR GeneWiki; Monooxygenase_DBH-like_1; -.
DR GenomeRNAi; 26002; -.
DR Pharos; Q6UVY6; Tbio.
DR PRO; PR:Q6UVY6; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q6UVY6; protein.
DR Bgee; ENSG00000079931; Expressed in ventricular zone and 154 other tissues.
DR ExpressionAtlas; Q6UVY6; baseline and differential.
DR Genevisible; Q6UVY6; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:CACAO.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004500; F:dopamine beta-monooxygenase activity; IBA:GO_Central.
DR GO; GO:0042420; P:dopamine catabolic process; IBA:GO_Central.
DR GO; GO:0042421; P:norepinephrine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006589; P:octopamine biosynthetic process; IBA:GO_Central.
DR CDD; cd09631; DOMON_DOH; 1.
DR Gene3D; 2.60.120.230; -; 1.
DR Gene3D; 2.60.120.310; -; 1.
DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR InterPro; IPR000323; Cu2_ascorb_mOase_N.
DR InterPro; IPR036939; Cu2_ascorb_mOase_N_sf.
DR InterPro; IPR024548; Cu2_monoox_C.
DR InterPro; IPR000945; DBH-like.
DR InterPro; IPR045266; DOH_DOMON.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR028463; MOXD1.
DR InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR InterPro; IPR028460; Tbh/DBH.
DR PANTHER; PTHR10157; PTHR10157; 1.
DR PANTHER; PTHR10157:SF28; PTHR10157:SF28; 1.
DR Pfam; PF03712; Cu2_monoox_C; 1.
DR Pfam; PF01082; Cu2_monooxygen; 1.
DR PRINTS; PR00767; DBMONOXGNASE.
DR SMART; SM00664; DoH; 1.
DR SUPFAM; SSF49742; SSF49742; 2.
DR PROSITE; PS50836; DOMON; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Copper; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..613
FT /note="DBH-like monooxygenase protein 1"
FT /id="PRO_0000305217"
FT TOPO_DOM 20..592
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 35..148
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT ACT_SITE 203
FT /evidence="ECO:0000255"
FT ACT_SITE 389
FT /evidence="ECO:0000255"
FT BINDING 235
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 205..257
FT /evidence="ECO:0000250"
FT DISULFID 242..269
FT /evidence="ECO:0000250"
FT DISULFID 364..480
FT /evidence="ECO:0000250"
FT DISULFID 368..550
FT /evidence="ECO:0000250"
FT DISULFID 443..465
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9751809"
FT /id="VSP_028288"
FT VAR_SEQ 27..87
FT /note="HRTLLDSEGKYWLGWSQRGSQIAFRLQVRTAGYVGFGFSPTGAMASADIVVG
FT GVAHGRPYL -> MNSFLSVFRYPDFSFPYFP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9751809"
FT /id="VSP_028289"
FT VARIANT 488
FT /note="E -> Q (in dbSNP:rs36075540)"
FT /id="VAR_035185"
FT VARIANT 539
FT /note="K -> E (in dbSNP:rs17851680)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035186"
FT CONFLICT 148
FT /note="H -> Y (in Ref. 6; BAC11263)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="N -> Y (in Ref. 7; CAB45692)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="P -> L (in Ref. 1; AAG09636)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 69652 MW; 57B407655A8294BB CRC64;
MCCWPLLLLW GLLPGTAAGG SGRTYPHRTL LDSEGKYWLG WSQRGSQIAF RLQVRTAGYV
GFGFSPTGAM ASADIVVGGV AHGRPYLQDY FTNANRELKK DAQQDYHLEY AMENSTHTII
EFTRELHTCD INDKSITDST VRVIWAYHHE DAGEAGPKYH DSNRGTKSLR LLNPEKTSVL
STALPYFDLV NQDVPIPNKD TTYWCQMFKI PVFQEKHHVI KVEPVIQRGH ESLVHHILLY
QCSNNFNDSV LESGHECYHP NMPDAFLTCE TVIFAWAIGG EGFSYPPHVG LSLGTPLDPH
YVLLEVHYDN PTYEEGLIDN SGLRLFYTMD IRKYDAGVIE AGLWVSLFHT IPPGMPEFQS
EGHCTLECLE EALEAEKPSG IHVFAVLLHA HLAGRGIRLR HFRKGKEMKL LAYDDDFDFN
FQEFQYLKEE QTILPGDNLI TECRYNTKDR AEMTWGGLST RSEMCLSYLL YYPRINLTRC
ASIPDIMEQL QFIGVKEIYR PVTTWPFIIK SPKQYKNLSF MDAMNKFKWT KKEGLSFNKL
VLSLPVNVRC SKTDNAEWSI QGMTALPPDI ERPYKAEPLV CGTSSSSSLH RDFSINLLVC
LLLLSCTLST KSL
