NDST3_HUMAN
ID NDST3_HUMAN Reviewed; 873 AA.
AC O95803; B4DI67; Q4W5C1; Q4W5D0; Q6UWC5; Q9UP21;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3 {ECO:0000305};
DE AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 3;
DE Short=NDST-3;
DE Short=hNDST-3;
DE AltName: Full=N-heparan sulfate sulfotransferase 3;
DE Short=N-HSST 3;
DE Includes:
DE RecName: Full=Heparan sulfate N-deacetylase NDST3 {ECO:0000305};
DE EC=3.-.-.- {ECO:0000269|PubMed:9915799};
DE Includes:
DE RecName: Full=[heparan sulfate]-glucosamine N-sulfotransferase NDST3 {ECO:0000305};
DE EC=2.8.2.8 {ECO:0000269|PubMed:9915799};
GN Name=NDST3 {ECO:0000312|HGNC:HGNC:7682}; Synonyms=HSST3;
GN ORFNames=UNQ2544/PRO4998;
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 1), FUNCTION, TISSUE SPECIFICITY, AND
RP CATALYTIC ACTIVITY.
RC TISSUE=Brain;
RX PubMed=9915799; DOI=10.1074/jbc.274.5.2690;
RA Aikawa J., Esko J.D.;
RT "Molecular cloning and expression of a third member of the heparan
RT sulfate/heparin GlcNAc N-deacetylase/ N-sulfotransferase family.";
RL J. Biol. Chem. 274:2690-2695(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Sakakibara Y., Sanematsu F., Takami Y., Yanagisawa K., Nakayama T.,
RA Suiko M., Liu M.-C.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Corpus callosum;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 VARIANT [LARGE SCALE ANALYSIS] GLN-264.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Essential bifunctional enzyme that catalyzes both the N-
CC deacetylation and the N-sulfation of glucosamine (GlcNAc) of the
CC glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA
CC disaccharide repeating sugar backbone to make N-sulfated heparosan, a
CC prerequisite substrate for later modifications in heparin biosynthesis.
CC Has high deacetylase activity but low sulfotransferase activity.
CC {ECO:0000269|PubMed:9915799}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC sulfate](n) = adenosine 3',5'-bisphosphate + 2 H(+) + N-sulfo-alpha-
CC D-glucosaminyl-[heparan sulfate](n); Xref=Rhea:RHEA:21980, Rhea:RHEA-
CC COMP:9830, Rhea:RHEA-COMP:14602, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388,
CC ChEBI:CHEBI:140572; EC=2.8.2.8;
CC Evidence={ECO:0000269|PubMed:9915799};
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000269|PubMed:9915799}.
CC -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC {ECO:0000269|PubMed:9915799}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95803-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95803-2; Sequence=VSP_017405, VSP_017406;
CC Name=3;
CC IsoId=O95803-3; Sequence=VSP_054350, VSP_054351, VSP_054352;
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, liver, fetal and adult
CC lung, adult pancreas, placenta, fetal spleen and fetal thymus. Not
CC detected in adult/ fetal heart and skeletal muscle.
CC {ECO:0000269|PubMed:9915799}.
CC -!- MISCELLANEOUS: The presence of 4 different heparan sulfate N-
CC deacetylase/N-sulfotransferase enzymes in mammals, as well as
CC differences in their enzyme activity suggest that some initiate heparan
CC sulfate modification/sulfation reactions, whereas other later on fill
CC in or extend already modified heparan sulfate sequences.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC {ECO:0000305}.
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DR EMBL; AF074924; AAD15978.1; -; mRNA.
DR EMBL; AF076605; AAD46061.1; -; mRNA.
DR EMBL; AY358852; AAQ89211.1; -; mRNA.
DR EMBL; AK295439; BAG58379.1; -; mRNA.
DR EMBL; AC096762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108201; AAY41001.1; -; Genomic_DNA.
DR EMBL; AC110999; AAY41056.1; -; Genomic_DNA.
DR EMBL; AC116639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109309; AAI09310.1; -; mRNA.
DR EMBL; BC109310; AAI09311.1; -; mRNA.
DR CCDS; CCDS3708.1; -. [O95803-1]
DR RefSeq; NP_004775.1; NM_004784.2. [O95803-1]
DR RefSeq; XP_006714479.1; XM_006714416.3. [O95803-1]
DR AlphaFoldDB; O95803; -.
DR SMR; O95803; -.
DR BioGRID; 114751; 8.
DR STRING; 9606.ENSP00000296499; -.
DR GlyGen; O95803; 6 sites.
DR iPTMnet; O95803; -.
DR PhosphoSitePlus; O95803; -.
DR BioMuta; NDST3; -.
DR jPOST; O95803; -.
DR MassIVE; O95803; -.
DR PaxDb; O95803; -.
DR PeptideAtlas; O95803; -.
DR PRIDE; O95803; -.
DR ProteomicsDB; 4279; -.
DR ProteomicsDB; 51059; -. [O95803-1]
DR ProteomicsDB; 51060; -. [O95803-2]
DR Antibodypedia; 26593; 128 antibodies from 18 providers.
DR DNASU; 9348; -.
DR Ensembl; ENST00000296499.6; ENSP00000296499.5; ENSG00000164100.9. [O95803-1]
DR GeneID; 9348; -.
DR KEGG; hsa:9348; -.
DR MANE-Select; ENST00000296499.6; ENSP00000296499.5; NM_004784.3; NP_004775.1.
DR UCSC; uc003ibx.4; human. [O95803-1]
DR CTD; 9348; -.
DR DisGeNET; 9348; -.
DR GeneCards; NDST3; -.
DR HGNC; HGNC:7682; NDST3.
DR HPA; ENSG00000164100; Group enriched (brain, liver, lymphoid tissue, retina).
DR MIM; 603950; gene.
DR neXtProt; NX_O95803; -.
DR OpenTargets; ENSG00000164100; -.
DR PharmGKB; PA31488; -.
DR VEuPathDB; HostDB:ENSG00000164100; -.
DR eggNOG; KOG3703; Eukaryota.
DR GeneTree; ENSGT00940000160665; -.
DR HOGENOM; CLU_011357_2_0_1; -.
DR InParanoid; O95803; -.
DR OMA; VRDCCIN; -.
DR OrthoDB; 388292at2759; -.
DR PhylomeDB; O95803; -.
DR TreeFam; TF313193; -.
DR BioCyc; MetaCyc:HS09011-MON; -.
DR BRENDA; 2.8.2.8; 2681.
DR PathwayCommons; O95803; -.
DR Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR BioGRID-ORCS; 9348; 12 hits in 1067 CRISPR screens.
DR ChiTaRS; NDST3; human.
DR GeneWiki; NDST3; -.
DR GenomeRNAi; 9348; -.
DR Pharos; O95803; Tbio.
DR PRO; PR:O95803; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O95803; protein.
DR Bgee; ENSG00000164100; Expressed in buccal mucosa cell and 90 other tissues.
DR Genevisible; O95803; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0102140; F:heparan sulfate N-deacetylase activity; IDA:UniProtKB.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR021930; Heparan_SO4_deacetylase.
DR InterPro; IPR037359; NST/OST.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR10605; PTHR10605; 1.
DR Pfam; PF12062; HSNSD; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Hydrolase; Membrane; Multifunctional enzyme; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..873
FT /note="Bifunctional heparan sulfate N-deacetylase/N-
FT sulfotransferase 3"
FT /id="PRO_0000225659"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..873
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 36..589
FT /note="Heparan sulfate N-deacetylase 3"
FT REGION 590..873
FT /note="Heparan sulfate N-sulfotransferase 3"
FT ACT_SITE 605
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000250"
FT BINDING 605..609
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 703
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 824..828
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 794
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 809..819
FT /evidence="ECO:0000250"
FT VAR_SEQ 328..408
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054350"
FT VAR_SEQ 328..385
FT /note="ALLDTQNLLRAQITNFTFNLGFSGKFYHTGTEEEDEGDDCLLGSVDEFWWFP
FT HMWSHM -> VRLYFLKFQSSVHLPAGIQLSQFVLQLGYPGHGIYWESLGNLGLSLTLN
FT QLRRLCISI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_017405"
FT VAR_SEQ 386..873
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_017406"
FT VAR_SEQ 635..642
FT /note="QFFNRNNY -> YGFLPSPI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054351"
FT VAR_SEQ 643..873
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054352"
FT VARIANT 264
FT /note="H -> Q (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036131"
FT CONFLICT 8..17
FT /note="HRHFQRTVIL -> STEQLSKEPVISW (in Ref. 2; AAD46061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 873 AA; 100902 MW; 4DDE39257CAC0D36 CRC64;
MSFIMKLHRH FQRTVILLAT FCMVSIIISA YYLYSGYKQE NELSETASEV DCGDLQHLPY
QLMEVKAMKL FDASRTDPTV LVFVESQYSS LGQDIIMILE SSRFQYHIEI APGKGDLPVL
IDKMKGKYIL IIYENILKYI NMDSWNRSLL DKYCVEYGVG VIGFHKTSEK SVQSFQLKGF
PFSIYGNLAV KDCCINPHSP LIRVTKSSKL EKGSLPGTDW TVFQINHSAY QPVIFAKVKT
PENLSPSISK GAFYATIIHD LGLHDGIQRV LFGNNLNFWL HKLIFIDAIS FLSGKRLTLS
LDRYILVDID DIFVGKEGTR MNTNDVKALL DTQNLLRAQI TNFTFNLGFS GKFYHTGTEE
EDEGDDCLLG SVDEFWWFPH MWSHMQPHLF HNESSLVEQM ILNKKFALEH GIPTDMGYAV
APHHSGVYPV HVQLYEAWKK VWNIKITSTE EYPHLKPARY RRGFIHKNIM VLPRQTCGLF
THTIFYKEYP GGPKELDKSI QGGELFFTVV LNPISIFMTH LSNYGNDRLG LYTFVNLANF
VKSWTNLRLQ TLPPVQLAHK YFELFPDQKD PLWQNPCDDK RHRDIWSKEK TCDRLPKFLV
IGPQKTGTTA LYLFLVMHPS ILSNSPSPKT FEEVQFFNRN NYHRGIDWYM DFFPVPSNVT
TDFLFEKSAN YFHSEEAPKR AASLVPKAKI ITILIDPSDR AYSWYQHQRS HEDPAALKFS
FYEVISAGPR APSELRALQK RCLVPGWYAS HIERWLVYFP PFQLLIIDGQ QLRTDPATVM
DEVQKFLGVL PHYNYSEALT FDSHKGFWCQ LLEEGKTKCL GKSKGRKYPP MDSDSRTFLS
SYYRDHNVEL SKLLHKLGQP LPSWLRQELQ KVR
