ID H6ST1_HUMAN Reviewed; 411 AA. AC O60243; B4DEP2; B4DJ29; Q53SL2; Q9BVI1; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 5. DT 24-JAN-2024, entry version 162. DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase 1 {ECO:0000305}; DE Short=HS6ST-1; DE EC=2.8.2.- {ECO:0000269|PubMed:21700882}; GN Name=HS6ST1 {ECO:0000312|HGNC:HGNC:5201}; Synonyms=HS6ST; 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, CATALYTIC ACTIVITY, AND RP TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=9535912; DOI=10.1074/jbc.273.15.9208; RA Habuchi H., Kobayashi M., Kimata K.; RT "Molecular characterization and expression of heparan-sulfate 6- RT sulfotransferase."; RL J. Biol. Chem. 273:9208-9213(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 171-411 (ISOFORM 1). RC TISSUE=Cerebellum, and Hippocampus; 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=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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye; 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 FUNCTION, CATALYTIC ACTIVITY, VARIANTS HH15 TRP-306; GLN-306; GLN-323; RP TRP-382 AND VAL-404, AND CHARACTERIZATION OF VARIANTS HH15 TRP-306; RP GLN-306; GLN-323; TRP-382 AND VAL-404. RX PubMed=21700882; DOI=10.1073/pnas.1102284108; RA Tornberg J., Sykiotis G.P., Keefe K., Plummer L., Hoang X., Hall J.E., RA Quinton R., Seminara S.B., Hughes V., Van Vliet G., Van Uum S., RA Crowley W.F., Habuchi H., Kimata K., Pitteloud N., Bulow H.E.; RT "Heparan sulfate 6-O-sulfotransferase 1, a gene involved in extracellular RT sugar modifications, is mutated in patients with idiopathic RT hypogonadotrophic hypogonadism."; RL Proc. Natl. Acad. Sci. U.S.A. 108:11524-11529(2011). RN [6] RP VARIANTS HH15 SER-218; GLN-306 AND TRP-306. RX PubMed=25077900; DOI=10.1210/jc.2014-2110; RA Marcos S., Sarfati J., Leroy C., Fouveaut C., Parent P., Metz C., RA Wolczynski S., Gerard M., Bieth E., Kurtz F., Verier-Mine O., Perrin L., RA Archambeaud F., Cabrol S., Rodien P., Hove H., Prescott T., Lacombe D., RA Christin-Maitre S., Touraine P., Hieronimus S., Dewailly D., Young J., RA Pugeat M., Hardelin J.P., Dode C.; RT "The prevalence of CHD7 missense versus truncating mutations is higher in RT patients with Kallmann syndrome than in typical CHARGE patients."; RL J. Clin. Endocrinol. Metab. 99:E2138-2143(2014). CC -!- FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate CC from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the CC N-sulfoglucosamine residue (GlcNS) of heparan sulfate. Critical for CC normal neuronal development where it may play a role in neuron CC branching. May also play a role in limb development. May prefer CC iduronic acid. {ECO:0000269|PubMed:21700882, CC ECO:0000269|PubMed:9535912}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan CC sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + CC adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:56604, Rhea:RHEA- CC COMP:9830, Rhea:RHEA-COMP:14621, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388, CC ChEBI:CHEBI:140604; Evidence={ECO:0000269|PubMed:21700882, CC ECO:0000269|PubMed:9535912}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56605; CC Evidence={ECO:0000305|PubMed:21700882}; CC -!- INTERACTION: CC O60243; Q15323: KRT31; NbExp=3; IntAct=EBI-12294537, EBI-948001; CC O60243; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-12294537, EBI-10171774; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II CC membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O60243-1; Sequence=Displayed; CC Name=2; CC IsoId=O60243-2; Sequence=VSP_037048, VSP_037049; CC -!- TISSUE SPECIFICITY: Expressed in fetal brain. CC {ECO:0000269|PubMed:9535912}. CC -!- PTM: N-glycosylated. {ECO:0000250}. CC -!- DISEASE: Hypogonadotropic hypogonadism 15 with or without anosmia CC (HH15) [MIM:614880]: A disorder characterized by absent or incomplete CC sexual maturation by the age of 18 years, in conjunction with low CC levels of circulating gonadotropins and testosterone and no other CC abnormalities of the hypothalamic-pituitary axis. In some cases, it is CC associated with non-reproductive phenotypes, such as anosmia, cleft CC palate, and sensorineural hearing loss. Anosmia or hyposmia is related CC to the absence or hypoplasia of the olfactory bulbs and tracts. CC Hypogonadism is due to deficiency in gonadotropin-releasing hormone and CC probably results from a failure of embryonic migration of gonadotropin- CC releasing hormone-synthesizing neurons. In the presence of anosmia, CC idiopathic hypogonadotropic hypogonadism is referred to as Kallmann CC syndrome, whereas in the presence of a normal sense of smell, it has CC been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). CC {ECO:0000269|PubMed:21700882, ECO:0000269|PubMed:25077900}. Note=The CC disease is caused by variants affecting distinct genetic loci, CC including the gene represented in this entry. CC -!- SIMILARITY: Belongs to the sulfotransferase 6 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAY14736.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA25760.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA25760.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAG57153.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB006179; BAA25760.1; ALT_SEQ; mRNA. DR EMBL; AK293724; BAG57153.1; ALT_INIT; mRNA. DR EMBL; AK295898; BAG58691.1; -; mRNA. DR EMBL; AC017079; AAY14736.1; ALT_INIT; Genomic_DNA. DR EMBL; BC001196; AAH01196.1; -; mRNA. DR EMBL; BC096239; AAH96239.4; -; mRNA. DR EMBL; BC096240; AAH96240.4; -; mRNA. DR EMBL; BC099638; AAH99638.4; -; mRNA. DR EMBL; BC099639; AAH99639.4; -; mRNA. DR CCDS; CCDS42748.1; -. [O60243-1] DR RefSeq; NP_004798.3; NM_004807.2. [O60243-1] DR AlphaFoldDB; O60243; -. DR SMR; O60243; -. DR BioGRID; 114793; 41. DR IntAct; O60243; 11. DR MINT; O60243; -. DR STRING; 9606.ENSP00000259241; -. DR GlyCosmos; O60243; 2 sites, No reported glycans. DR GlyGen; O60243; 2 sites. DR iPTMnet; O60243; -. DR PhosphoSitePlus; O60243; -. DR BioMuta; HS6ST1; -. DR EPD; O60243; -. DR MassIVE; O60243; -. DR MaxQB; O60243; -. DR PaxDb; 9606-ENSP00000259241; -. DR PeptideAtlas; O60243; -. DR ProteomicsDB; 49276; -. [O60243-1] DR ProteomicsDB; 49277; -. [O60243-2] DR Antibodypedia; 33479; 134 antibodies from 18 providers. DR DNASU; 9394; -. DR Ensembl; ENST00000259241.7; ENSP00000259241.6; ENSG00000136720.7. [O60243-1] DR GeneID; 9394; -. DR KEGG; hsa:9394; -. DR MANE-Select; ENST00000259241.7; ENSP00000259241.6; NM_004807.3; NP_004798.3. DR UCSC; uc002tpt.5; human. [O60243-1] DR AGR; HGNC:5201; -. DR CTD; 9394; -. DR DisGeNET; 9394; -. DR GeneCards; HS6ST1; -. DR GeneReviews; HS6ST1; -. DR HGNC; HGNC:5201; HS6ST1. DR HPA; ENSG00000136720; Low tissue specificity. DR MalaCards; HS6ST1; -. DR MIM; 604846; gene. DR MIM; 614880; phenotype. DR neXtProt; NX_O60243; -. DR OpenTargets; ENSG00000136720; -. DR Orphanet; 478; Kallmann syndrome. DR Orphanet; 432; Normosmic congenital hypogonadotropic hypogonadism. DR PharmGKB; PA35102; -. DR VEuPathDB; HostDB:ENSG00000136720; -. DR eggNOG; KOG3955; Eukaryota. DR GeneTree; ENSGT00950000183071; -. DR HOGENOM; CLU_027877_1_0_1; -. DR InParanoid; O60243; -. DR OMA; AYNELQP; -. DR OrthoDB; 2896660at2759; -. DR PhylomeDB; O60243; -. DR TreeFam; TF312835; -. DR BioCyc; MetaCyc:ENSG00000136720-MONOMER; -. DR PathwayCommons; O60243; -. DR Reactome; R-HSA-2022928; HS-GAG biosynthesis. DR SignaLink; O60243; -. DR BioGRID-ORCS; 9394; 187 hits in 1125 CRISPR screens. DR ChiTaRS; HS6ST1; human. DR GenomeRNAi; 9394; -. DR Pharos; O60243; Tbio. DR PRO; PR:O60243; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; O60243; Protein. DR Bgee; ENSG00000136720; Expressed in kidney epithelium and 183 other cell types or tissues. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IBA:GO_Central. DR GO; GO:0008146; F:sulfotransferase activity; TAS:ProtInc. DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl. DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IBA:GO_Central. DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl. DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl. DR GO; GO:0048666; P:neuron development; IMP:UniProtKB. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005331; Sulfotransferase. DR PANTHER; PTHR12812; HEPARAN SULFATE 6-O-SULFOTRANSFERASE 3; 1. DR PANTHER; PTHR12812:SF1; HEPARAN-SULFATE 6-O-SULFOTRANSFERASE 1; 1. DR Pfam; PF03567; Sulfotransfer_2; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR Genevisible; O60243; HS. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Disease variant; Glycoprotein; KW Hypogonadotropic hypogonadism; Kallmann syndrome; Membrane; KW Reference proteome; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..411 FT /note="Heparan-sulfate 6-O-sulfotransferase 1" FT /id="PRO_0000190801" FT TOPO_DOM 11..17 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 18..37 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 38..411 FT /note="Lumenal" FT /evidence="ECO:0000255" FT COILED 352..387 FT /evidence="ECO:0000255" FT ACT_SITE 150 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:A0MGZ7" FT BINDING 93..101 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000250|UniProtKB:A0MGZ7" FT BINDING 123..124 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:A0MGZ7" FT BINDING 140 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:A0MGZ7" FT BINDING 145 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:A0MGZ7" FT BINDING 150 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:A0MGZ7" FT BINDING 185 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000250|UniProtKB:A0MGZ7" FT BINDING 193 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000250|UniProtKB:A0MGZ7" FT BINDING 197 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:A0MGZ7" FT BINDING 204 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:A0MGZ7" FT BINDING 317..319 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000250|UniProtKB:A0MGZ7" FT BINDING 323..324 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000250|UniProtKB:A0MGZ7" FT CARBOHYD 264 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 320 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..162 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037048" FT VAR_SEQ 163..175 FT /note="VLDRRDSAALRTP -> MFSWCLWPVVGES (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037049" FT VARIANT 218 FT /note="P -> S (in HH15; dbSNP:rs200268730)" FT /evidence="ECO:0000269|PubMed:25077900" FT /id="VAR_072980" FT VARIANT 306 FT /note="R -> Q (in HH15; 15 to 30% reduction in enzymatic FT activity compared to wild-type; dbSNP:rs201307896)" FT /evidence="ECO:0000269|PubMed:21700882, FT ECO:0000269|PubMed:25077900" FT /id="VAR_069283" FT VARIANT 306 FT /note="R -> W (in HH15; with anosmia; results in Kallmann FT syndrome in the presence of FGFR1 mutation Gln-250; FT approximately 50% reduction in enzymatic activity compared FT to wild-type; dbSNP:rs780352591)" FT /evidence="ECO:0000269|PubMed:21700882, FT ECO:0000269|PubMed:25077900" FT /id="VAR_069284" FT VARIANT 323 FT /note="R -> Q (in HH15; approximately 30% reduction in FT enzymatic activity compared to wild-type when heparan FT sulfate is the acceptor substrate; dbSNP:rs761325768)" FT /evidence="ECO:0000269|PubMed:21700882" FT /id="VAR_069285" FT VARIANT 382 FT /note="R -> W (in HH15; with or without anosmia; results in FT Kallmann syndrome in the presence of NSMF mutation Ala-480; FT 25 to 35% reduction in enzymatic activity compared to FT wild-type; dbSNP:rs199538589)" FT /evidence="ECO:0000269|PubMed:21700882" FT /id="VAR_069286" FT VARIANT 404 FT /note="M -> V (in HH15; with anosmia; 30 to 70% reduction FT in enzymatic activity compared to wild-type)" FT /evidence="ECO:0000269|PubMed:21700882" FT /id="VAR_069287" FT CONFLICT 55 FT /note="D -> Y (in Ref. 1; BAA25760)" FT /evidence="ECO:0000305" FT CONFLICT 191 FT /note="Y -> C (in Ref. 2; BAG57153)" FT /evidence="ECO:0000305" FT CONFLICT 255 FT /note="A -> T (in Ref. 2; BAG57153)" FT /evidence="ECO:0000305" SQ SEQUENCE 411 AA; 48226 MW; FCBF7AFAF1F3325D CRC64; MRRRRAGGRT MVERASKFVL VVAGSVCFML ILYQYAGPGL SLGAPGGRAP PDDLDLFPTP DPHYEKKYYF PVRELERSLR FDMKGDDVIV FLHIQKTGGT TFGRHLVQNV RLEVPCDCRP GQKKCTCYRP NRRETWLFSR FSTGWSCGLH ADWTELTNCV PGVLDRRDSA ALRTPRKFYY ITLLRDPVSR YLSEWRHVQR GATWKTSLHM CDGRTPTPEE LPPCYEGTDW SGCTLQEFMD CPYNLANNRQ VRMLADLSLV GCYNLSFIPE GKRAQLLLES AKKNLRGMAF FGLTEFQRKT QYLFERTFNL KFIRPFMQYN STRAGGVEVD EDTIRRIEEL NDLDMQLYDY AKDLFQQRYQ YKRQLERREQ RLRSREERLL HRAKEALPRE DADEPGRVPT EDYMSHIIEK W //