H6ST1_HUMAN
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 03-AUG-2022, entry version 154.
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};
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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 GlyGen; O60243; 2 sites.
DR iPTMnet; O60243; -.
DR PhosphoSitePlus; O60243; -.
DR BioMuta; HS6ST1; -.
DR EPD; O60243; -.
DR MassIVE; O60243; -.
DR MaxQB; O60243; -.
DR PaxDb; O60243; -.
DR PeptideAtlas; O60243; -.
DR PRIDE; O60243; -.
DR ProteomicsDB; 49276; -. [O60243-1]
DR ProteomicsDB; 49277; -. [O60243-2]
DR Antibodypedia; 33479; 115 antibodies from 17 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 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; ELPACYK; -.
DR OrthoDB; 288325at2759; -.
DR PhylomeDB; O60243; -.
DR TreeFam; TF312835; -.
DR BioCyc; MetaCyc:ENSG00000136720-MON; -.
DR PathwayCommons; O60243; -.
DR Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR SignaLink; O60243; -.
DR BioGRID-ORCS; 9394; 170 hits in 1042 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 181 other tissues.
DR Genevisible; O60243; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of 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:0006024; P:glycosaminoglycan biosynthetic process; TAS:Reactome.
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; -; 1.
DR InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12812; PTHR12812; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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 wild-
FT 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
