CHSS1_HUMAN
ID CHSS1_HUMAN Reviewed; 802 AA.
AC Q86X52; Q6UX38; Q7LFU5; Q9Y2J5;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Chondroitin sulfate synthase 1 {ECO:0000305};
DE EC=2.4.1.175 {ECO:0000269|PubMed:12716890};
DE EC=2.4.1.226 {ECO:0000269|PubMed:12716890};
DE AltName: Full=Chondroitin glucuronyltransferase 1;
DE AltName: Full=Chondroitin synthase 1;
DE Short=ChSy-1;
DE AltName: Full=Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase 1;
DE AltName: Full=N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 1;
DE AltName: Full=N-acetylgalactosaminyltransferase 1;
GN Name=CHSY1 {ECO:0000312|HGNC:HGNC:17198}; Synonyms=CHSY, CSS1, KIAA0990;
GN ORFNames=UNQ756/PRO1487;
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], FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11514575; DOI=10.1074/jbc.m106871200;
RA Kitagawa H., Uyama T., Sugahara K.;
RT "Molecular cloning and expression of a human chondroitin synthase.";
RL J. Biol. Chem. 276:38721-38726(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RC TISSUE=Brain;
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, AND CATALYTIC ACTIVITY.
RX PubMed=12716890; DOI=10.1074/jbc.m302493200;
RA Kitagawa H., Izumikawa T., Uyama T., Sugahara K.;
RT "Molecular cloning of a chondroitin polymerizing factor that cooperates
RT with chondroitin synthase for chondroitin polymerization.";
RL J. Biol. Chem. 278:23666-23671(2003).
RN [6]
RP COFACTOR, AND TISSUE SPECIFICITY.
RX PubMed=12907687; DOI=10.1074/jbc.m304421200;
RA Yada T., Sato T., Kaseyama H., Gotoh M., Iwasaki H., Kikuchi N.,
RA Kwon Y.-D., Togayachi A., Kudo T., Watanabe H., Narimatsu H., Kimata K.;
RT "Chondroitin sulfate synthase-3. Molecular cloning and characterization.";
RL J. Biol. Chem. 278:39711-39725(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INVOLVEMENT IN TPBS.
RX PubMed=21129727; DOI=10.1016/j.ajhg.2010.11.005;
RA Tian J., Ling L., Shboul M., Lee H., O'Connor B., Merriman B., Nelson S.F.,
RA Cool S., Ababneh O.H., Al-Hadidy A., Masri A., Hamamy H., Reversade B.;
RT "Loss of CHSY1, a secreted FRINGE enzyme, causes syndromic brachydactyly in
RT humans via increased NOTCH signaling.";
RL Am. J. Hum. Genet. 87:768-778(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP VARIANTS TPBS 19-GLY--LEU-28 DEL AND ARG-539.
RX PubMed=21129728; DOI=10.1016/j.ajhg.2010.10.003;
RA Li Y., Laue K., Temtamy S., Aglan M., Kotan L.D., Yigit G., Canan H.,
RA Pawlik B., Nurnberg G., Wakeling E.L., Quarrell O.W., Baessmann I.,
RA Lanktree M.B., Yilmaz M., Hegele R.A., Amr K., May K.W., Nurnberg P.,
RA Topaloglu A.K., Hammerschmidt M., Wollnik B.;
RT "Temtamy preaxial brachydactyly syndrome is caused by loss-of-function
RT mutations in chondroitin synthase 1, a potential target of BMP signaling.";
RL Am. J. Hum. Genet. 87:757-767(2010).
CC -!- FUNCTION: Has both beta-1,3-glucuronic acid and beta-1,4-N-
CC acetylgalactosamine transferase activity. Transfers glucuronic acid
CC (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-
CC GalNAc to the non-reducing end of the elongating chondroitin polymer.
CC Involved in the negative control of osteogenesis likely through the
CC modulation of NOTCH signaling. {ECO:0000269|PubMed:11514575,
CC ECO:0000269|PubMed:12716890, ECO:0000269|PubMed:21129727}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-(beta-D-GalNAc-
CC (1->4)-beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-
CC beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] +
CC H(+) + UDP; Xref=Rhea:RHEA:20800, Rhea:RHEA-COMP:14058, Rhea:RHEA-
CC COMP:14059, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:138442, ChEBI:CHEBI:138443; EC=2.4.1.175;
CC Evidence={ECO:0000269|PubMed:12716890};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20801;
CC Evidence={ECO:0000305|PubMed:12716890};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)](n)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-
CC beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-
CC D-galactosamine = 3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)](n+1)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-
CC (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:55000, Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14301,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:138444, ChEBI:CHEBI:138445; EC=2.4.1.175;
CC Evidence={ECO:0000269|PubMed:12716890};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55001;
CC Evidence={ECO:0000305|PubMed:12716890};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-
CC (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-
CC glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:23428, Rhea:RHEA-COMP:12575,
CC Rhea:RHEA-COMP:14058, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132105, ChEBI:CHEBI:138442;
CC EC=2.4.1.226; Evidence={ECO:0000269|PubMed:12716890};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23429;
CC Evidence={ECO:0000305|PubMed:12716890};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-
CC D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:54996,
CC Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14061, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:138444,
CC ChEBI:CHEBI:138445; EC=2.4.1.226;
CC Evidence={ECO:0000269|PubMed:12716890};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54997;
CC Evidence={ECO:0000305|PubMed:12716890};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:12907687};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12907687};
CC Name=Cd(2+); Xref=ChEBI:CHEBI:48775;
CC Evidence={ECO:0000269|PubMed:12907687};
CC Note=Divalent metal cations. Highest activities are measured with
CC Co(2+), Mn(2+) and Cd(2+). {ECO:0000269|PubMed:12907687};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305|PubMed:11514575}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:11514575}. Secreted {ECO:0000269|PubMed:21129727}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with the highest levels in placenta.
CC Detected at low levels in brain, heart, skeletal muscle, colon, thymus,
CC spleen, kidney, liver, adrenal gland, mammary gland, stomach, small
CC intestine, lung and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:11514575, ECO:0000269|PubMed:12907687}.
CC -!- DISEASE: Temtamy preaxial brachydactyly syndrome (TPBS) [MIM:605282]: A
CC syndrome characterized by multiple congenital anomalies, intellectual
CC disability, sensorineural deafness, talon cusps of upper central
CC incisors, growth retardation, and bilateral symmetric digital anomalies
CC mainly in the form of preaxial brachydactyly and hyperphalangism.
CC {ECO:0000269|PubMed:21129727, ECO:0000269|PubMed:21129728}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76834.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Chondroitin sulfate synthase 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_445";
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DR EMBL; AB071402; BAB64936.1; -; mRNA.
DR EMBL; AB023207; BAA76834.2; ALT_INIT; mRNA.
DR EMBL; AY358529; AAQ88893.1; -; mRNA.
DR EMBL; BC046247; AAH46247.1; -; mRNA.
DR CCDS; CCDS10390.1; -.
DR RefSeq; NP_055733.2; NM_014918.4.
DR AlphaFoldDB; Q86X52; -.
DR SMR; Q86X52; -.
DR BioGRID; 116526; 55.
DR IntAct; Q86X52; 14.
DR MINT; Q86X52; -.
DR STRING; 9606.ENSP00000254190; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q86X52; 3 sites.
DR iPTMnet; Q86X52; -.
DR PhosphoSitePlus; Q86X52; -.
DR BioMuta; CHSY1; -.
DR DMDM; 116241296; -.
DR EPD; Q86X52; -.
DR jPOST; Q86X52; -.
DR MassIVE; Q86X52; -.
DR MaxQB; Q86X52; -.
DR PaxDb; Q86X52; -.
DR PeptideAtlas; Q86X52; -.
DR PRIDE; Q86X52; -.
DR ProteomicsDB; 70239; -.
DR Antibodypedia; 43966; 152 antibodies from 23 providers.
DR DNASU; 22856; -.
DR Ensembl; ENST00000254190.4; ENSP00000254190.3; ENSG00000131873.7.
DR GeneID; 22856; -.
DR KEGG; hsa:22856; -.
DR MANE-Select; ENST00000254190.4; ENSP00000254190.3; NM_014918.5; NP_055733.2.
DR UCSC; uc021sxt.1; human.
DR CTD; 22856; -.
DR DisGeNET; 22856; -.
DR GeneCards; CHSY1; -.
DR HGNC; HGNC:17198; CHSY1.
DR HPA; ENSG00000131873; Low tissue specificity.
DR MalaCards; CHSY1; -.
DR MIM; 605282; phenotype.
DR MIM; 608183; gene.
DR neXtProt; NX_Q86X52; -.
DR OpenTargets; ENSG00000131873; -.
DR Orphanet; 363417; Temtamy preaxial brachydactyly syndrome.
DR PharmGKB; PA26509; -.
DR VEuPathDB; HostDB:ENSG00000131873; -.
DR eggNOG; KOG3588; Eukaryota.
DR GeneTree; ENSGT01050000244857; -.
DR HOGENOM; CLU_016244_2_0_1; -.
DR InParanoid; Q86X52; -.
DR OMA; FEKNDPN; -.
DR OrthoDB; 442283at2759; -.
DR PhylomeDB; Q86X52; -.
DR TreeFam; TF318303; -.
DR BioCyc; MetaCyc:HS13400-MON; -.
DR BRENDA; 2.4.1.175; 2681.
DR BRENDA; 2.4.1.226; 2681.
DR PathwayCommons; Q86X52; -.
DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-HSA-3595177; Defective CHSY1 causes TPBS.
DR SABIO-RK; Q86X52; -.
DR SignaLink; Q86X52; -.
DR BioGRID-ORCS; 22856; 10 hits in 1082 CRISPR screens.
DR ChiTaRS; CHSY1; human.
DR GeneWiki; CHSY1; -.
DR GenomeRNAi; 22856; -.
DR Pharos; Q86X52; Tbio.
DR PRO; PR:Q86X52; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q86X52; protein.
DR Bgee; ENSG00000131873; Expressed in tibia and 196 other tissues.
DR ExpressionAtlas; Q86X52; baseline and differential.
DR Genevisible; Q86X52; HS.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050510; F:N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity; IDA:FlyBase.
DR GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl.
DR GO; GO:0002063; P:chondrocyte development; IEA:Ensembl.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:MGI.
DR GO; GO:0030279; P:negative regulation of ossification; IMP:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR GO; GO:0051923; P:sulfation; IEA:Ensembl.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR008428; Chond_GalNAc.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF05679; CHGN; 1.
DR SUPFAM; SSF53448; SSF53448; 2.
PE 1: Evidence at protein level;
KW Disease variant; Glycoprotein; Golgi apparatus; Membrane; Metal-binding;
KW Reference proteome; Secreted; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..802
FT /note="Chondroitin sulfate synthase 1"
FT /id="PRO_0000189558"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..802
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 34..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 633
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 747
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 19..28
FT /note="Missing (in TPBS)"
FT /evidence="ECO:0000269|PubMed:21129728"
FT /id="VAR_065821"
FT VARIANT 359
FT /note="P -> S (in dbSNP:rs3743193)"
FT /id="VAR_021173"
FT VARIANT 539
FT /note="P -> R (in TPBS; dbSNP:rs387906985)"
FT /evidence="ECO:0000269|PubMed:21129728"
FT /id="VAR_065822"
FT VARIANT 652
FT /note="Q -> H (in dbSNP:rs4426333)"
FT /id="VAR_028009"
FT CONFLICT 274
FT /note="Q -> R (in Ref. 3; AAQ88893)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="R -> T (in Ref. 1; BAB64936 and 2; BAA76834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 802 AA; 91784 MW; 5B4C02670332FA0E CRC64;
MAARGRRAWL SVLLGLVLGF VLASRLVLPR ASELKRAGPR RRASPEGCRS GQAAASQAGG
ARGDARGAQL WPPGSDPDGG PRDRNFLFVG VMTAQKYLQT RAVAAYRTWS KTIPGKVQFF
SSEGSDTSVP IPVVPLRGVD DSYPPQKKSF MMLKYMHDHY LDKYEWFMRA DDDVYIKGDR
LENFLRSLNS SEPLFLGQTG LGTTEEMGKL ALEPGENFCM GGPGVIMSRE VLRRMVPHIG
KCLREMYTTH EDVEVGRCVR RFAGVQCVWS YEMQQLFYEN YEQNKKGYIR DLHNSKIHQA
ITLHPNKNPP YQYRLHSYML SRKISELRHR TIQLHREIVL MSKYSNTEIH KEDLQLGIPP
SFMRFQPRQR EEILEWEFLT GKYLYSAVDG QPPRRGMDSA QREALDDIVM QVMEMINANA
KTRGRIIDFK EIQYGYRRVN PMYGAEYILD LLLLYKKHKG KKMTVPVRRH AYLQQTFSKI
QFVEHEELDA QELAKRINQE SGSLSFLSNS LKKLVPFQLP GSKSEHKEPK DKKINILIPL
SGRFDMFVRF MGNFEKTCLI PNQNVKLVVL LFNSDSNPDK AKQVELMRDY RIKYPKADMQ
ILPVSGEFSR ALALEVGSSQ FNNESLLFFC DVDLVFTTEF LQRCRANTVL GQQIYFPIIF
SQYDPKIVYS GKVPSDNHFA FTQKTGFWRN YGFGITCIYK GDLVRVGGFD VSIQGWGLED
VDLFNKVVQA GLKTFRSQEV GVVHVHHPVF CDPNLDPKQY KMCLGSKAST YGSTQQLAEM
WLEKNDPSYS KSSNNNGSVR TA
