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   27-MAR-2024, entry version 174.
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};
GN   Synonyms=CHSY, CSS1, KIAA0990; 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; 58.
DR   IntAct; Q86X52; 14.
DR   MINT; Q86X52; -.
DR   STRING; 9606.ENSP00000254190; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   CAZy; GT7; Glycosyltransferase Family 7.
DR   GlyCosmos; Q86X52; 3 sites, No reported glycans.
DR   GlyGen; Q86X52; 6 sites, 1 O-linked glycan (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; 9606-ENSP00000254190; -.
DR   PeptideAtlas; Q86X52; -.
DR   ProteomicsDB; 70239; -.
DR   Pumba; Q86X52; -.
DR   Antibodypedia; 43966; 173 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   AGR; HGNC:17198; -.
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; HYLDRYE; -.
DR   OrthoDB; 2914228at2759; -.
DR   PhylomeDB; Q86X52; -.
DR   TreeFam; TF318303; -.
DR   BioCyc; MetaCyc:HS13400-MONOMER; -.
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; 11 hits in 1160 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 198 other cell types or tissues.
DR   ExpressionAtlas; Q86X52; baseline and differential.
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:0016020; C:membrane; HDA:UniProtKB.
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; 3.90.550.50; -; 1.
DR   InterPro; IPR008428; Chond_GalNAc.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR12369:SF42; CHONDROITIN SULFATE SYNTHASE 1; 1.
DR   PANTHER; PTHR12369; CHONDROITIN SYNTHASE; 1.
DR   Pfam; PF05679; CHGN; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 2.
DR   Genevisible; Q86X52; HS.
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
//