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Database: UniProt
Entry: P09871
LinkDB: P09871
Original site: P09871 
ID   C1S_HUMAN               Reviewed;         688 AA.
AC   P09871; D3DUT4; Q9UCU7; Q9UCU8; Q9UCU9; Q9UCV0; Q9UCV1; Q9UCV2;
AC   Q9UCV3; Q9UCV4; Q9UCV5; Q9UM14;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   16-APR-2014, entry version 183.
DE   RecName: Full=Complement C1s subcomponent;
DE            EC=3.4.21.42;
DE   AltName: Full=C1 esterase;
DE   AltName: Full=Complement component 1 subcomponent s;
DE   Contains:
DE     RecName: Full=Complement C1s subcomponent heavy chain;
DE   Contains:
DE     RecName: Full=Complement C1s subcomponent light chain;
DE   Flags: Precursor;
GN   Name=C1S;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=3500856; DOI=10.1111/j.1432-1033.1987.tb13644.x;
RA   McKinnon C.M., Carter P.E., Smyth S.J., Dunbar B., Fothergill J.E.;
RT   "Molecular cloning of cDNA for human complement component C1s. The
RT   complete amino acid sequence.";
RL   Eur. J. Biochem. 169:547-553(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2831944; DOI=10.1021/bi00400a004;
RA   Tosi M., Duponchel C., Meo T., Julier C.;
RT   "Complete cDNA sequence of human complement Cls and close physical
RT   linkage of the homologous genes Cls and Clr.";
RL   Biochemistry 26:8516-8524(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2459702; DOI=10.1073/pnas.85.19.7307;
RA   Kusumoto H., Hirosawa S., Salier J.-P., Hagen F.S., Kurachi K.;
RT   "Human genes for complement components C1r and C1s in a close tail-to-
RT   tail arrangement.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:7307-7311(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PNS;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-329.
RC   TISSUE=Peripheral blood leukocyte;
RX   PubMed=9794427;
RA   Endo Y., Takahashi M., Nakao M., Saiga H., Sekine H., Matsushita M.,
RA   Nonaka M., Fujita T.;
RT   "Two lineages of mannose-binding lectin-associated serine protease
RT   (MASP) in vertebrates.";
RL   J. Immunol. 161:4924-4930(1998).
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 291-688.
RX   PubMed=2553984; DOI=10.1016/0022-2836(89)90161-7;
RA   Tosi M., Duponchel C., Meo T., Couture-Tosi E.;
RT   "Complement genes C1r and C1s feature an intronless serine protease
RT   domain closely related to haptoglobin.";
RL   J. Mol. Biol. 208:709-714(1989).
RN   [8]
RP   PROTEIN SEQUENCE OF 16-61; 168-219; 287-334 AND 384-445.
RX   PubMed=3007145; DOI=10.1111/j.1432-1033.1986.tb09546.x;
RA   Spycher S.E., Nick H., Rickli E.E.;
RT   "Human complement component C1s. Partial sequence determination of the
RT   heavy chain and identification of the peptide bond cleaved during
RT   activation.";
RL   Eur. J. Biochem. 156:49-57(1986).
RN   [9]
RP   PROTEIN SEQUENCE OF 438-500; 503-534; 542-601; 617-623 AND 626-656.
RX   PubMed=6362661;
RA   Carter P.E., Dunbar B., Fothergill J.E.;
RT   "The serine proteinase chain of human complement component C1s.
RT   Cyanogen bromide cleavage and N-terminal sequences of the fragments.";
RL   Biochem. J. 215:565-571(1983).
RN   [10]
RP   PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-174, AND HYDROXYLATION
RP   AT ASN-149.
RX   PubMed=2141278; DOI=10.1021/bi00466a021;
RA   Thielens N.M., van Dorsselaer A., Gagnon J., Arlaud G.J.;
RT   "Chemical and functional characterization of a fragment of C1-s
RT   containing the epidermal growth factor homology region.";
RL   Biochemistry 29:3570-3578(1990).
RN   [11]
RP   PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Plasma;
RX   PubMed=1854725; DOI=10.1021/bi00243a014;
RA   Illy C., Thielens N.M., Gagnon J., Arlaud G.J.;
RT   "Effect of lactoperoxidase-catalyzed iodination on the Ca(2+)-
RT   dependent interactions of human C1s. Location of the iodination
RT   sites.";
RL   Biochemistry 30:7135-7141(1991).
RN   [12]
RP   DISULFIDE BONDS.
RX   PubMed=2007122; DOI=10.1021/bi00225a014;
RA   Hess D., Schaller J., Rickli E.E.;
RT   "Identification of the disulfide bonds of human complement C1s.";
RL   Biochemistry 30:2827-2833(1991).
RN   [13]
RP   PARTIAL PROTEIN SEQUENCE, AND 3D-STRUCTURE MODELING OF CATALYTIC
RP   DOMAIN.
RX   PubMed=7779774; DOI=10.1021/bi00022a004;
RA   Rossi V., Gaboriaud C., Lacroix M., Ulrich J., Fontecilla-Camps J.-C.,
RA   Gagnon J., Arlaud G.J.;
RT   "Structure of the catalytic region of human complement protease C1s:
RT   study by chemical cross-linking and three-dimensional homology
RT   modeling.";
RL   Biochemistry 34:7311-7321(1995).
RN   [14]
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME
RP   REGULATION.
RX   PubMed=11527969; DOI=10.1074/jbc.M105934200;
RA   Rossi V., Cseh S., Bally I., Thielens N.M., Jensenius J.C.,
RA   Arlaud G.J.;
RT   "Substrate specificities of recombinant mannan-binding lectin-
RT   associated serine proteases-1 and -2.";
RL   J. Biol. Chem. 276:40880-40887(2001).
RN   [15]
RP   INVOLVEMENT IN COMPLEMENT COMPONENT C1S DEFICIENCY.
RX   PubMed=11390518;
RA   Dragon-Durey M.-A., Quartier P., Fremeaux-Bacchi V., Blouin J.,
RA   de Barace C., Prieur A.-M., Weiss L., Fridman W.-H.;
RT   "Molecular basis of a selective C1s deficiency associated with early
RT   onset multiple autoimmune diseases.";
RL   J. Immunol. 166:7612-7616(2001).
RN   [16]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [17]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174 AND ASN-406.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 358-688.
RX   PubMed=10775260; DOI=10.1093/emboj/19.8.1755;
RA   Gaboriaud C., Rossi V., Bally I., Arlaud G.J., Fontecilla-Camps J.-C.;
RT   "Crystal structure of the catalytic domain of human complement c1s: a
RT   serine protease with a handle.";
RL   EMBO J. 19:1755-1765(2000).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 16-174, CALCIUM-BINDING
RP   SITES, AND GLYCOSYLATION AT ASN-406.
RX   PubMed=12788922; DOI=10.1074/jbc.M305175200;
RA   Gregory L.A., Thielens N.M., Arlaud G.J., Fontecilla-Camps J.-C.,
RA   Gaboriaud C.;
RT   "X-ray structure of the Ca2+-binding interaction domain of C1s.
RT   Insights into the assembly of the C1 complex of complement.";
RL   J. Biol. Chem. 278:32157-32164(2003).
CC   -!- FUNCTION: C1s B chain is a serine protease that combines with C1q
CC       and C1r to form C1, the first component of the classical pathway
CC       of the complement system. C1r activates C1s so that it can, in
CC       turn, activate C2 and C4.
CC   -!- CATALYTIC ACTIVITY: Cleavage of Arg-|-Ala bond in complement
CC       component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in
CC       complement component C2 to form C2a and C2b: the 'classical'
CC       pathway C3 convertase.
CC   -!- ENZYME REGULATION: Inhibited by SERPING1.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12.3 uM for complement component C2 (at 37 degrees Celsius);
CC         KM=1.9 uM for complement component C4 (at 37 degrees Celsius);
CC         Note=Less efficient than MASP2 in C4 cleavage;
CC   -!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q,
CC       C1r and C1s in the molar ration of 1:2:2. Activated C1s is an
CC       disulfide-linked heterodimer of a heavy chain and a light chain.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-2810045, EBI-2810045;
CC       P00736:C1R; NbExp=3; IntAct=EBI-2810045, EBI-3926504;
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC   -!- DISEASE: Complement component C1s deficiency (C1SD) [MIM:613783]:
CC       A rare defect resulting in C1 deficiency and impaired activation
CC       of the complement classical pathway. C1 deficiency generally leads
CC       to severe immune complex disease with features of systemic lupus
CC       erythematosus and glomerulonephritis. Note=The disease is caused
CC       by mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 2 CUB domains.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC   -!- SIMILARITY: Contains 2 Sushi (CCP/SCR) domains.
CC   -!- WEB RESOURCE: Name=C1Sbase; Note=C1S mutation db;
CC       URL="http://bioinf.uta.fi/C1Sbase/";
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DR   EMBL; X06596; CAA29817.1; -; mRNA.
DR   EMBL; M18767; AAA51853.1; -; mRNA.
DR   EMBL; J04080; AAA51852.1; -; mRNA.
DR   EMBL; CH471116; EAW88689.1; -; Genomic_DNA.
DR   EMBL; CH471116; EAW88690.1; -; Genomic_DNA.
DR   EMBL; BC056903; AAH56903.1; -; mRNA.
DR   EMBL; AB009076; BAA86864.1; -; Genomic_DNA.
DR   PIR; A40496; C1HUS.
DR   RefSeq; NP_001725.1; NM_001734.3.
DR   RefSeq; NP_958850.1; NM_201442.2.
DR   RefSeq; XP_005253817.1; XM_005253760.1.
DR   UniGene; Hs.458355; -.
DR   PDB; 1ELV; X-ray; 1.70 A; A=358-688.
DR   PDB; 1NZI; X-ray; 1.50 A; A/B=16-174.
DR   PDB; 4J1Y; X-ray; 2.66 A; A/B=292-688.
DR   PDB; 4LMF; X-ray; 2.92 A; A/B/C/D=17-292.
DR   PDB; 4LOR; X-ray; 2.50 A; A=17-292.
DR   PDB; 4LOS; X-ray; 2.00 A; A=172-358.
DR   PDB; 4LOT; X-ray; 2.92 A; A=175-423.
DR   PDBsum; 1ELV; -.
DR   PDBsum; 1NZI; -.
DR   PDBsum; 4J1Y; -.
DR   PDBsum; 4LMF; -.
DR   PDBsum; 4LOR; -.
DR   PDBsum; 4LOS; -.
DR   PDBsum; 4LOT; -.
DR   ProteinModelPortal; P09871; -.
DR   SMR; P09871; 17-684.
DR   BioGrid; 107177; 7.
DR   IntAct; P09871; 8.
DR   MINT; MINT-4655918; -.
DR   BindingDB; P09871; -.
DR   ChEMBL; CHEMBL3913; -.
DR   DrugBank; DB00054; Abciximab.
DR   DrugBank; DB00051; Adalimumab.
DR   DrugBank; DB00074; Basiliximab.
DR   DrugBank; DB00002; Cetuximab.
DR   DrugBank; DB00005; Etanercept.
DR   DrugBank; DB00056; Gemtuzumab ozogamicin.
DR   DrugBank; DB00078; Ibritumomab.
DR   DrugBank; DB00028; Immune globulin.
DR   DrugBank; DB00075; Muromonab.
DR   DrugBank; DB00073; Rituximab.
DR   DrugBank; DB00072; Trastuzumab.
DR   MEROPS; S01.193; -.
DR   PhosphoSite; P09871; -.
DR   DMDM; 115205; -.
DR   SWISS-2DPAGE; P09871; -.
DR   PaxDb; P09871; -.
DR   PeptideAtlas; P09871; -.
DR   PRIDE; P09871; -.
DR   Ensembl; ENST00000328916; ENSP00000328173; ENSG00000182326.
DR   Ensembl; ENST00000360817; ENSP00000354057; ENSG00000182326.
DR   Ensembl; ENST00000406697; ENSP00000385035; ENSG00000182326.
DR   Ensembl; ENST00000594877; ENSP00000471707; ENSG00000269882.
DR   Ensembl; ENST00000595575; ENSP00000469947; ENSG00000269882.
DR   Ensembl; ENST00000600933; ENSP00000469899; ENSG00000269882.
DR   GeneID; 716; -.
DR   KEGG; hsa:716; -.
DR   UCSC; uc001qsj.3; human.
DR   CTD; 716; -.
DR   GeneCards; GC12P007096; -.
DR   HGNC; HGNC:1247; C1S.
DR   HPA; CAB016722; -.
DR   HPA; HPA018852; -.
DR   MIM; 120580; gene.
DR   MIM; 613783; phenotype.
DR   neXtProt; NX_P09871; -.
DR   Orphanet; 169147; Immunodeficiency due to an early component of complement deficiency.
DR   PharmGKB; PA25636; -.
DR   eggNOG; COG5640; -.
DR   HOVERGEN; HBG000559; -.
DR   InParanoid; P09871; -.
DR   KO; K01331; -.
DR   OMA; PTMYGEI; -.
DR   PhylomeDB; P09871; -.
DR   TreeFam; TF330373; -.
DR   Reactome; REACT_6900; Immune System.
DR   ChiTaRS; C1S; human.
DR   EvolutionaryTrace; P09871; -.
DR   GeneWiki; C1S; -.
DR   GenomeRNAi; 716; -.
DR   NextBio; 2912; -.
DR   PMAP-CutDB; P09871; -.
DR   PRO; PR:P09871; -.
DR   ArrayExpress; P09871; -.
DR   Bgee; P09871; -.
DR   Genevestigator; P09871; -.
DR   GO; GO:0072562; C:blood microparticle; IDA:UniProt.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0006956; P:complement activation; TAS:Reactome.
DR   GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.290; -; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024175; Pept_S1A_C1r/C1S/mannan-bd.
DR   InterPro; IPR001254; Peptidase_S1.
DR   InterPro; IPR018114; Peptidase_S1_AS.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR000436; Sushi_SCR_CCP.
DR   InterPro; IPR009003; Trypsin-like_Pept_dom.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF00084; Sushi; 2.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001155; C1r_C1s_MASP; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00032; CCP; 2.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49854; SSF49854; 2.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57535; SSF57535; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50923; SUSHI; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Complement pathway; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Hydrolase; Hydroxylation; Immunity; Innate immunity;
KW   Metal-binding; Polymorphism; Protease; Reference proteome; Repeat;
KW   Serine protease; Signal; Sushi.
FT   SIGNAL        1     15
FT   CHAIN        16    688       Complement C1s subcomponent.
FT                                /FTId=PRO_0000027586.
FT   CHAIN        16    437       Complement C1s subcomponent heavy chain.
FT                                /FTId=PRO_0000027587.
FT   CHAIN       438    688       Complement C1s subcomponent light chain.
FT                                /FTId=PRO_0000027588.
FT   DOMAIN       16    130       CUB 1.
FT   DOMAIN      131    172       EGF-like; calcium-binding.
FT   DOMAIN      175    290       CUB 2.
FT   DOMAIN      292    356       Sushi 1.
FT   DOMAIN      357    423       Sushi 2.
FT   DOMAIN      438    680       Peptidase S1.
FT   ACT_SITE    475    475       Charge relay system.
FT   ACT_SITE    529    529       Charge relay system.
FT   ACT_SITE    632    632       Charge relay system.
FT   METAL        60     60       Calcium.
FT   METAL        68     68       Calcium.
FT   METAL       113    113       Calcium.
FT   METAL       131    131       Calcium.
FT   METAL       132    132       Calcium; via carbonyl oxygen.
FT   METAL       134    134       Calcium.
FT   METAL       149    149       Calcium.
FT   METAL       150    150       Calcium; via carbonyl oxygen.
FT   METAL       153    153       Calcium; via carbonyl oxygen.
FT   MOD_RES     149    149       (3R)-3-hydroxyasparagine.
FT   CARBOHYD    174    174       N-linked (GlcNAc...).
FT   CARBOHYD    406    406       N-linked (GlcNAc...).
FT   DISULFID     65     83
FT   DISULFID    135    147
FT   DISULFID    143    156
FT   DISULFID    158    171
FT   DISULFID    175    202
FT   DISULFID    234    251
FT   DISULFID    294    341
FT   DISULFID    321    354
FT   DISULFID    359    403
FT   DISULFID    386    421
FT   DISULFID    425    549       Interchain (between heavy and light
FT                                chains).
FT   DISULFID    595    618
FT   DISULFID    628    659
FT   VARIANT     119    119       R -> H (in dbSNP:rs12146727).
FT                                /FTId=VAR_033643.
FT   VARIANT     327    327       V -> L (in dbSNP:rs2239170).
FT                                /FTId=VAR_033644.
FT   VARIANT     383    383       R -> H (in dbSNP:rs20573).
FT                                /FTId=VAR_014565.
FT   CONFLICT    294    294       C -> K (in Ref. 8; AA sequence).
FT   CONFLICT    513    513       G -> GG (in Ref. 7).
FT   CONFLICT    573    573       T -> A (in Ref. 9; AA sequence).
FT   CONFLICT    645    646       TK -> GR (in Ref. 9; AA sequence).
FT   STRAND       19     24
FT   TURN         26     29
FT   STRAND       34     43
FT   STRAND       48     58
FT   HELIX        63     65
FT   STRAND       67     73
FT   STRAND       80     82
FT   STRAND       84     86
FT   STRAND       96    112
FT   STRAND      122    131
FT   TURN        134    136
FT   STRAND      137    140
FT   STRAND      143    150
FT   STRAND      153    157
FT   STRAND      162    164
FT   STRAND      171    173
FT   STRAND      176    180
FT   STRAND      182    188
FT   TURN        190    193
FT   STRAND      201    207
FT   STRAND      212    217
FT   HELIX       220    222
FT   STRAND      223    225
FT   STRAND      235    242
FT   STRAND      245    250
FT   STRAND      252    254
FT   STRAND      259    262
FT   STRAND      265    273
FT   STRAND      282    291
FT   STRAND      300    306
FT   STRAND      309    312
FT   STRAND      316    321
FT   STRAND      325    331
FT   STRAND      334    341
FT   TURN        348    351
FT   STRAND      353    356
FT   STRAND      368    370
FT   STRAND      381    386
FT   TURN        388    390
FT   STRAND      391    393
FT   STRAND      395    397
FT   STRAND      399    403
FT   TURN        405    407
FT   STRAND      409    411
FT   TURN        412    414
FT   STRAND      421    423
FT   HELIX       446    448
FT   STRAND      452    455
FT   TURN        456    459
FT   STRAND      460    466
FT   STRAND      469    472
FT   HELIX       474    477
FT   STRAND      490    492
FT   HELIX       494    499
FT   STRAND      505    510
FT   HELIX       520    522
FT   STRAND      531    537
FT   HELIX       555    557
FT   STRAND      564    570
FT   STRAND      576    578
FT   STRAND      583    590
FT   HELIX       592    596
FT   STRAND      616    620
FT   HELIX       627    629
FT   STRAND      635    639
FT   STRAND      647    655
FT   STRAND      661    667
FT   HELIX       668    671
FT   HELIX       672    681
SQ   SEQUENCE   688 AA;  76684 MW;  85522647A4C47205 CRC64;
     MWCIVLFSLL AWVYAEPTMY GEILSPNYPQ AYPSEVEKSW DIEVPEGYGI HLYFTHLDIE
     LSENCAYDSV QIISGDTEEG RLCGQRSSNN PHSPIVEEFQ VPYNKLQVIF KSDFSNEERF
     TGFAAYYVAT DINECTDFVD VPCSHFCNNF IGGYFCSCPP EYFLHDDMKN CGVNCSGDVF
     TALIGEIASP NYPKPYPENS RCEYQIRLEK GFQVVVTLRR EDFDVEAADS AGNCLDSLVF
     VAGDRQFGPY CGHGFPGPLN IETKSNALDI IFQTDLTGQK KGWKLRYHGD PMPCPKEDTP
     NSVWEPAKAK YVFRDVVQIT CLDGFEVVEG RVGATSFYST CQSNGKWSNS KLKCQPVDCG
     IPESIENGKV EDPESTLFGS VIRYTCEEPY YYMENGGGGE YHCAGNGSWV NEVLGPELPK
     CVPVCGVPRE PFEEKQRIIG GSDADIKNFP WQVFFDNPWA GGALINEYWV LTAAHVVEGN
     REPTMYVGST SVQTSRLAKS KMLTPEHVFI HPGWKLLEVP EGRTNFDNDI ALVRLKDPVK
     MGPTVSPICL PGTSSDYNLM DGDLGLISGW GRTEKRDRAV RLKAARLPVA PLRKCKEVKV
     EKPTADAEAY VFTPNMICAG GEKGMDSCKG DSGGAFAVQD PNDKTKFYAA GLVSWGPQCG
     TYGLYTRVKN YVDWIMKTMQ ENSTPRED
//
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