GenomeNet

Database: UniProt
Entry: P07357
LinkDB: P07357
Original site: P07357 
ID   CO8A_HUMAN              Reviewed;         584 AA.
AC   P07357; A2RUI4; A2RUI5; Q13668; Q9H130;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   31-JUL-2019, entry version 202.
DE   RecName: Full=Complement component C8 alpha chain;
DE   AltName: Full=Complement component 8 subunit alpha;
DE   Flags: Precursor;
GN   Name=C8A;
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], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=2820471; DOI=10.1021/bi00386a046;
RA   Rao A.G., Howard O.M.Z., Ng S.C., Whitehead A.S., Colten H.R.,
RA   Sodetz J.M.;
RT   "Complementary DNA and derived amino acid sequence of the alpha
RT   subunit of human complement protein C8: evidence for the existence of
RT   a separate alpha subunit messenger RNA.";
RL   Biochemistry 26:3556-3564(1987).
RN   [2]
RP   SEQUENCE REVISION TO 467-479.
RA   Sodetz J.M.;
RL   Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RX   PubMed=7759071; DOI=10.1007/BF00223862;
RA   Michelotti G.A., Snider J.V., Sodetz J.M.;
RT   "Genomic organization of human complement protein C8 alpha and further
RT   examination of its linkage to C8 beta.";
RL   Hum. Genet. 95:513-518(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-93.
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   PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RX   PubMed=7440581;
RA   Steckel E.W., York R.G., Monahan J.B., Sodetz J.M.;
RT   "The eighth component of human complement. Purification and
RT   physicochemical characterization of its unusual subunit structure.";
RL   J. Biol. Chem. 255:11997-12005(1980).
RN   [7]
RP   GLYCOSYLATION AT TRP-44; TRP-542; TRP-545 AND TRP-548.
RX   PubMed=10551839; DOI=10.1074/jbc.274.46.32786;
RA   Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O.;
RT   "The four terminal components of the complement system are C-
RT   mannosylated on multiple tryptophan residues.";
RL   J. Biol. Chem. 274:32786-32794(1999).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-437.
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   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-437.
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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 133-492, AND FUNCTION.
RX   PubMed=17872444; DOI=10.1126/science.1147103;
RA   Hadders M.A., Beringer D.X., Gros P.;
RT   "Structure of C8alpha-MACPF reveals mechanism of membrane attack in
RT   complement immune defense.";
RL   Science 317:1552-1554(2007).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 133-492 IN COMPLEX WITH C8G,
RP   AND INTERCHAIN DISULFIDE BOND.
RX   PubMed=18440555; DOI=10.1016/j.jmb.2008.03.061;
RA   Slade D.J., Lovelace L.L., Chruszcz M., Minor W., Lebioda L.,
RA   Sodetz J.M.;
RT   "Crystal structure of the MACPF domain of human complement protein C8
RT   alpha in complex with the C8 gamma subunit.";
RL   J. Mol. Biol. 379:331-342(2008).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 188-198 IN COMPLEX WITH C8G.
RX   PubMed=17692377; DOI=10.1016/j.molimm.2007.06.359;
RA   Lovelace L.L., Chiswell B., Slade D.J., Sodetz J.M., Lebioda L.;
RT   "Crystal structure of complement protein C8gamma in complex with a
RT   peptide containing the C8gamma binding site on C8alpha: implications
RT   for C8gamma ligand binding.";
RL   Mol. Immunol. 45:750-756(2008).
RN   [14]
RP   VARIANT C8A*B LYS-93.
RX   PubMed=7649542; DOI=10.1007/BF00210407;
RA   Zhang L., Rittner C., Sodetz J.M., Schneider P.M., Kaufmann T.;
RT   "The eighth component of human complement: molecular basis of C8A
RT   (C81) polymorphism.";
RL   Hum. Genet. 96:281-284(1995).
CC   -!- FUNCTION: Constituent of the membrane attack complex (MAC) that
CC       plays a key role in the innate and adaptive immune response by
CC       forming pores in the plasma membrane of target cells. C8A inserts
CC       into the target membrane, but does not form pores by itself.
CC       {ECO:0000269|PubMed:17872444, ECO:0000269|PubMed:7440581}.
CC   -!- SUBUNIT: Heterotrimer of 3 chains: alpha, beta and gamma. The
CC       alpha and gamma chains are disulfide bonded. Component of the
CC       membrane attack complex (MAC). MAC assembly is initiated by
CC       proteolytic cleavage of C5 into C5a and C5b. C5b sequentially
CC       binds C6, C7, C8 and multiple copies of the pore-forming subunit
CC       C9. {ECO:0000269|PubMed:17692377, ECO:0000269|PubMed:18440555,
CC       ECO:0000269|PubMed:7440581}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Cell membrane; Multi-pass membrane
CC       protein. Note=Secreted as soluble protein. Inserts into the cell
CC       membrane of target cells.
CC   -!- DISEASE: Complement component 8 deficiency, 1 (C8D1) [MIM:613790]:
CC       A rare defect of the complement classical pathway associated with
CC       susceptibility to severe recurrent infections, predominantly by
CC       Neisseria gonorrhoeae or Neisseria meningitidis. Note=Disease
CC       susceptibility is associated with variations affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC       {ECO:0000305}.
DR   EMBL; M16974; AAA52200.1; -; mRNA.
DR   EMBL; U08006; AAA82124.1; -; Genomic_DNA.
DR   EMBL; U07996; AAA82124.1; JOINED; Genomic_DNA.
DR   EMBL; U07997; AAA82124.1; JOINED; Genomic_DNA.
DR   EMBL; U07998; AAA82124.1; JOINED; Genomic_DNA.
DR   EMBL; U07999; AAA82124.1; JOINED; Genomic_DNA.
DR   EMBL; U08000; AAA82124.1; JOINED; Genomic_DNA.
DR   EMBL; U08001; AAA82124.1; JOINED; Genomic_DNA.
DR   EMBL; U08002; AAA82124.1; JOINED; Genomic_DNA.
DR   EMBL; U08003; AAA82124.1; JOINED; Genomic_DNA.
DR   EMBL; U08004; AAA82124.1; JOINED; Genomic_DNA.
DR   EMBL; U08005; AAA82124.1; JOINED; Genomic_DNA.
DR   EMBL; AL121998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC132911; AAI32912.1; -; mRNA.
DR   EMBL; BC132913; AAI32914.1; -; mRNA.
DR   CCDS; CCDS606.1; -.
DR   PIR; I37213; C8HUA.
DR   RefSeq; NP_000553.1; NM_000562.2.
DR   PDB; 2QOS; X-ray; 1.81 A; A=188-198.
DR   PDB; 2QQH; X-ray; 2.50 A; A=133-366, A=410-492.
DR   PDB; 2RD7; X-ray; 2.15 A; A=133-492.
DR   PDB; 3OJY; X-ray; 2.51 A; A=31-584.
DR   PDB; 6H03; EM; 5.60 A; F=31-584.
DR   PDB; 6H04; EM; 5.60 A; F=31-584.
DR   PDBsum; 2QOS; -.
DR   PDBsum; 2QQH; -.
DR   PDBsum; 2RD7; -.
DR   PDBsum; 3OJY; -.
DR   PDBsum; 6H03; -.
DR   PDBsum; 6H04; -.
DR   SMR; P07357; -.
DR   BioGrid; 107192; 13.
DR   DIP; DIP-1125N; -.
DR   IntAct; P07357; 2.
DR   STRING; 9606.ENSP00000354458; -.
DR   TCDB; 1.C.39.3.1; the membrane attack complex/perforin (macpf) family.
DR   GlyConnect; 1148; -.
DR   iPTMnet; P07357; -.
DR   PhosphoSitePlus; P07357; -.
DR   BioMuta; C8A; -.
DR   DMDM; 729167; -.
DR   CPTAC; CPTAC-667; -.
DR   jPOST; P07357; -.
DR   MaxQB; P07357; -.
DR   PaxDb; P07357; -.
DR   PeptideAtlas; P07357; -.
DR   PRIDE; P07357; -.
DR   ProteomicsDB; 51997; -.
DR   DNASU; 731; -.
DR   Ensembl; ENST00000361249; ENSP00000354458; ENSG00000157131.
DR   GeneID; 731; -.
DR   KEGG; hsa:731; -.
DR   UCSC; uc001cyo.3; human.
DR   CTD; 731; -.
DR   DisGeNET; 731; -.
DR   GeneCards; C8A; -.
DR   HGNC; HGNC:1352; C8A.
DR   MalaCards; C8A; -.
DR   MIM; 120950; gene.
DR   MIM; 613790; phenotype.
DR   neXtProt; NX_P07357; -.
DR   OpenTargets; ENSG00000157131; -.
DR   Orphanet; 169150; Immunodeficiency due to a late component of complement deficiency.
DR   PharmGKB; PA25951; -.
DR   eggNOG; ENOG410IE8U; Eukaryota.
DR   eggNOG; ENOG410Y5MF; LUCA.
DR   GeneTree; ENSGT00940000160126; -.
DR   HOGENOM; HOG000231146; -.
DR   InParanoid; P07357; -.
DR   KO; K03997; -.
DR   OMA; MRIFTKV; -.
DR   OrthoDB; 787014at2759; -.
DR   PhylomeDB; P07357; -.
DR   TreeFam; TF330498; -.
DR   Reactome; R-HSA-166665; Terminal pathway of complement.
DR   Reactome; R-HSA-977606; Regulation of Complement cascade.
DR   ChiTaRS; C8A; human.
DR   EvolutionaryTrace; P07357; -.
DR   GenomeRNAi; 731; -.
DR   PRO; PR:P07357; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000157131; Expressed in 33 organ(s), highest expression level in right lobe of liver.
DR   Genevisible; P07357; HS.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB.
DR   GO; GO:0001848; F:complement binding; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0006956; P:complement activation; IDA:MGI.
DR   GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 2.20.100.10; -; 2.
DR   Gene3D; 4.10.400.10; -; 1.
DR   InterPro; IPR037565; Complement_C8_alpha.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR001862; MAC_perforin.
DR   InterPro; IPR020864; MACPF.
DR   InterPro; IPR020863; MACPF_CS.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR45742:SF1; PTHR45742:SF1; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF01823; MACPF; 1.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR00764; COMPLEMENTC9.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00457; MACPF; 1.
DR   SMART; SM00209; TSP1; 2.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   SUPFAM; SSF82895; SSF82895; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS00279; MACPF_1; 1.
DR   PROSITE; PS51412; MACPF_2; 1.
DR   PROSITE; PS50092; TSP1; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cleavage on pair of basic residues;
KW   Complement alternate pathway; Complement pathway; Complete proteome;
KW   Cytolysis; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Immunity; Innate immunity; Membrane;
KW   Membrane attack complex; Polymorphism; Reference proteome; Repeat;
KW   Secreted; Signal; Transmembrane; Transmembrane beta strand.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   PROPEP       21     30       {ECO:0000255}.
FT                                /FTId=PRO_0000023585.
FT   CHAIN        31    584       Complement component C8 alpha chain.
FT                                /FTId=PRO_0000023586.
FT   DOMAIN       38     91       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN       94    132       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      135    498       MACPF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00745}.
FT   DOMAIN      499    529       EGF-like.
FT   DOMAIN      539    583       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   SITE         43     43       Not glycosylated.
FT   CARBOHYD     44     44       C-linked (Man) tryptophan.
FT                                {ECO:0000269|PubMed:10551839}.
FT   CARBOHYD    437    437       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    542    542       C-linked (Man) tryptophan.
FT                                {ECO:0000269|PubMed:10551839}.
FT   CARBOHYD    545    545       C-linked (Man) tryptophan.
FT                                {ECO:0000269|PubMed:10551839}.
FT   CARBOHYD    548    548       C-linked (Man) tryptophan.
FT                                {ECO:0000269|PubMed:10551839}.
FT   DISULFID     39     74       {ECO:0000250}.
FT   DISULFID     50     53       {ECO:0000250}.
FT   DISULFID     84     90       {ECO:0000250}.
FT   DISULFID     96    108       {ECO:0000250}.
FT   DISULFID    102    121       {ECO:0000250}.
FT   DISULFID    115    130       {ECO:0000250}.
FT   DISULFID    140    177
FT   DISULFID    194    194       Interchain (with C-60 in C8-gamma chain).
FT   DISULFID    375    399
FT   VARIANT      93     93       Q -> K (in allele C8A*B; dbSNP:rs652785).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:7649542}.
FT                                /FTId=VAR_011889.
FT   VARIANT     407    407       T -> I (in dbSNP:rs706479).
FT                                /FTId=VAR_011890.
FT   VARIANT     458    458       D -> N (in dbSNP:rs17114555).
FT                                /FTId=VAR_033800.
FT   VARIANT     485    485       R -> L (in dbSNP:rs1620075).
FT                                /FTId=VAR_011891.
FT   VARIANT     561    561       E -> Q (in dbSNP:rs1342440).
FT                                /FTId=VAR_011892.
FT   VARIANT     575    575       P -> L (in dbSNP:rs17300936).
FT                                /FTId=VAR_033801.
FT   CONFLICT    575    575       P -> S (in Ref. 3; AAA82124).
FT                                {ECO:0000305}.
FT   TURN         52     54       {ECO:0000244|PDB:3OJY}.
FT   STRAND       56     60       {ECO:0000244|PDB:3OJY}.
FT   STRAND       63     65       {ECO:0000244|PDB:3OJY}.
FT   STRAND       78     83       {ECO:0000244|PDB:3OJY}.
FT   STRAND       97    101       {ECO:0000244|PDB:3OJY}.
FT   STRAND      103    105       {ECO:0000244|PDB:3OJY}.
FT   HELIX       111    113       {ECO:0000244|PDB:3OJY}.
FT   STRAND      116    118       {ECO:0000244|PDB:3OJY}.
FT   STRAND      121    123       {ECO:0000244|PDB:3OJY}.
FT   STRAND      127    129       {ECO:0000244|PDB:3OJY}.
FT   STRAND      140    143       {ECO:0000244|PDB:2QQH}.
FT   HELIX       149    152       {ECO:0000244|PDB:2RD7}.
FT   STRAND      154    157       {ECO:0000244|PDB:2RD7}.
FT   TURN        158    161       {ECO:0000244|PDB:2RD7}.
FT   STRAND      162    168       {ECO:0000244|PDB:2RD7}.
FT   STRAND      179    182       {ECO:0000244|PDB:2RD7}.
FT   TURN        183    186       {ECO:0000244|PDB:2QQH}.
FT   STRAND      189    191       {ECO:0000244|PDB:2QOS}.
FT   TURN        192    195       {ECO:0000244|PDB:2QOS}.
FT   STRAND      196    198       {ECO:0000244|PDB:2QOS}.
FT   HELIX       201    203       {ECO:0000244|PDB:3OJY}.
FT   STRAND      204    207       {ECO:0000244|PDB:2RD7}.
FT   STRAND      212    217       {ECO:0000244|PDB:2RD7}.
FT   STRAND      226    232       {ECO:0000244|PDB:2RD7}.
FT   HELIX       233    243       {ECO:0000244|PDB:2RD7}.
FT   STRAND      246    252       {ECO:0000244|PDB:2RD7}.
FT   STRAND      260    266       {ECO:0000244|PDB:2RD7}.
FT   HELIX       273    280       {ECO:0000244|PDB:2RD7}.
FT   STRAND      287    303       {ECO:0000244|PDB:2RD7}.
FT   STRAND      305    308       {ECO:0000244|PDB:2RD7}.
FT   HELIX       312    319       {ECO:0000244|PDB:2RD7}.
FT   HELIX       327    337       {ECO:0000244|PDB:2RD7}.
FT   STRAND      339    358       {ECO:0000244|PDB:2RD7}.
FT   HELIX       359    365       {ECO:0000244|PDB:2RD7}.
FT   HELIX       369    379       {ECO:0000244|PDB:2RD7}.
FT   HELIX       398    402       {ECO:0000244|PDB:2RD7}.
FT   HELIX       408    413       {ECO:0000244|PDB:2RD7}.
FT   STRAND      416    421       {ECO:0000244|PDB:2RD7}.
FT   HELIX       443    449       {ECO:0000244|PDB:2RD7}.
FT   TURN        450    452       {ECO:0000244|PDB:2RD7}.
FT   STRAND      455    463       {ECO:0000244|PDB:2RD7}.
FT   HELIX       464    470       {ECO:0000244|PDB:2RD7}.
FT   HELIX       477    491       {ECO:0000244|PDB:2RD7}.
FT   HELIX       496    498       {ECO:0000244|PDB:3OJY}.
FT   TURN        503    505       {ECO:0000244|PDB:3OJY}.
FT   STRAND      508    511       {ECO:0000244|PDB:3OJY}.
FT   STRAND      514    517       {ECO:0000244|PDB:3OJY}.
FT   STRAND      525    527       {ECO:0000244|PDB:3OJY}.
FT   STRAND      552    554       {ECO:0000244|PDB:3OJY}.
FT   STRAND      556    559       {ECO:0000244|PDB:3OJY}.
FT   STRAND      578    582       {ECO:0000244|PDB:3OJY}.
SQ   SEQUENCE   584 AA;  65163 MW;  9F61DDA51D2F3BBA CRC64;
     MFAVVFFILS LMTCQPGVTA QEKVNQRVRR AATPAAVTCQ LSNWSEWTDC FPCQDKKYRH
     RSLLQPNKFG GTICSGDIWD QASCSSSTTC VRQAQCGQDF QCKETGRCLK RHLVCNGDQD
     CLDGSDEDDC EDVRAIDEDC SQYEPIPGSQ KAALGYNILT QEDAQSVYDA SYYGGQCETV
     YNGEWRELRY DSTCERLYYG DDEKYFRKPY NFLKYHFEAL ADTGISSEFY DNANDLLSKV
     KKDKSDSFGV TIGIGPAGSP LLVGVGVSHS QDTSFLNELN KYNEKKFIFT RIFTKVQTAH
     FKMRKDDIML DEGMLQSLME LPDQYNYGMY AKFINDYGTH YITSGSMGGI YEYILVIDKA
     KMESLGITSR DITTCFGGSL GIQYEDKINV GGGLSGDHCK KFGGGKTERA RKAMAVEDII
     SRVRGGSSGW SGGLAQNRST ITYRSWGRSL KYNPVVIDFE MQPIHEVLRH TSLGPLEAKR
     QNLRRALDQY LMEFNACRCG PCFNNGVPIL EGTSCRCQCR LGSLGAACEQ TQTEGAKADG
     SWSCWSSWSV CRAGIQERRR ECDNPAPQNG GASCPGRKVQ TQAC
//
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