CO8A_HUMAN
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 03-AUG-2022, entry version 218.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Sodetz J.M.;
RT "Complementary DNA and derived amino acid sequence of the alpha subunit of
RT human complement protein C8: evidence for the existence of a separate alpha
RT 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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RX PubMed=7440581; DOI=10.1016/s0021-9258(19)70233-6;
RA Steckel E.W., York R.G., Monahan J.B., Sodetz J.M.;
RT "The eighth component of human complement. Purification and physicochemical
RT 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-mannosylated
RT 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., Moore R.J.,
RA 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 multiple
RT 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT 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, AND
RP 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., Sodetz J.M.;
RT "Crystal structure of the MACPF domain of human complement protein C8 alpha
RT 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 peptide
RT containing the C8gamma binding site on C8alpha: implications for C8gamma
RT 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 (C81)
RT polymorphism.";
RL Hum. Genet. 96:281-284(1995).
CC -!- FUNCTION: Constituent of the membrane attack complex (MAC) that plays a
CC key role in the innate and adaptive immune response by forming pores in
CC the plasma membrane of target cells. C8A inserts into the target
CC 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 alpha and
CC gamma chains are disulfide bonded. Component of the membrane attack
CC complex (MAC). MAC assembly is initiated by proteolytic cleavage of C5
CC into C5a and C5b. C5b sequentially binds C6, C7, C8 and multiple copies
CC of the pore-forming subunit C9. {ECO:0000269|PubMed:17692377,
CC ECO:0000269|PubMed:18440555, ECO:0000269|PubMed:7440581}.
CC -!- INTERACTION:
CC P07357; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-9021639, EBI-17231387;
CC P07357; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-9021639, EBI-13345167;
CC P07357; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-9021639, EBI-6163737;
CC P07357; Q14973: SLC10A1; NbExp=3; IntAct=EBI-9021639, EBI-3923031;
CC P07357; P30825: SLC7A1; NbExp=3; IntAct=EBI-9021639, EBI-4289564;
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]: A
CC 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 variants affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC {ECO:0000305}.
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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 PDB; 7NYC; EM; 3.50 A; E=31-584.
DR PDB; 7NYD; EM; 3.30 A; E=31-584.
DR PDBsum; 2QOS; -.
DR PDBsum; 2QQH; -.
DR PDBsum; 2RD7; -.
DR PDBsum; 3OJY; -.
DR PDBsum; 6H03; -.
DR PDBsum; 6H04; -.
DR PDBsum; 7NYC; -.
DR PDBsum; 7NYD; -.
DR AlphaFoldDB; P07357; -.
DR SMR; P07357; -.
DR BioGRID; 107192; 21.
DR ComplexPortal; CPX-6159; Membrane attack complex.
DR DIP; DIP-1125N; -.
DR IntAct; P07357; 6.
DR STRING; 9606.ENSP00000354458; -.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR TCDB; 1.C.39.3.1; the membrane attack complex/perforin (macpf) family.
DR GlyConnect; 1148; 3 N-Linked glycans (1 site).
DR GlyGen; P07357; 5 sites, 6 N-linked glycans (1 site).
DR iPTMnet; P07357; -.
DR PhosphoSitePlus; P07357; -.
DR BioMuta; C8A; -.
DR DMDM; 729167; -.
DR CPTAC; CPTAC-667; -.
DR jPOST; P07357; -.
DR MassIVE; P07357; -.
DR MaxQB; P07357; -.
DR PaxDb; P07357; -.
DR PeptideAtlas; P07357; -.
DR PRIDE; P07357; -.
DR ProteomicsDB; 51997; -.
DR Antibodypedia; 19367; 58 antibodies from 18 providers.
DR DNASU; 731; -.
DR Ensembl; ENST00000361249.4; ENSP00000354458.3; ENSG00000157131.11.
DR GeneID; 731; -.
DR KEGG; hsa:731; -.
DR MANE-Select; ENST00000361249.4; ENSP00000354458.3; NM_000562.3; NP_000553.1.
DR UCSC; uc001cyo.3; human.
DR CTD; 731; -.
DR DisGeNET; 731; -.
DR GeneCards; C8A; -.
DR HGNC; HGNC:1352; C8A.
DR HPA; ENSG00000157131; Tissue enriched (liver).
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 VEuPathDB; HostDB:ENSG00000157131; -.
DR eggNOG; ENOG502QT87; Eukaryota.
DR GeneTree; ENSGT00940000160126; -.
DR HOGENOM; CLU_032453_1_0_1; -.
DR InParanoid; P07357; -.
DR OMA; EQYDFGM; -.
DR OrthoDB; 787014at2759; -.
DR PhylomeDB; P07357; -.
DR TreeFam; TF330498; -.
DR PathwayCommons; P07357; -.
DR Reactome; R-HSA-166665; Terminal pathway of complement.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SignaLink; P07357; -.
DR SIGNOR; P07357; -.
DR BioGRID-ORCS; 731; 8 hits in 1067 CRISPR screens.
DR ChiTaRS; C8A; human.
DR EvolutionaryTrace; P07357; -.
DR GenomeRNAi; 731; -.
DR Pharos; P07357; Tbio.
DR PRO; PR:P07357; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P07357; protein.
DR Bgee; ENSG00000157131; Expressed in right lobe of liver and 47 other tissues.
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; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
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:0050778; P:positive regulation of immune response; IC:ComplexPortal.
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; Cytolysis;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Immunity; Innate immunity; Membrane; Membrane attack complex;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane beta strand.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..30
FT /evidence="ECO:0000255"
FT /id="PRO_0000023585"
FT CHAIN 31..584
FT /note="Complement component C8 alpha chain"
FT /id="PRO_0000023586"
FT DOMAIN 38..91
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 94..132
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 135..498
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 499..529
FT /note="EGF-like"
FT DOMAIN 539..583
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 562..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 43
FT /note="Not glycosylated"
FT CARBOHYD 44
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10551839"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 542
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10551839"
FT CARBOHYD 545
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10551839"
FT CARBOHYD 548
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10551839"
FT DISULFID 39..74
FT /evidence="ECO:0000250"
FT DISULFID 50..53
FT /evidence="ECO:0000250"
FT DISULFID 84..90
FT /evidence="ECO:0000250"
FT DISULFID 96..108
FT /evidence="ECO:0000250"
FT DISULFID 102..121
FT /evidence="ECO:0000250"
FT DISULFID 115..130
FT /evidence="ECO:0000250"
FT DISULFID 140..177
FT DISULFID 194
FT /note="Interchain (with C-60 in C8-gamma chain)"
FT DISULFID 375..399
FT VARIANT 93
FT /note="Q -> K (in allele C8A*B; dbSNP:rs652785)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7649542"
FT /id="VAR_011889"
FT VARIANT 407
FT /note="T -> I (in dbSNP:rs706479)"
FT /id="VAR_011890"
FT VARIANT 458
FT /note="D -> N (in dbSNP:rs17114555)"
FT /id="VAR_033800"
FT VARIANT 485
FT /note="R -> L (in dbSNP:rs1620075)"
FT /id="VAR_011891"
FT VARIANT 561
FT /note="E -> Q (in dbSNP:rs1342440)"
FT /id="VAR_011892"
FT VARIANT 575
FT /note="P -> L (in dbSNP:rs17300936)"
FT /id="VAR_033801"
FT CONFLICT 575
FT /note="P -> S (in Ref. 3; AAA82124)"
FT /evidence="ECO:0000305"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:7NYC"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:2QQH"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:2RD7"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2RD7"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:2RD7"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:2RD7"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:2RD7"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:2QQH"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2QOS"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:2QOS"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2QOS"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:2RD7"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:2RD7"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:2RD7"
FT HELIX 233..243
FT /evidence="ECO:0007829|PDB:2RD7"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:2RD7"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:2RD7"
FT HELIX 273..280
FT /evidence="ECO:0007829|PDB:2RD7"
FT STRAND 287..303
FT /evidence="ECO:0007829|PDB:2RD7"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:2RD7"
FT HELIX 312..319
FT /evidence="ECO:0007829|PDB:2RD7"
FT HELIX 327..337
FT /evidence="ECO:0007829|PDB:2RD7"
FT STRAND 339..358
FT /evidence="ECO:0007829|PDB:2RD7"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:2RD7"
FT HELIX 369..379
FT /evidence="ECO:0007829|PDB:2RD7"
FT HELIX 398..402
FT /evidence="ECO:0007829|PDB:2RD7"
FT HELIX 408..413
FT /evidence="ECO:0007829|PDB:2RD7"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:2RD7"
FT HELIX 428..436
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 443..449
FT /evidence="ECO:0007829|PDB:2RD7"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:2RD7"
FT STRAND 455..463
FT /evidence="ECO:0007829|PDB:2RD7"
FT HELIX 464..470
FT /evidence="ECO:0007829|PDB:2RD7"
FT HELIX 477..491
FT /evidence="ECO:0007829|PDB:2RD7"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:3OJY"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 567..570
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 578..582
FT /evidence="ECO:0007829|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
