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   29-SEP-2021, entry version 215.
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;
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   PDBsum; 2QOS; -.
DR   PDBsum; 2QQH; -.
DR   PDBsum; 2RD7; -.
DR   PDBsum; 3OJY; -.
DR   PDBsum; 6H03; -.
DR   PDBsum; 6H04; -.
DR   SMR; P07357; -.
DR   BioGRID; 107192; 18.
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; 53 antibodies.
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   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; RGTQGYN; -.
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   SIGNOR; P07357; -.
DR   BioGRID-ORCS; 731; 4 hits in 1008 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 50 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; 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   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          78..83
FT                   /evidence="ECO:0007829|PDB:3OJY"
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           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          525..527
FT                   /evidence="ECO:0007829|PDB:3OJY"
FT   STRAND          552..554
FT                   /evidence="ECO:0007829|PDB:3OJY"
FT   STRAND          556..559
FT                   /evidence="ECO:0007829|PDB:3OJY"
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
//
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