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Complement component C8 beta chain (Complement component 8 subunit beta)

 CO8B_HUMAN              Reviewed;         591 AA.
P07358; A1L4K7;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 3.
25-OCT-2017, entry version 178.
RecName: Full=Complement component C8 beta chain;
AltName: Full=Complement component 8 subunit beta;
Flags: Precursor;
Name=C8B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
GLYCOSYLATION.
TISSUE=Liver;
PubMed=2820472; DOI=10.1021/bi00386a047;
Howard O.M.Z., Rao A.G., Sodetz J.M.;
"Complementary DNA and derived amino acid sequence of the beta subunit
of human complement protein C8: identification of a close structural
and ancestral relationship to the alpha subunit and C9.";
Biochemistry 26:3565-3570(1987).
[2]
SEQUENCE REVISION.
Sodetz J.M.;
Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-117.
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 47-591, AND PROTEIN SEQUENCE OF 55-68.
TISSUE=Liver;
PubMed=3651397; DOI=10.1021/bi00386a045;
Haefliger J.-A., Tschopp J., Nardelli D., Wahli W., Kocher H.-P.,
Tosi M., Stanley K.K.;
"Complementary DNA cloning of complement C8 beta and its sequence
homology to C9.";
Biochemistry 26:3551-3556(1987).
[8]
PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, AND SUBUNIT.
PubMed=7440581;
Steckel E.W., York R.G., Monahan J.B., Sodetz J.M.;
"The eighth component of human complement. Purification and
physicochemical characterization of its unusual subunit structure.";
J. Biol. Chem. 255:11997-12005(1980).
[9]
GLYCOSYLATION AT TRP-70; TRP-73; TRP-551 AND TRP-554.
PubMed=10551839; DOI=10.1074/jbc.274.46.32786;
Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O.;
"The four terminal components of the complement system are C-
mannosylated on multiple tryptophan residues.";
J. Biol. Chem. 274:32786-32794(1999).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-243.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-243.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 55-591, PHOSPHORYLATION AT
THR-418, SUBUNIT, AND DISULFIDE BONDS.
PubMed=21454577; DOI=10.1074/jbc.M111.219766;
Lovelace L.L., Cooper C.L., Sodetz J.M., Lebioda L.;
"Structure of human C8 protein provides mechanistic insight into
membrane pore formation by complement.";
J. Biol. Chem. 286:17585-17592(2011).
[14]
VARIANT GLY-117, AND DEFINITION OF ALLOTYPES C8B A AND C8B B.
PubMed=8131848; DOI=10.1016/0014-5793(94)80140-1;
Dewald G., Hemmer S., Noethen M.M.;
"Human complement component C8. Molecular basis of the beta-chain
polymorphism.";
FEBS Lett. 340:211-215(1994).
-!- FUNCTION: Constituent of the membrane attack complex (MAC) that
plays a key role in the innate and adaptive immune response by
forming pores in the plasma membrane of target cells.
-!- SUBUNIT: Heterotrimer of 3 chains: alpha, beta and gamma. The
alpha and gamma chains are disulfide bonded. Component of the
membrane attack complex (MAC). MAC assembly is initiated by
proteolytic cleavage of C5 into C5a and C5b. C5b binds
sequentially C6, C7, C8 and multiple copies of the pore-forming
subunit C9. {ECO:0000269|PubMed:21454577,
ECO:0000269|PubMed:7440581}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: N-glycosylated; contains one or two bound glycans. Not O-
glycosylated. {ECO:0000269|PubMed:10551839,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:2820472}.
-!- POLYMORPHISM: The sequence shown is that of allotype C8B B.
-!- DISEASE: Complement component 8 deficiency, 2 (C8D2) [MIM:613789]:
A rare defect of the complement classical pathway associated with
susceptibility to severe recurrent infections, predominantly by
Neisseria gonorrhoeae or Neisseria meningitidis. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=C8Bbase; Note=C8B mutation db;
URL="http://structure.bmc.lu.se/idbase/C8Bbase/";
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EMBL; M16973; AAA51862.1; -; mRNA.
EMBL; AK313382; BAG36180.1; -; mRNA.
EMBL; AL121998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX06641.1; -; Genomic_DNA.
EMBL; BC130575; AAI30576.1; -; mRNA.
EMBL; X04393; CAA27981.1; -; mRNA.
CCDS; CCDS30730.1; -.
PIR; A43071; C8HUB.
RefSeq; NP_000057.2; NM_000066.3.
RefSeq; XP_016857724.1; XM_017002235.1.
UniGene; Hs.391835; -.
PDB; 3OJY; X-ray; 2.51 A; B=55-591.
PDBsum; 3OJY; -.
ProteinModelPortal; P07358; -.
SMR; P07358; -.
BioGrid; 107193; 6.
STRING; 9606.ENSP00000360281; -.
iPTMnet; P07358; -.
PhosphoSitePlus; P07358; -.
DMDM; 20141201; -.
PaxDb; P07358; -.
PeptideAtlas; P07358; -.
PRIDE; P07358; -.
DNASU; 732; -.
Ensembl; ENST00000371237; ENSP00000360281; ENSG00000021852.
GeneID; 732; -.
KEGG; hsa:732; -.
UCSC; uc001cyp.5; human.
CTD; 732; -.
DisGeNET; 732; -.
EuPathDB; HostDB:ENSG00000021852.12; -.
GeneCards; C8B; -.
HGNC; HGNC:1353; C8B.
HPA; HPA023694; -.
MalaCards; C8B; -.
MIM; 120960; gene.
MIM; 613789; phenotype.
neXtProt; NX_P07358; -.
Orphanet; 169150; Immunodeficiency due to a late component of complements deficiency.
PharmGKB; PA25952; -.
eggNOG; ENOG410IE7H; Eukaryota.
eggNOG; ENOG410Y2J1; LUCA.
HOGENOM; HOG000231146; -.
HOVERGEN; HBG106489; -.
InParanoid; P07358; -.
KO; K03998; -.
OrthoDB; EOG091G07LK; -.
PhylomeDB; P07358; -.
TreeFam; TF330498; -.
Reactome; R-HSA-166665; Terminal pathway of complement.
Reactome; R-HSA-977606; Regulation of Complement cascade.
EvolutionaryTrace; P07358; -.
GenomeRNAi; 732; -.
PRO; PR:P07358; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000021852; -.
CleanEx; HS_C8B; -.
ExpressionAtlas; P07358; baseline and differential.
Genevisible; P07358; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0006956; P:complement activation; TAS:ProtInc.
GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
CDD; cd00112; LDLa; 1.
Gene3D; 2.20.100.10; -; 2.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR001862; MAC_perforin.
InterPro; IPR020864; MACPF.
InterPro; IPR020863; MACPF_CS.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
Pfam; PF00057; Ldl_recept_a; 1.
Pfam; PF01823; MACPF; 1.
Pfam; PF00090; TSP_1; 2.
PRINTS; PR00764; COMPLEMENTC9.
SMART; SM00192; LDLa; 1.
SMART; SM00457; MACPF; 1.
SMART; SM00209; TSP1; 2.
SUPFAM; SSF57424; SSF57424; 1.
SUPFAM; SSF82895; SSF82895; 2.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01209; LDLRA_1; 1.
PROSITE; PS50068; LDLRA_2; 1.
PROSITE; PS00279; MACPF_1; 1.
PROSITE; PS51412; MACPF_2; 1.
PROSITE; PS50092; TSP1; 2.
1: Evidence at protein level;
3D-structure; Complement alternate pathway; Complement pathway;
Complete proteome; Cytolysis; Direct protein sequencing;
Disulfide bond; EGF-like domain; Glycoprotein; Immunity;
Innate immunity; Membrane attack complex; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 32 {ECO:0000255}.
PROPEP 33 54 {ECO:0000269|PubMed:3651397}.
/FTId=PRO_0000023591.
CHAIN 55 591 Complement component C8 beta chain.
/FTId=PRO_0000023592.
DOMAIN 64 117 TSP type-1 1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 120 157 LDL-receptor class A.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 158 504 MACPF. {ECO:0000255|PROSITE-
ProRule:PRU00745}.
DOMAIN 505 535 EGF-like.
DOMAIN 545 591 TSP type-1 2. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
MOD_RES 418 418 Phosphothreonine.
{ECO:0000269|PubMed:21454577}.
CARBOHYD 70 70 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 73 73 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 243 243 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 551 551 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 554 554 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:10551839}.
DISULFID 65 100 {ECO:0000269|PubMed:21454577}.
DISULFID 76 110 {ECO:0000269|PubMed:21454577}.
DISULFID 79 116 {ECO:0000269|PubMed:21454577}.
DISULFID 122 133 {ECO:0000269|PubMed:21454577}.
DISULFID 127 146 {ECO:0000269|PubMed:21454577}.
DISULFID 140 155 {ECO:0000269|PubMed:21454577}.
DISULFID 378 403 {ECO:0000269|PubMed:21454577}.
DISULFID 503 550 {ECO:0000269|PubMed:21454577}.
DISULFID 505 521 {ECO:0000269|PubMed:21454577}.
DISULFID 508 523 {ECO:0000269|PubMed:21454577}.
DISULFID 525 534 {ECO:0000269|PubMed:21454577}.
DISULFID 557 590 {ECO:0000269|PubMed:21454577}.
VARIANT 108 108 E -> K (in dbSNP:rs12067507).
/FTId=VAR_027649.
VARIANT 117 117 R -> G (in allotype C8B A;
dbSNP:rs1013579).
{ECO:0000269|PubMed:16710414,
ECO:0000269|PubMed:8131848}.
/FTId=VAR_012642.
VARIANT 261 261 P -> L (in dbSNP:rs12085435).
/FTId=VAR_027650.
TURN 78 81 {ECO:0000244|PDB:3OJY}.
STRAND 82 86 {ECO:0000244|PDB:3OJY}.
STRAND 89 91 {ECO:0000244|PDB:3OJY}.
STRAND 104 109 {ECO:0000244|PDB:3OJY}.
STRAND 123 126 {ECO:0000244|PDB:3OJY}.
TURN 128 130 {ECO:0000244|PDB:3OJY}.
HELIX 136 138 {ECO:0000244|PDB:3OJY}.
STRAND 141 143 {ECO:0000244|PDB:3OJY}.
STRAND 146 149 {ECO:0000244|PDB:3OJY}.
HELIX 172 176 {ECO:0000244|PDB:3OJY}.
STRAND 177 179 {ECO:0000244|PDB:3OJY}.
TURN 181 183 {ECO:0000244|PDB:3OJY}.
STRAND 186 189 {ECO:0000244|PDB:3OJY}.
STRAND 201 205 {ECO:0000244|PDB:3OJY}.
STRAND 208 212 {ECO:0000244|PDB:3OJY}.
STRAND 216 221 {ECO:0000244|PDB:3OJY}.
STRAND 229 236 {ECO:0000244|PDB:3OJY}.
HELIX 237 240 {ECO:0000244|PDB:3OJY}.
TURN 256 258 {ECO:0000244|PDB:3OJY}.
TURN 269 271 {ECO:0000244|PDB:3OJY}.
STRAND 272 275 {ECO:0000244|PDB:3OJY}.
HELIX 276 283 {ECO:0000244|PDB:3OJY}.
STRAND 290 297 {ECO:0000244|PDB:3OJY}.
STRAND 299 306 {ECO:0000244|PDB:3OJY}.
STRAND 308 310 {ECO:0000244|PDB:3OJY}.
HELIX 315 321 {ECO:0000244|PDB:3OJY}.
HELIX 330 340 {ECO:0000244|PDB:3OJY}.
STRAND 342 352 {ECO:0000244|PDB:3OJY}.
STRAND 355 361 {ECO:0000244|PDB:3OJY}.
HELIX 362 365 {ECO:0000244|PDB:3OJY}.
TURN 366 369 {ECO:0000244|PDB:3OJY}.
HELIX 372 378 {ECO:0000244|PDB:3OJY}.
TURN 379 381 {ECO:0000244|PDB:3OJY}.
TURN 404 408 {ECO:0000244|PDB:3OJY}.
HELIX 409 412 {ECO:0000244|PDB:3OJY}.
TURN 413 415 {ECO:0000244|PDB:3OJY}.
STRAND 419 426 {ECO:0000244|PDB:3OJY}.
HELIX 435 439 {ECO:0000244|PDB:3OJY}.
STRAND 441 443 {ECO:0000244|PDB:3OJY}.
HELIX 449 457 {ECO:0000244|PDB:3OJY}.
STRAND 461 469 {ECO:0000244|PDB:3OJY}.
HELIX 470 473 {ECO:0000244|PDB:3OJY}.
TURN 476 478 {ECO:0000244|PDB:3OJY}.
HELIX 482 499 {ECO:0000244|PDB:3OJY}.
HELIX 502 504 {ECO:0000244|PDB:3OJY}.
STRAND 513 517 {ECO:0000244|PDB:3OJY}.
STRAND 520 524 {ECO:0000244|PDB:3OJY}.
HELIX 532 534 {ECO:0000244|PDB:3OJY}.
STRAND 536 541 {ECO:0000244|PDB:3OJY}.
STRAND 557 563 {ECO:0000244|PDB:3OJY}.
STRAND 584 588 {ECO:0000244|PDB:3OJY}.
SEQUENCE 591 AA; 67047 MW; B01722A6F2E9AFCE CRC64;
MKNSRTWAWR APVELFLLCA ALGCLSLPGS RGERPHSFGS NAVNKSFAKS RQMRSVDVTL
MPIDCELSSW SSWTTCDPCQ KKRYRYAYLL QPSQFHGEPC NFSDKEVEDC VTNRPCRSQV
RCEGFVCAQT GRCVNRRLLC NGDNDCGDQS DEANCRRIYK KCQHEMDQYW GIGSLASGIN
LFTNSFEGPV LDHRYYAGGC SPHYILNTRF RKPYNVESYT PQTQGKYEFI LKEYESYSDF
ERNVTEKMAS KSGFSFGFKI PGIFELGISS QSDRGKHYIR RTKRFSHTKS VFLHARSDLE
VAHYKLKPRS LMLHYEFLQR VKRLPLEYSY GEYRDLFRDF GTHYITEAVL GGIYEYTLVM
NKEAMERGDY TLNNVHACAK NDFKIGGAIE EVYVSLGVSV GKCRGILNEI KDRNKRDTMV
EDLVVLVRGG ASEHITTLAY QELPTADLMQ EWGDAVQYNP AIIKVKVEPL YELVTATDFA
YSSTVRQNMK QALEEFQKEV SSCHCAPCQG NGVPVLKGSR CDCICPVGSQ GLACEVSYRK
NTPIDGKWNC WSNWSSCSGR RKTRQRQCNN PPPQNGGSPC SGPASETLDC S


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