GENTAUR Molecular Products.

 CO8B_HUMAN              Reviewed;         591 AA.
 P07358; A1L4K7;
 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
 23-JAN-2002, sequence version 3.
 28-FEB-2018, entry version 180.
 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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 Distributed under the Creative Commons Attribution-NoDerivs License
 -----------------------------------------------------------------------
 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.
 ChiTaRS; C8B; human.
 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; HDA:UniProtKB.
 GO; GO:0005576; C:extracellular region; TAS:Reactome.
 GO; GO:1903561; C:extracellular vesicle; HDA: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; IPR037566; Complement_C8_beta.
 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.
 PANTHER; PTHR19325:SF401; PTHR19325:SF401; 1.
 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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