CO8B_HUMAN
ID CO8B_HUMAN Reviewed; 591 AA.
AC P07358; A1L4K7;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Complement component C8 beta chain;
DE AltName: Full=Complement component 8 subunit beta;
DE Flags: Precursor;
GN Name=C8B;
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], PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION.
RC TISSUE=Liver;
RX PubMed=2820472; DOI=10.1021/bi00386a047;
RA Howard O.M.Z., Rao A.G., Sodetz J.M.;
RT "Complementary DNA and derived amino acid sequence of the beta subunit of
RT human complement protein C8: identification of a close structural and
RT ancestral relationship to the alpha subunit and C9.";
RL Biochemistry 26:3565-3570(1987).
RN [2]
RP SEQUENCE REVISION.
RA Sodetz J.M.;
RL Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-117.
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 47-591, AND PROTEIN SEQUENCE OF 55-68.
RC TISSUE=Liver;
RX PubMed=3651397; DOI=10.1021/bi00386a045;
RA Haefliger J.-A., Tschopp J., Nardelli D., Wahli W., Kocher H.-P., Tosi M.,
RA Stanley K.K.;
RT "Complementary DNA cloning of complement C8 beta and its sequence homology
RT to C9.";
RL Biochemistry 26:3551-3556(1987).
RN [8]
RP PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, 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 [9]
RP GLYCOSYLATION AT TRP-70; TRP-73; TRP-551 AND TRP-554.
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 [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-243.
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 [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-243.
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 [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 55-591, PHOSPHORYLATION AT
RP THR-418, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=21454577; DOI=10.1074/jbc.m111.219766;
RA Lovelace L.L., Cooper C.L., Sodetz J.M., Lebioda L.;
RT "Structure of human C8 protein provides mechanistic insight into membrane
RT pore formation by complement.";
RL J. Biol. Chem. 286:17585-17592(2011).
RN [14]
RP VARIANT GLY-117, AND DEFINITION OF ALLOTYPES C8B A AND C8B B.
RX PubMed=8131848; DOI=10.1016/0014-5793(94)80140-1;
RA Dewald G., Hemmer S., Noethen M.M.;
RT "Human complement component C8. Molecular basis of the beta-chain
RT polymorphism.";
RL FEBS Lett. 340:211-215(1994).
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.
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 binds sequentially C6, C7, C8 and multiple copies
CC of the pore-forming subunit C9. {ECO:0000269|PubMed:21454577,
CC ECO:0000269|PubMed:7440581}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: N-glycosylated; contains one or two bound glycans. Not O-
CC glycosylated. {ECO:0000269|PubMed:10551839,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:2820472}.
CC -!- POLYMORPHISM: The sequence shown is that of allotype C8B B.
CC -!- DISEASE: Complement component 8 deficiency, 2 (C8D2) [MIM:613789]: 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}.
CC -!- WEB RESOURCE: Name=C8Bbase; Note=C8B mutation db;
CC URL="http://structure.bmc.lu.se/idbase/C8Bbase/";
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DR EMBL; M16973; AAA51862.1; -; mRNA.
DR EMBL; AK313382; BAG36180.1; -; mRNA.
DR EMBL; AL121998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06641.1; -; Genomic_DNA.
DR EMBL; BC130575; AAI30576.1; -; mRNA.
DR EMBL; X04393; CAA27981.1; -; mRNA.
DR CCDS; CCDS30730.1; -.
DR PIR; A43071; C8HUB.
DR RefSeq; NP_000057.2; NM_000066.3.
DR RefSeq; XP_016857724.1; XM_017002235.1.
DR PDB; 3OJY; X-ray; 2.51 A; B=55-591.
DR PDB; 6H03; EM; 5.60 A; C=55-591.
DR PDB; 6H04; EM; 5.60 A; C=55-591.
DR PDB; 7NYC; EM; 3.50 A; D=55-591.
DR PDB; 7NYD; EM; 3.30 A; D=55-591.
DR PDBsum; 3OJY; -.
DR PDBsum; 6H03; -.
DR PDBsum; 6H04; -.
DR PDBsum; 7NYC; -.
DR PDBsum; 7NYD; -.
DR AlphaFoldDB; P07358; -.
DR SMR; P07358; -.
DR BioGRID; 107193; 25.
DR ComplexPortal; CPX-6159; Membrane attack complex.
DR IntAct; P07358; 1.
DR STRING; 9606.ENSP00000360281; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR GlyConnect; 1149; 3 N-Linked glycans (1 site).
DR GlyGen; P07358; 6 sites, 4 N-linked glycans (1 site).
DR iPTMnet; P07358; -.
DR PhosphoSitePlus; P07358; -.
DR BioMuta; C8B; -.
DR DMDM; 20141201; -.
DR jPOST; P07358; -.
DR MassIVE; P07358; -.
DR PaxDb; P07358; -.
DR PeptideAtlas; P07358; -.
DR PRIDE; P07358; -.
DR ProteomicsDB; 51998; -.
DR Antibodypedia; 19370; 211 antibodies from 27 providers.
DR DNASU; 732; -.
DR Ensembl; ENST00000371237.9; ENSP00000360281.4; ENSG00000021852.13.
DR GeneID; 732; -.
DR KEGG; hsa:732; -.
DR UCSC; uc001cyp.5; human.
DR CTD; 732; -.
DR DisGeNET; 732; -.
DR GeneCards; C8B; -.
DR HGNC; HGNC:1353; C8B.
DR HPA; ENSG00000021852; Tissue enriched (liver).
DR MalaCards; C8B; -.
DR MIM; 120960; gene.
DR MIM; 613789; phenotype.
DR neXtProt; NX_P07358; -.
DR Orphanet; 169150; Immunodeficiency due to a late component of complement deficiency.
DR PharmGKB; PA25952; -.
DR VEuPathDB; HostDB:ENSG00000021852; -.
DR eggNOG; KOG3535; Eukaryota.
DR InParanoid; P07358; -.
DR OrthoDB; 787014at2759; -.
DR PhylomeDB; P07358; -.
DR TreeFam; TF330498; -.
DR PathwayCommons; P07358; -.
DR Reactome; R-HSA-166665; Terminal pathway of complement.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SignaLink; P07358; -.
DR SIGNOR; P07358; -.
DR BioGRID-ORCS; 732; 13 hits in 1066 CRISPR screens.
DR EvolutionaryTrace; P07358; -.
DR GenomeRNAi; 732; -.
DR Pharos; P07358; Tbio.
DR PRO; PR:P07358; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P07358; protein.
DR Bgee; ENSG00000021852; Expressed in right lobe of liver and 78 other tissues.
DR ExpressionAtlas; P07358; baseline and differential.
DR Genevisible; P07358; HS.
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:1903561; C:extracellular vesicle; HDA:UniProtKB.
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:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0006956; P:complement activation; IBA:GO_Central.
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; IPR037566; Complement_C8_beta.
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:SF5; PTHR45742:SF5; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF01823; MACPF; 1.
DR Pfam; PF00090; TSP_1; 2.
DR PRINTS; PR00764; COMPLEMENTC9.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00457; MACPF; 1.
DR SMART; SM00209; TSP1; 2.
DR SUPFAM; SSF57424; SSF57424; 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; Complement alternate pathway; Complement pathway; Cytolysis;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Immunity; Innate immunity; Membrane attack complex; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT PROPEP 33..54
FT /evidence="ECO:0000269|PubMed:3651397"
FT /id="PRO_0000023591"
FT CHAIN 55..591
FT /note="Complement component C8 beta chain"
FT /id="PRO_0000023592"
FT DOMAIN 64..117
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 120..157
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 158..504
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 505..535
FT /note="EGF-like"
FT DOMAIN 545..591
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 568..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 418
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21454577"
FT CARBOHYD 70
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10551839"
FT CARBOHYD 73
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10551839"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 551
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10551839"
FT CARBOHYD 554
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10551839"
FT DISULFID 65..100
FT /evidence="ECO:0000269|PubMed:21454577"
FT DISULFID 76..110
FT /evidence="ECO:0000269|PubMed:21454577"
FT DISULFID 79..116
FT /evidence="ECO:0000269|PubMed:21454577"
FT DISULFID 122..133
FT /evidence="ECO:0000269|PubMed:21454577"
FT DISULFID 127..146
FT /evidence="ECO:0000269|PubMed:21454577"
FT DISULFID 140..155
FT /evidence="ECO:0000269|PubMed:21454577"
FT DISULFID 378..403
FT /evidence="ECO:0000269|PubMed:21454577"
FT DISULFID 503..550
FT /evidence="ECO:0000269|PubMed:21454577"
FT DISULFID 505..521
FT /evidence="ECO:0000269|PubMed:21454577"
FT DISULFID 508..523
FT /evidence="ECO:0000269|PubMed:21454577"
FT DISULFID 525..534
FT /evidence="ECO:0000269|PubMed:21454577"
FT DISULFID 557..590
FT /evidence="ECO:0000269|PubMed:21454577"
FT VARIANT 108
FT /note="E -> K (in dbSNP:rs12067507)"
FT /id="VAR_027649"
FT VARIANT 117
FT /note="R -> G (in allotype C8B A; dbSNP:rs1013579)"
FT /evidence="ECO:0000269|PubMed:16710414,
FT ECO:0000269|PubMed:8131848"
FT /id="VAR_012642"
FT VARIANT 261
FT /note="P -> L (in dbSNP:rs12085435)"
FT /id="VAR_027650"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:3OJY"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3OJY"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:3OJY"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:3OJY"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 315..321
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 342..352
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:3OJY"
FT TURN 366..369
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 372..378
FT /evidence="ECO:0007829|PDB:3OJY"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:3OJY"
FT TURN 404..408
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:3OJY"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 419..426
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 435..439
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 449..457
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 461..469
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:3OJY"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 482..499
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 513..517
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 520..524
FT /evidence="ECO:0007829|PDB:3OJY"
FT HELIX 532..534
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 536..541
FT /evidence="ECO:0007829|PDB:3OJY"
FT STRAND 557..563
FT /evidence="ECO:0007829|PDB:3OJY"
FT TURN 567..569
FT /evidence="ECO:0007829|PDB:7NYC"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 584..588
FT /evidence="ECO:0007829|PDB:3OJY"
SQ 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
