GenomeNet

Database: UniProt
Entry: P07358
LinkDB: P07358
Original site: P07358 
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   29-SEP-2021, entry version 200.
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;
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   PDBsum; 3OJY; -.
DR   PDBsum; 6H03; -.
DR   PDBsum; 6H04; -.
DR   SMR; P07358; -.
DR   BioGRID; 107193; 6.
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; 208 antibodies.
DR   DNASU; 732; -.
DR   Ensembl; ENST00000371237; ENSP00000360281; ENSG00000021852.
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   SIGNOR; P07358; -.
DR   BioGRID-ORCS; 732; 9 hits in 1007 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 liver and 74 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: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:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0006956; P:complement activation; TAS:ProtInc.
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; 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           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   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
//
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