CO4B_HUMAN
ID CO4B_HUMAN Reviewed; 1744 AA.
AC P0C0L5; A2BHY4; P01028; P78445; Q13160; Q13906; Q14033; Q14835; Q6U2E9;
AC Q6U2G1; Q6U2I5; Q6U2L1; Q6U2L7; Q6U2L9; Q6U2M5; Q6VCV8; Q96SA7; Q9NPK5;
AC Q9UIP5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Complement C4-B;
DE AltName: Full=Basic complement C4;
DE AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 3;
DE Contains:
DE RecName: Full=Complement C4 beta chain;
DE Contains:
DE RecName: Full=Complement C4-B alpha chain;
DE Contains:
DE RecName: Full=C4a anaphylatoxin;
DE Contains:
DE RecName: Full=C4b-B;
DE Contains:
DE RecName: Full=C4d-B;
DE Contains:
DE RecName: Full=Complement C4 gamma chain;
DE Flags: Precursor;
GN Name=C4B; Synonyms=CO4, CPAMD3;
GN and
GN Name=C4B_2;
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 [GENOMIC DNA], AND VARIANT PHE-1317.
RC TISSUE=Blood;
RX PubMed=8575831; DOI=10.1007/bf00587313;
RA Ulgiati D., Townend D.C., Christiansen F.T., Dawkins R.L., Abraham L.J.;
RT "Complete sequence of the complement C4 gene from the HLA-A1, B8, C4AQ0,
RT C4B1, DR3 haplotype.";
RL Immunogenetics 43:250-252(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TYR-347 AND ALA-907.
RA Rowen L., Dankers C., Baskin D., Faust J., Loretz C., Ahearn M.E.,
RA Banta A., Swartzell S., Smith T.M., Spies T., Hood L.;
RT "Sequence determination of 300 kilobases of the human class III MHC
RT locus.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-907 AND ASP-1073.
RA Sayer D., Puschendorf M., Wetherall J.;
RT "Molecular genetics of complement C4: implications for MHC evolution and
RT disease susceptibility gene mapping.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS TYR-347 AND
RP ALA-907.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP PROTEIN SEQUENCE OF 680-756.
RX PubMed=6167582; DOI=10.1016/s0021-9258(19)68898-8;
RA Moon K.E., Gorski J.P., Hugli T.E.;
RT "Complete primary structure of human C4a anaphylatoxin.";
RL J. Biol. Chem. 256:8685-8692(1981).
RN [6]
RP PROTEIN SEQUENCE OF 757-771 AND 980-990.
RX PubMed=1699796; DOI=10.1016/0014-5793(90)80389-z;
RA Hessing M., van 't Veer C., Hackeng T.M., Bouma B.N., Iwanaga S.;
RT "Importance of the alpha 3-fragment of complement C4 for the binding with
RT C4b-binding protein.";
RL FEBS Lett. 271:131-136(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 956-1336, AND VARIANT ASP-1073.
RC TISSUE=Liver;
RX PubMed=6546707; DOI=10.1016/0092-8674(84)90040-0;
RA Belt K.T., Carroll M.C., Porter R.R.;
RT "The structural basis of the multiple forms of human complement component
RT C4.";
RL Cell 36:907-914(1984).
RN [8]
RP PROTEIN SEQUENCE OF 957-1044.
RX PubMed=6978711; DOI=10.1042/bj1990359;
RA Campbell R.D., Gagnon J., Porter R.R.;
RT "Amino acid sequence around the thiol and reactive acyl groups of human
RT complement component C4.";
RL Biochem. J. 199:359-370(1981).
RN [9]
RP PROTEIN SEQUENCE OF 957-1336.
RX PubMed=3696167; DOI=10.1016/0161-5890(87)90165-9;
RA Chakravarti D.N., Campbell R.D., Porter R.R.;
RT "The chemical structure of the C4d fragment of the human complement
RT component C4.";
RL Mol. Immunol. 24:1187-1197(1987).
RN [10]
RP PROTEIN SEQUENCE OF 990-1037.
RX PubMed=6950384; DOI=10.1073/pnas.78.12.7388;
RA Harrison R.A., Thomas M.L., Tack B.F.;
RT "Sequence determination of the thiolester site of the fourth component of
RT human complement.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:7388-7392(1981).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1055-1225 (ALLOTYPE C4B12).
RX PubMed=9759862;
RA Martinez-Quiles N., Paz-Artal E., Moreno-Pelayo M.A., Longas J.,
RA Ferre-Lopez S., Rosal M., Arnaiz-Villena A.;
RT "C4d DNA sequences of two infrequent human allotypes (C4A13 and C4B12) and
RT the presence of signal sequences enhancing recombination.";
RL J. Immunol. 161:3438-3443(1998).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1055-1225, AND VARIANTS ASN-1176;
RP VAL-1207 AND LEU-1210.
RX PubMed=14989716; DOI=10.1111/j.0001-2815.2004.00147.x;
RA Lopez-Goyanes A., Moreno M.A., Ferre S., Paz-Artal E.;
RT "C4d DNA sequence of complement C4B93 and recombination mechanisms for its
RT generation.";
RL Tissue Antigens 63:260-262(2004).
RN [13]
RP PROTEIN SEQUENCE OF 1199-1304.
RX PubMed=6832377; DOI=10.1016/0014-5793(83)80188-4;
RA Chakravarti D.N., Campbell R.D., Gagnon J.;
RT "Amino acid sequence of a polymorphic segment from fragment C4d of human
RT complement component C4.";
RL FEBS Lett. 154:387-390(1983).
RN [14]
RP PROTEIN SEQUENCE OF 1405-1431, AND SULFATION AT TYR-1417; TYR-1420 AND
RP TYR-1422.
RX PubMed=3944109; DOI=10.1016/s0021-9258(17)36009-x;
RA Hortin G., Sims H., Strauss A.W.;
RT "Identification of the site of sulfation of the fourth component of human
RT complement.";
RL J. Biol. Chem. 261:1786-1793(1986).
RN [15]
RP INVOLVEMENT IN C4BD AND SLE.
RX PubMed=3265961;
RA Wilson W.A., Perez M.C.;
RT "Complete C4B deficiency in black Americans with systemic lupus
RT erythematosus.";
RL J. Rheumatol. 15:1855-1858(1988).
RN [16]
RP INTERACTION WITH CR1.
RX PubMed=2972794; DOI=10.1084/jem.168.5.1699;
RA Klickstein L.B., Bartow T.J., Miletic V., Rabson L.D., Smith J.A.,
RA Fearon D.T.;
RT "Identification of distinct C3b and C4b recognition sites in the human
RT C3b/C4b receptor (CR1, CD35) by deletion mutagenesis.";
RL J. Exp. Med. 168:1699-1717(1988).
RN [17]
RP FUNCTION, INVOLVEMENT OF HIS-1125 IN IMMUNOGLOBULIN-BINDING AND HEMOLYSIS,
RP AND MUTAGENESIS OF LEU-1120; SER-1121; ILE-1124 AND HIS-1125.
RX PubMed=2395880; DOI=10.1073/pnas.87.17.6868;
RA Carroll M.C., Fathallah D.M., Bergamaschini L., Alicot E.M., Isenman D.E.;
RT "Substitution of a single amino acid (aspartic acid for histidine) converts
RT the functional activity of human complement C4B to C4A.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6868-6872(1990).
RN [18]
RP INTERACTION WITH CR1.
RX PubMed=8175757; DOI=10.1016/s0021-9258(17)36829-1;
RA Krych M., Clemenza L., Howdeshell D., Hauhart R., Hourcade D.,
RA Atkinson J.P.;
RT "Analysis of the functional domains of complement receptor type 1 (C3b/C4b
RT receptor; CD35) by substitution mutagenesis.";
RL J. Biol. Chem. 269:13273-13278(1994).
RN [19]
RP FUNCTION.
RX PubMed=8538770; DOI=10.1038/379177a0;
RA Dodds A.W., Ren X.D., Willis A.C., Law S.K.;
RT "The reaction mechanism of the internal thioester in the human complement
RT component C4.";
RL Nature 379:177-179(1996).
RN [20]
RP INVOLVEMENT IN SLE.
RX PubMed=10092831;
RA Lokki M.L., Circolo A., Ahokas P., Rupert K.L., Yu C.Y., Colten H.R.;
RT "Deficiency of human complement protein C4 due to identical frameshift
RT mutations in the C4A and C4B genes.";
RL J. Immunol. 162:3687-3693(1999).
RN [21]
RP REVIEW, DESCRIPTION OF ALLOTYPES, AND TISSUE SPECIFICITY.
RX PubMed=11367523; DOI=10.1016/s1567-5769(01)00019-4;
RA Blanchong C.A., Chung E.K., Rupert K.L., Yang Y., Yang Z., Zhou B.,
RA Moulds J.M., Yu C.Y.;
RT "Genetic, structural and functional diversities of human complement
RT components C4A and C4B and their mouse homologues, Slp and C4.";
RL Int. Immunopharmacol. 1:365-392(2001).
RN [22]
RP GLYCOSYLATION AT ASN-226.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [23]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1391.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [24]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1328.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [25]
RP STRUCTURAL BASIS OF POLYMORPHISM.
RX PubMed=2431902; DOI=10.1002/j.1460-2075.1986.tb04582.x;
RA Yu C.Y., Belt K.T., Giles C.M., Campbell R.D., Porter R.R.;
RT "Structural basis of the polymorphism of human complement components C4A
RT and C4B: gene size, reactivity and antigenicity.";
RL EMBO J. 5:2873-2881(1986).
RN [26]
RP INVOLVEMENT IN SLE.
RX PubMed=17503323; DOI=10.1086/518257;
RA Yang Y., Chung E.K., Wu Y.L., Savelli S.L., Nagaraja H.N., Zhou B.,
RA Hebert M., Jones K.N., Shu Y., Kitzmiller K., Blanchong C.A., McBride K.L.,
RA Higgins G.C., Rennebohm R.M., Rice R.R., Hackshaw K.V., Roubey R.A.,
RA Grossman J.M., Tsao B.P., Birmingham D.J., Rovin B.H., Hebert L.A.,
RA Yu C.Y.;
RT "Gene copy-number variation and associated polymorphisms of complement
RT component C4 in human systemic lupus erythematosus (SLE): low copy number
RT is a risk factor for and high copy number is a protective factor against
RT SLE susceptibility in European Americans.";
RL Am. J. Hum. Genet. 80:1037-1054(2007).
RN [27]
RP POLYMORPHISM, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=26814963; DOI=10.1038/nature16549;
RG Schizophrenia Working Group of the Psychiatric Genomics Consortium;
RA Sekar A., Bialas A.R., de Rivera H., Davis A., Hammond T.R., Kamitaki N.,
RA Tooley K., Presumey J., Baum M., Van Doren V., Genovese G., Rose S.A.,
RA Handsaker R.E., Daly M.J., Carroll M.C., Stevens B., McCarroll S.A.;
RT "Schizophrenia risk from complex variation of complement component 4.";
RL Nature 530:177-183(2016).
CC -!- FUNCTION: Non-enzymatic component of the C3 and C5 convertases and thus
CC essential for the propagation of the classical complement pathway.
CC Covalently binds to immunoglobulins and immune complexes and enhances
CC the solubilization of immune aggregates and the clearance of IC through
CC CR1 on erythrocytes. C4A isotype is responsible for effective binding
CC to form amide bonds with immune aggregates or protein antigens, while
CC C4B isotype catalyzes the transacylation of the thioester carbonyl
CC group to form ester bonds with carbohydrate antigens.
CC -!- FUNCTION: Derived from proteolytic degradation of complement C4, C4a
CC anaphylatoxin is a mediator of local inflammatory process. It induces
CC the contraction of smooth muscle, increases vascular permeability and
CC causes histamine release from mast cells and basophilic leukocytes.
CC -!- SUBUNIT: Circulates in blood as a disulfide-linked trimer of alpha,
CC beta and gamma chains. C4b interacts with CR1 (via Sushi 1 and Sushi 2
CC domains). {ECO:0000269|PubMed:2972794, ECO:0000269|PubMed:8175757}.
CC -!- INTERACTION:
CC PRO_0000042699; O00187: MASP2; NbExp=4; IntAct=EBI-26369106, EBI-7965040;
CC -!- SUBCELLULAR LOCATION: Secreted. Synapse {ECO:0000269|PubMed:26814963}.
CC Cell projection, axon {ECO:0000269|PubMed:26814963}. Cell projection,
CC dendrite {ECO:0000269|PubMed:26814963}.
CC -!- TISSUE SPECIFICITY: Complement component C4 is expressed at highest
CC levels in the liver, at moderate levels in the adrenal cortex, adrenal
CC medulla, thyroid gland, and the kidney, and at lowest levels in the
CC heart, ovary, small intestine, thymus, pancreas and spleen. The extra-
CC hepatic sites of expression may be important for the local protection
CC and inflammatory response. {ECO:0000269|PubMed:11367523}.
CC -!- PTM: Prior to secretion, the single-chain precursor is enzymatically
CC cleaved to yield non-identical chains alpha, beta and gamma. During
CC activation, the alpha chain is cleaved by C1 into C4a and C4b, and C4b
CC stays linked to the beta and gamma chains. Further degradation of C4b
CC by C1 into the inactive fragments C4c and C4d blocks the generation of
CC C3 convertase. The proteolytic cleavages often are incomplete so that
CC many structural forms can be found in plasma.
CC -!- POLYMORPHISM: The complement component C4 is the most polymorphic
CC protein of the complement system. It is the product of 2 closely linked
CC and highly homologous genes, C4A and C4B. Once polymorphic variation is
CC discounted, the 2 isotypes differ by only 4 amino acids at positions
CC 1120-1125: PCPVLD for C4A and LSPVIH for C4B. The 2 isotypes bear
CC several antigenic determinants defining Chido/Rodgers blood group
CC system [MIM:614374]. Rodgers determinants are generally associated with
CC C4A allotypes, and Chido with C4B. Variations at these loci involve not
CC only nucleotide polymorphisms, but also gene number and gene size. The
CC second copy of C4B gene present in some individuals has been called
CC C4B_2 by the HUGO Gene Nomenclature Committee (HGNC). Some individuals
CC may lack either C4A, or C4B gene. Partial deficiency of C4A or C4B is
CC the most commonly inherited immune deficiency known in humans with a
CC combined frequency over 31% in the normal Caucasian population
CC (PubMed:11367523). Common copy-number variants of C4A and C4B affecting
CC expression of complement component C4 in the brain have been associated
CC with schizophrenia risk (PubMed:26814963).
CC {ECO:0000269|PubMed:11367523, ECO:0000269|PubMed:26814963}.
CC -!- DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic,
CC relapsing, inflammatory, and often febrile multisystemic disorder of
CC connective tissue, characterized principally by involvement of the
CC skin, joints, kidneys and serosal membranes. It is of unknown etiology,
CC but is thought to represent a failure of the regulatory mechanisms of
CC the autoimmune system. The disease is marked by a wide range of system
CC dysfunctions, an elevated erythrocyte sedimentation rate, and the
CC formation of LE cells in the blood or bone marrow.
CC {ECO:0000269|PubMed:10092831, ECO:0000269|PubMed:17503323}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry. Interindividual copy-number variation
CC (CNV) of complement component C4 and associated polymorphisms result in
CC different susceptibilities to SLE. The risk of SLE susceptibility has
CC been shown to be significantly increased among subjects with only two
CC copies of total C4. A high copy number is a protective factor against
CC SLE.
CC -!- DISEASE: Complement component 4B deficiency (C4BD) [MIM:614379]: A rare
CC defect of the complement classical pathway associated with the
CC development of autoimmune disorders, mainly systemic lupus with or
CC without associated glomerulonephritis. {ECO:0000269|PubMed:3265961}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA99717.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=chrg";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U24578; AAA99717.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF019413; AAB67980.1; -; Genomic_DNA.
DR EMBL; AY379860; AAR89087.1; -; Genomic_DNA.
DR EMBL; AY379862; AAR89089.1; -; Genomic_DNA.
DR EMBL; AY379864; AAR89091.1; -; Genomic_DNA.
DR EMBL; AY379866; AAR89093.1; -; Genomic_DNA.
DR EMBL; AY379868; AAR89095.1; -; Genomic_DNA.
DR EMBL; AY379870; AAR89097.1; -; Genomic_DNA.
DR EMBL; AY379872; AAR89099.1; -; Genomic_DNA.
DR EMBL; AY379874; AAR89101.1; -; Genomic_DNA.
DR EMBL; AY379876; AAR89103.1; -; Genomic_DNA.
DR EMBL; AY379878; AAR89105.1; -; Genomic_DNA.
DR EMBL; AY379880; AAR89107.1; -; Genomic_DNA.
DR EMBL; AY379882; AAR89109.1; -; Genomic_DNA.
DR EMBL; AY379884; AAR89111.1; -; Genomic_DNA.
DR EMBL; AY379886; AAR89113.1; -; Genomic_DNA.
DR EMBL; AY379888; AAR89115.1; -; Genomic_DNA.
DR EMBL; AY379890; AAR89117.1; -; Genomic_DNA.
DR EMBL; AY379892; AAR89119.1; -; Genomic_DNA.
DR EMBL; AY379894; AAR89121.1; -; Genomic_DNA.
DR EMBL; AY379896; AAR89123.1; -; Genomic_DNA.
DR EMBL; AY379898; AAR89125.1; -; Genomic_DNA.
DR EMBL; AY379900; AAR89127.1; -; Genomic_DNA.
DR EMBL; AY379902; AAR89130.1; -; Genomic_DNA.
DR EMBL; AY379904; AAR89132.1; -; Genomic_DNA.
DR EMBL; AY379906; AAR89134.1; -; Genomic_DNA.
DR EMBL; AY379908; AAR89136.1; -; Genomic_DNA.
DR EMBL; AY379910; AAR89138.1; -; Genomic_DNA.
DR EMBL; AY379912; AAR89139.1; -; Genomic_DNA.
DR EMBL; AY379914; AAR89142.1; -; Genomic_DNA.
DR EMBL; AY379916; AAR89144.1; -; Genomic_DNA.
DR EMBL; AY379918; AAR89145.1; -; Genomic_DNA.
DR EMBL; AY379920; AAR89148.1; -; Genomic_DNA.
DR EMBL; AY379922; AAR89150.1; -; Genomic_DNA.
DR EMBL; AY379924; AAR89151.1; -; Genomic_DNA.
DR EMBL; AY379959; AAR89163.1; -; Genomic_DNA.
DR EMBL; AY379936; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379937; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379938; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379939; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379940; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379941; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379942; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379943; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379944; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379945; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379946; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379947; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379948; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379949; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379950; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379951; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379952; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379953; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379954; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379955; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379956; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379957; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AY379958; AAR89163.1; JOINED; Genomic_DNA.
DR EMBL; AL049547; CAB89302.1; -; Genomic_DNA.
DR EMBL; BX679671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; K02404; AAA59651.1; -; mRNA.
DR EMBL; U77887; AAK49811.1; -; Genomic_DNA.
DR EMBL; AY343497; AAQ99144.1; -; Genomic_DNA.
DR CCDS; CCDS47405.1; -.
DR PIR; B20807; B20807.
DR RefSeq; NP_001002029.3; NM_001002029.3.
DR RefSeq; NP_001229752.1; NM_001242823.2.
DR PDB; 4XAM; X-ray; 4.20 A; A/B=20-675.
DR PDB; 6YSQ; X-ray; 3.30 A; A/B=1-1744.
DR PDBsum; 4XAM; -.
DR PDBsum; 6YSQ; -.
DR AlphaFoldDB; P0C0L5; -.
DR SMR; P0C0L5; -.
DR BioGRID; 107182; 7.
DR BioGRID; 945184; 1.
DR ComplexPortal; CPX-6156; Classical and lectin pathway C3 convertase complex C4b2a-B.
DR DIP; DIP-47260N; -.
DR IntAct; P0C0L5; 14.
DR MINT; P0C0L5; -.
DR STRING; 9606.ENSP00000415941; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB00028; Human immunoglobulin G.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR MEROPS; I39.951; -.
DR GlyConnect; 1146; 32 N-Linked glycans (4 sites), 1 O-Linked glycan (1 site).
DR GlyGen; P0C0L5; 5 sites, 34 N-linked glycans (4 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P0C0L5; -.
DR PhosphoSitePlus; P0C0L5; -.
DR BioMuta; C4B; -.
DR DMDM; 476007828; -.
DR SWISS-2DPAGE; P0C0L5; -.
DR CPTAC; non-CPTAC-1107; -.
DR EPD; P0C0L5; -.
DR jPOST; P0C0L5; -.
DR MassIVE; P0C0L5; -.
DR PaxDb; P0C0L5; -.
DR PeptideAtlas; P0C0L5; -.
DR PRIDE; P0C0L5; -.
DR ProteomicsDB; 67395; -.
DR TopDownProteomics; P0C0L5; -.
DR Antibodypedia; 35326; 372 antibodies from 21 providers.
DR DNASU; 721; -.
DR Ensembl; ENST00000375177.9; ENSP00000364321.5; ENSG00000228454.7.
DR Ensembl; ENST00000411583.6; ENSP00000407942.2; ENSG00000228267.8.
DR Ensembl; ENST00000435363.7; ENSP00000415941.2; ENSG00000224389.9.
DR Ensembl; ENST00000435500.6; ENSP00000412786.2; ENSG00000233312.8.
DR Ensembl; ENST00000449788.6; ENSP00000414200.2; ENSG00000236625.8.
DR GeneID; 100293534; -.
DR GeneID; 721; -.
DR KEGG; hsa:100293534; -.
DR KEGG; hsa:721; -.
DR MANE-Select; ENST00000435363.7; ENSP00000415941.2; NM_001002029.4; NP_001002029.3.
DR UCSC; uc011dpd.3; human.
DR CTD; 100293534; -.
DR CTD; 721; -.
DR DisGeNET; 100293534; -.
DR DisGeNET; 721; -.
DR GeneCards; C4B; -.
DR GeneCards; C4B_2; -.
DR HGNC; HGNC:1324; C4B.
DR HGNC; HGNC:42398; C4B_2.
DR HPA; ENSG00000224389; Group enriched (adrenal gland, liver).
DR MalaCards; C4B; -.
DR MIM; 120820; gene.
DR MIM; 152700; phenotype.
DR MIM; 614374; phenotype.
DR MIM; 614379; phenotype.
DR neXtProt; NX_P0C0L5; -.
DR OpenTargets; ENSG00000224389; -.
DR Orphanet; 169147; Immunodeficiency due to a classical component pathway complement deficiency.
DR Orphanet; 536; Systemic lupus erythematosus.
DR PharmGKB; PA25904; -.
DR VEuPathDB; HostDB:ENSG00000224389; -.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000155739; -.
DR InParanoid; P0C0L5; -.
DR OMA; CVRQKSN; -.
DR OrthoDB; 28894at2759; -.
DR PhylomeDB; P0C0L5; -.
DR TreeFam; TF313285; -.
DR PathwayCommons; P0C0L5; -.
DR Reactome; R-HSA-166663; Initial triggering of complement.
DR Reactome; R-HSA-174577; Activation of C3 and C5.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SABIO-RK; P0C0L5; -.
DR SignaLink; P0C0L5; -.
DR SIGNOR; P0C0L5; -.
DR BioGRID-ORCS; 100293534; 6 hits in 65 CRISPR screens.
DR BioGRID-ORCS; 721; 8 hits in 671 CRISPR screens.
DR ChiTaRS; C4B; human.
DR GeneWiki; Complement_component_4B; -.
DR Pharos; P0C0L5; Tbio.
DR PRO; PR:P0C0L5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P0C0L5; protein.
DR Bgee; ENSG00000224389; Expressed in right lobe of liver and 91 other tissues.
DR ExpressionAtlas; P0C0L5; baseline and differential.
DR Genevisible; P0C0L5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005601; C:classical-complement-pathway C3/C5 convertase complex; IPI:ComplexPortal.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
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; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0106139; C:symbiont cell surface; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IDA:BHF-UCL.
DR GO; GO:0001848; F:complement binding; IDA:BHF-UCL.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0006956; P:complement activation; IDA:ComplexPortal.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0032490; P:detection of molecule of bacterial origin; IDA:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0008228; P:opsonization; TAS:BHF-UCL.
DR GO; GO:2000427; P:positive regulation of apoptotic cell clearance; IGI:BHF-UCL.
DR GO; GO:0050778; P:positive regulation of immune response; IC:ComplexPortal.
DR GO; GO:1903028; P:positive regulation of opsonization; IC:ComplexPortal.
DR CDD; cd00017; ANATO; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
DR InterPro; IPR037569; Complement_C4A.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11412:SF86; PTHR11412:SF86; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF07678; TED_complement; 1.
DR PRINTS; PR00004; ANAPHYLATOXN.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SMART; SM00104; ANATO; 1.
DR SMART; SM00643; C345C; 1.
DR SUPFAM; SSF47686; SSF47686; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF50242; SSF50242; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS50189; NTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood group antigen; Cell projection;
KW Cleavage on pair of basic residues; Complement pathway;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW Inflammatory response; Innate immunity; Phosphoprotein; Reference proteome;
KW Secreted; Signal; Sulfation; Synapse; Systemic lupus erythematosus;
KW Thioester bond.
FT SIGNAL 1..19
FT CHAIN 20..675
FT /note="Complement C4 beta chain"
FT /id="PRO_0000042699"
FT PROPEP 676..679
FT /evidence="ECO:0000269|PubMed:6167582"
FT /id="PRO_0000042700"
FT CHAIN 680..1446
FT /note="Complement C4-B alpha chain"
FT /id="PRO_0000042701"
FT CHAIN 680..756
FT /note="C4a anaphylatoxin"
FT /id="PRO_0000042702"
FT CHAIN 757..1446
FT /note="C4b-B"
FT /id="PRO_0000042703"
FT CHAIN 957..1336
FT /note="C4d-B"
FT /id="PRO_0000042704"
FT PROPEP 1447..1453
FT /id="PRO_0000042705"
FT CHAIN 1454..1744
FT /note="Complement C4 gamma chain"
FT /id="PRO_0000042706"
FT DOMAIN 702..736
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 1595..1742
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT MOD_RES 918
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C0L4"
FT MOD_RES 1417
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:3944109"
FT MOD_RES 1420
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:3944109"
FT MOD_RES 1422
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:3944109"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519"
FT CARBOHYD 862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002"
FT CARBOHYD 1391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718"
FT DISULFID 702..728
FT /evidence="ECO:0000250"
FT DISULFID 703..735
FT /evidence="ECO:0000250"
FT DISULFID 716..736
FT /evidence="ECO:0000250"
FT DISULFID 1595..1673
FT /evidence="ECO:0000250"
FT DISULFID 1618..1742
FT /evidence="ECO:0000250"
FT CROSSLNK 1010..1013
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT VARIANT 347
FT /note="S -> Y (in allotype C4B-long; dbSNP:rs139889867)"
FT /evidence="ECO:0000269|PubMed:14574404, ECO:0000269|Ref.2"
FT /id="VAR_023729"
FT VARIANT 478
FT /note="P -> L (in allotype C4B1-hi)"
FT /id="VAR_069160"
FT VARIANT 907
FT /note="T -> A (in allotype C4B-long and allotype C4B2;
FT dbSNP:rs796750528)"
FT /evidence="ECO:0000269|PubMed:14574404, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.3"
FT /id="VAR_023730"
FT VARIANT 1073
FT /note="G -> D (in allotype C4B2 and allotype C4B5-Rg1;
FT dbSNP:rs2258218)"
FT /evidence="ECO:0000269|PubMed:6546707, ECO:0000269|Ref.3"
FT /id="VAR_023731"
FT VARIANT 1176
FT /note="S -> N (in allotype C4B1a; dbSNP:rs2746414)"
FT /evidence="ECO:0000269|PubMed:14989716"
FT /id="VAR_023732"
FT VARIANT 1207
FT /note="A -> V (in allotype C4B5-Rg1; dbSNP:rs2229403)"
FT /evidence="ECO:0000269|PubMed:14989716"
FT /id="VAR_023734"
FT VARIANT 1210
FT /note="R -> L (in allotype C4B5-Rg1; dbSNP:rs2229409)"
FT /evidence="ECO:0000269|PubMed:14989716"
FT /id="VAR_023735"
FT VARIANT 1317
FT /note="I -> F (in allotype C4B1-SC01; dbSNP:rs2023616)"
FT /evidence="ECO:0000269|PubMed:8575831"
FT /id="VAR_069161"
FT MUTAGEN 1120
FT /note="L->P: No effect on hemolytic activity, nor on C1-
FT dependent binding to IgG."
FT /evidence="ECO:0000269|PubMed:2395880"
FT MUTAGEN 1121
FT /note="S->C: 30-40% decrease in hemolytic activity and C1-
FT dependent binding to IgG."
FT /evidence="ECO:0000269|PubMed:2395880"
FT MUTAGEN 1124
FT /note="I->A: 50-60% decrease in hemolytic activity and C1-
FT dependent binding to IgG."
FT /evidence="ECO:0000269|PubMed:2395880"
FT MUTAGEN 1125
FT /note="H->A: 20% decrease in hemolytic activity, 2-fold
FT increase in C1-dependent binding to IgG."
FT /evidence="ECO:0000269|PubMed:2395880"
FT MUTAGEN 1125
FT /note="H->D: 2.5-3 fold-decrease in hemolytic activity, 3-
FT fold increase in C1-dependent binding to IgG."
FT /evidence="ECO:0000269|PubMed:2395880"
FT CONFLICT 714
FT /note="R -> S (in Ref. 3; AAR89101)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="R -> Q (in Ref. 3; AAR89127)"
FT /evidence="ECO:0000305"
FT CONFLICT 980..981
FT /note="VT -> LQ (in Ref. 1; AAA99717)"
FT /evidence="ECO:0000305"
FT CONFLICT 1013
FT /note="Q -> E (in Ref. 8; AA sequence, 9; AA sequence and
FT 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1109..1110
FT /note="SQ -> IA (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1271
FT /note="H -> V (in Ref. 9; AA sequence and 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1300
FT /note="R -> V (in Ref. 9; AA sequence and 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1654
FT /note="T -> RA (in Ref. 1; AAA99717)"
FT /evidence="ECO:0000305"
FT CONFLICT 1698
FT /note="H -> Q (in Ref. 1; AAA99717)"
FT /evidence="ECO:0000305"
FT STRAND 22..32
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:6YSQ"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:6YSQ"
FT TURN 115..120
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 194..203
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 210..221
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 240..250
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 262..270
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 278..287
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:6YSQ"
FT HELIX 316..325
FT /evidence="ECO:0007829|PDB:6YSQ"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 337..346
FT /evidence="ECO:0007829|PDB:6YSQ"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 417..424
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 430..435
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 443..450
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 488..498
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 504..511
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 514..522
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 525..532
FT /evidence="ECO:0007829|PDB:6YSQ"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 539..549
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 552..561
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 586..605
FT /evidence="ECO:0007829|PDB:6YSQ"
FT HELIX 608..611
FT /evidence="ECO:0007829|PDB:6YSQ"
FT HELIX 622..628
FT /evidence="ECO:0007829|PDB:6YSQ"
FT HELIX 629..631
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:6YSQ"
FT HELIX 644..650
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 652..655
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1465..1474
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1484..1489
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1494..1496
FT /evidence="ECO:0007829|PDB:6YSQ"
FT HELIX 1498..1501
FT /evidence="ECO:0007829|PDB:6YSQ"
FT HELIX 1502..1504
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1506..1509
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1512..1517
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1519..1527
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1534..1536
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1539..1544
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1554..1560
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1564..1567
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1573..1575
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1581..1584
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1587..1590
FT /evidence="ECO:0007829|PDB:6YSQ"
FT HELIX 1613..1618
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1625..1634
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1640..1652
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1664..1670
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1681..1687
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1695..1699
FT /evidence="ECO:0007829|PDB:6YSQ"
FT STRAND 1708..1711
FT /evidence="ECO:0007829|PDB:6YSQ"
FT HELIX 1715..1718
FT /evidence="ECO:0007829|PDB:6YSQ"
FT HELIX 1724..1739
FT /evidence="ECO:0007829|PDB:6YSQ"
SQ SEQUENCE 1744 AA; 192751 MW; E724B85F7FA673C5 CRC64;
MRLLWGLIWA SSFFTLSLQK PRLLLFSPSV VHLGVPLSVG VQLQDVPRGQ VVKGSVFLRN
PSRNNVPCSP KVDFTLSSER DFALLSLQVP LKDAKSCGLH QLLRGPEVQL VAHSPWLKDS
LSRTTNIQGI NLLFSSRRGH LFLQTDQPIY NPGQRVRYRV FALDQKMRPS TDTITVMVEN
SHGLRVRKKE VYMPSSIFQD DFVIPDISEP GTWKISARFS DGLESNSSTQ FEVKKYVLPN
FEVKITPGKP YILTVPGHLD EMQLDIQARY IYGKPVQGVA YVRFGLLDED GKKTFFRGLE
SQTKLVNGQS HISLSKAEFQ DALEKLNMGI TDLQGLRLYV AAAIIESPGG EMEEAELTSW
YFVSSPFSLD LSKTKRHLVP GAPFLLQALV REMSGSPASG IPVKVSATVS SPGSVPEVQD
IQQNTDGSGQ VSIPIIIPQT ISELQLSVSA GSPHPAIARL TVAAPPSGGP GFLSIERPDS
RPPRVGDTLN LNLRAVGSGA TFSHYYYMIL SRGQIVFMNR EPKRTLTSVS VFVDHHLAPS
FYFVAFYYHG DHPVANSLRV DVQAGACEGK LELSVDGAKQ YRNGESVKLH LETDSLALVA
LGALDTALYA AGSKSHKPLN MGKVFEAMNS YDLGCGPGGG DSALQVFQAA GLAFSDGDQW
TLSRKRLSCP KEKTTRKKRN VNFQKAINEK LGQYASPTAK RCCQDGVTRL PMMRSCEQRA
ARVQQPDCRE PFLSCCQFAE SLRKKSRDKG QAGLQRALEI LQEEDLIDED DIPVRSFFPE
NWLWRVETVD RFQILTLWLP DSLTTWEIHG LSLSKTKGLC VATPVQLRVF REFHLHLRLP
MSVRRFEQLE LRPVLYNYLD KNLTVSVHVS PVEGLCLAGG GGLAQQVLVP AGSARPVAFS
VVPTAATAVS LKVVARGSFE FPVGDAVSKV LQIEKEGAIH REELVYELNP LDHRGRTLEI
PGNSDPNMIP DGDFNSYVRV TASDPLDTLG SEGALSPGGV ASLLRLPRGC GEQTMIYLAP
TLAASRYLDK TEQWSTLPPE TKDHAVDLIQ KGYMRIQQFR KADGSYAAWL SRGSSTWLTA
FVLKVLSLAQ EQVGGSPEKL QETSNWLLSQ QQADGSFQDL SPVIHRSMQG GLVGNDETVA
LTAFVTIALH HGLAVFQDEG AEPLKQRVEA SISKASSFLG EKASAGLLGA HAAAITAYAL
TLTKAPADLR GVAHNNLMAM AQETGDNLYW GSVTGSQSNA VSPTPAPRNP SDPMPQAPAL
WIETTAYALL HLLLHEGKAE MADQAAAWLT RQGSFQGGFR STQDTVIALD ALSAYWIASH
TTEERGLNVT LSSTGRNGFK SHALQLNNRQ IRGLEEELQF SLGSKINVKV GGNSKGTLKV
LRTYNVLDMK NTTCQDLQIE VTVKGHVEYT MEANEDYEDY EYDELPAKDD PDAPLQPVTP
LQLFEGRRNR RRREAPKVVE EQESRVHYTV CIWRNGKVGL SGMAIADVTL LSGFHALRAD
LEKLTSLSDR YVSHFETEGP HVLLYFDSVP TSRECVGFEA VQEVPVGLVQ PASATLYDYY
NPERRCSVFY GAPSKSRLLA TLCSAEVCQC AEGKCPRQRR ALERGLQDED GYRMKFACYY
PRVEYGFQVK VLREDSRAAF RLFETKITQV LHFTKDVKAA ANQMRNFLVR ASCRLRLEPG
KEYLIMGLDG ATYDLEGHPQ YLLDSNSWIE EMPSERLCRS TRQRAACAQL NDFLQEYGTQ
GCQV
