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Complement C4-B [Cleaved into: Complement C4 beta chain; Complement C4 alpha chain; C4a anaphylatoxin; Complement C4 gamma chain]

 CO4B_MOUSE              Reviewed;        1738 AA.
P01029; E9QKK7; O70346; Q31201; Q3TYY1; Q3TZC9; Q61372; Q61859;
Q62353; Q6NWV8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
23-MAY-2018, entry version 175.
RecName: Full=Complement C4-B;
Contains:
RecName: Full=Complement C4 beta chain;
Contains:
RecName: Full=Complement C4 alpha chain;
Contains:
RecName: Full=C4a anaphylatoxin;
Contains:
RecName: Full=Complement C4 gamma chain;
Flags: Precursor;
Name=C4b; Synonyms=C4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=FM;
PubMed=2993295;
Nonaka M., Nakayama K., Yeul Y.D., Takahashi M.;
"Complete nucleotide and derived amino acid sequences of the fourth
component of mouse complement (C4). Evolutionary aspects.";
J. Biol. Chem. 260:10936-10943(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=B10.WR;
PubMed=3862104; DOI=10.1073/pnas.82.17.5895;
Sepich D.S., Noonan D.J., Ogata R.T.;
"Complete cDNA sequence of the fourth component of murine
complement.";
Proc. Natl. Acad. Sci. U.S.A. 82:5895-5899(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=B10.WR;
PubMed=2777798;
Ogata R.T., Rosa P.A., Zepf N.E.;
"Sequence of the gene for murine complement component C4.";
J. Biol. Chem. 264:16565-16572(1989).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Inner ear;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=129;
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and CD-1; TISSUE=Germ cell, and Neural stem cell;
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-128.
STRAIN=FM;
PubMed=2997024; DOI=10.1111/j.1600-065X.1985.tb01146.x;
Nonaka M., Nakayama K., Yeul Y.D., Shimizu A., Takahashi M.;
"Molecular cloning and characterization of complementary and genomic
DNA clones for mouse C4 and Slp.";
Immunol. Rev. 87:81-99(1985).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
PubMed=3464002; DOI=10.1073/pnas.83.20.7883;
Nonaka M., Kimura H., Yeul Y.D., Yokoyama S., Nakayama K.,
Takahashi M.;
"Identification of the 5'-flanking regulatory region responsible for
the difference in transcriptional control between mouse complement C4
and Slp genes.";
Proc. Natl. Acad. Sci. U.S.A. 83:7883-7887(1986).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 591-1738.
STRAIN=C57BL/10 X DBA/2;
PubMed=3008092; DOI=10.1093/nar/14.6.2539;
Hemenway C., Kalff M., Stavenhagen J., Walthall D., Robins D.;
"Sequence comparison of alleles of the fourth component of complement
(C4) and sex-limited protein (Slp).";
Nucleic Acids Res. 14:2539-2554(1986).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 651-810 AND 924-1083.
PubMed=6208559; DOI=10.1073/pnas.81.21.6822;
Nonaka M., Takahashi M., Natsuume-Sakai S., Nonaka M., Tanaka S.,
Shimizu A., Honjo T.;
"Isolation of cDNA clones specifying the fourth component of mouse
complement and its isotype, sex-limited protein.";
Proc. Natl. Acad. Sci. U.S.A. 81:6822-6826(1984).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 961-1290.
PubMed=2459207;
Taillon-Miller P.A., Shreffler D.C.;
"Structural basis for the C4d.1/C4d.2 serologic allotypes of murine
complement component C4.";
J. Immunol. 141:2382-2387(1988).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1099-1142.
STRAIN=B10.BR, B10.WR, C3H/He, C57BL/6J, CBA/J, and DBA/2J;
PubMed=2387317; DOI=10.1002/eji.1830200730;
Ogata R.T., Zepf N.E.;
"C4 from C4-high and C4-low mouse strains have identical sequences in
the region corresponding to the isotype-specific segment of human
C4.";
Eur. J. Immunol. 20:1607-1610(1990).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 1105-1449.
PubMed=3856857; DOI=10.1073/pnas.82.6.1746;
Levi-Strauss M., Tosi M., Steinmetz M., Klein J., Meo T.;
"Multiple duplications of complement C4 gene correlate with H-2-
controlled testosterone-independent expression of its sex-limited
isoform, C4-Slp.";
Proc. Natl. Acad. Sci. U.S.A. 82:1746-1750(1985).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 1257-1376.
PubMed=6149581; DOI=10.1098/rstb.1984.0099;
Tosi M., Levi-Strauss M., Duponchel C., Meo T.;
"Sequence heterogeneity of murine complementary DNA clones related to
the C4 and C4-Slp isoforms of the fourth complement component.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 306:389-394(1984).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 1360-1511.
PubMed=6192448; DOI=10.1073/pnas.80.16.5061;
Ogata R.T., Shreffler D.C., Sepich D.S., Lilly S.P.;
"cDNA clone spanning the alpha-gamma subunit junction in the precursor
of the murine fourth complement component (C4).";
Proc. Natl. Acad. Sci. U.S.A. 80:5061-5065(1983).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1324.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=17330941; DOI=10.1021/pr0604559;
Bernhard O.K., Kapp E.A., Simpson R.J.;
"Enhanced analysis of the mouse plasma proteome using cysteine-
containing tryptic glycopeptides.";
J. Proteome Res. 6:987-995(2007).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Non-enzymatic component of C3 and C5 convertases and
thus essential for the propagation of the classical complement
pathway. Covalently binds to immunoglobulins and immune complexes
and enhances the solubilization of immune aggregates and the
clearance of IC through CR1 on erythrocytes. Catalyzes the
transacylation of the thioester carbonyl group to form ester bonds
with carbohydrate antigens (By similarity). {ECO:0000250}.
-!- SUBUNIT: Circulates in blood as a disulfide-linked trimer of an
alpha, beta and gamma chain.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C0L5}.
Cell junction, synapse {ECO:0000250|UniProtKB:P0C0L5}. Cell
projection, axon {ECO:0000250|UniProtKB:P0C0L5}. Cell projection,
dendrite {ECO:0000250|UniProtKB:P0C0L5}.
-!- PTM: Prior to secretion, the single-chain precursor is
enzymatically cleaved to yield non-identical chains alpha, beta
and gamma. During activation, the alpha chain is cleaved by C1
into C4a and C4b, and C4b stays linked to the beta and gamma
chains. Further degradation of C4b by C1 into the inactive
fragments C4c and C4d blocks the generation of C3 convertase.
-!- MISCELLANEOUS: C4 is a major histocompatibility complex class-III
protein.
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EMBL; M11789; AAA39557.1; -; Genomic_DNA.
EMBL; M11729; AAA39506.1; -; mRNA.
EMBL; M17440; AAA39561.1; -; Genomic_DNA.
EMBL; AK157954; BAE34280.1; -; mRNA.
EMBL; AK158256; BAE34429.1; -; mRNA.
EMBL; AF049850; AAC05279.1; -; Genomic_DNA.
EMBL; CT573030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC067394; AAH67394.1; -; mRNA.
EMBL; BC067409; AAH67409.1; -; mRNA.
EMBL; M12968; AAA39558.1; -; Genomic_DNA.
EMBL; M12969; AAA39559.1; -; Genomic_DNA.
EMBL; M14225; AAA39563.1; -; Genomic_DNA.
EMBL; X05314; CAA28936.1; -; mRNA.
EMBL; M12970; AAA39555.1; -; mRNA.
EMBL; M12972; AAA39556.1; -; mRNA.
EMBL; M23186; AAA40487.1; -; Genomic_DNA.
EMBL; X55493; CAA39112.1; -; Genomic_DNA.
EMBL; X55495; CAA39114.1; -; Genomic_DNA.
EMBL; K02798; AAC42021.1; -; mRNA.
EMBL; K02799; AAC42022.1; -; mRNA.
EMBL; K00019; AAA39554.1; -; mRNA.
CCDS; CCDS28657.1; -.
PIR; A24558; A24558.
PIR; A29176; A29176.
RefSeq; NP_033910.2; NM_009780.2.
UniGene; Mm.439678; -.
UniGene; Mm.477109; -.
ProteinModelPortal; P01029; -.
SMR; P01029; -.
BioGrid; 198420; 1.
IntAct; P01029; 2.
MINT; P01029; -.
STRING; 10090.ENSMUSP00000069418; -.
MEROPS; I39.951; -.
GlyConnect; 720; -.
iPTMnet; P01029; -.
PhosphoSitePlus; P01029; -.
SwissPalm; P01029; -.
MaxQB; P01029; -.
PaxDb; P01029; -.
PRIDE; P01029; -.
Ensembl; ENSMUST00000069507; ENSMUSP00000069418; ENSMUSG00000073418.
GeneID; 12268; -.
KEGG; mmu:12268; -.
UCSC; uc008cdk.2; mouse.
CTD; 721; -.
MGI; MGI:88228; C4b.
eggNOG; KOG1366; Eukaryota.
eggNOG; ENOG410XRED; LUCA.
GeneTree; ENSGT00760000118982; -.
HOVERGEN; HBG107123; -.
InParanoid; P01029; -.
KO; K03989; -.
OMA; GQCHISL; -.
OrthoDB; EOG091G00FL; -.
TreeFam; TF313285; -.
Reactome; R-MMU-166663; Initial triggering of complement.
Reactome; R-MMU-174577; Activation of C3 and C5.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
Reactome; R-MMU-977606; Regulation of Complement cascade.
ChiTaRS; C4b; mouse.
PRO; PR:P01029; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000073418; -.
CleanEx; MM_C4B; -.
ExpressionAtlas; P01029; baseline and differential.
Genevisible; P01029; MM.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0044216; C:other organism cell; ISO:MGI.
GO; GO:0045202; C:synapse; ISO:MGI.
GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
GO; GO:0001848; F:complement binding; ISO:MGI.
GO; GO:0001849; F:complement component C1q binding; ISO:MGI.
GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
GO; GO:0006956; P:complement activation; IMP:MGI.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 2.60.40.690; -; 1.
InterPro; IPR009048; A-macroglobulin_rcpt-bd.
InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
InterPro; IPR011626; A2M_comp.
InterPro; IPR002890; A2M_N.
InterPro; IPR011625; A2M_N_2.
InterPro; IPR000020; Anaphylatoxin/fibulin.
InterPro; IPR018081; Anaphylatoxin_comp_syst.
InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
InterPro; IPR037569; Complement_C4A.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR001599; Macroglobln_a2.
InterPro; IPR019742; MacrogloblnA2_CS.
InterPro; IPR019565; MacrogloblnA2_thiol-ester-bond.
InterPro; IPR001134; Netrin_domain.
InterPro; IPR018933; Netrin_module_non-TIMP.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
InterPro; IPR008993; TIMP-like_OB-fold.
PANTHER; PTHR11412:SF134; PTHR11412:SF134; 1.
Pfam; PF00207; A2M; 1.
Pfam; PF07678; A2M_comp; 1.
Pfam; PF01835; A2M_N; 1.
Pfam; PF07703; A2M_N_2; 1.
Pfam; PF07677; A2M_recep; 1.
Pfam; PF01821; ANATO; 1.
Pfam; PF01759; NTR; 1.
Pfam; PF10569; Thiol-ester_cl; 1.
PRINTS; PR00004; ANAPHYLATOXN.
SMART; SM01360; A2M; 1.
SMART; SM01359; A2M_N_2; 1.
SMART; SM01361; A2M_recep; 1.
SMART; SM00104; ANATO; 1.
SMART; SM00643; C345C; 1.
SUPFAM; SSF47686; SSF47686; 1.
SUPFAM; SSF48239; SSF48239; 1.
SUPFAM; SSF49410; SSF49410; 1.
SUPFAM; SSF50242; SSF50242; 1.
PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
PROSITE; PS50189; NTR; 1.
1: Evidence at protein level;
Cell junction; Cell projection; Cleavage on pair of basic residues;
Complement pathway; Complete proteome; Disulfide bond; Glycoprotein;
Immunity; Inflammatory response; Innate immunity; Reference proteome;
Secreted; Signal; Sulfation; Synapse; Thioester bond.
SIGNAL 1 19
CHAIN 20 673 Complement C4 beta chain.
/FTId=PRO_0000005973.
PROPEP 674 677
/FTId=PRO_0000005974.
CHAIN 678 1443 Complement C4 alpha chain.
/FTId=PRO_0000005975.
CHAIN 678 753 C4a anaphylatoxin.
/FTId=PRO_0000005976.
PROPEP 1444 1447
/FTId=PRO_0000005977.
CHAIN 1448 1738 Complement C4 gamma chain.
/FTId=PRO_0000005978.
DOMAIN 700 734 Anaphylatoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00022}.
DOMAIN 1589 1736 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
MOD_RES 1413 1413 Sulfotyrosine. {ECO:0000250}.
MOD_RES 1416 1416 Sulfotyrosine. {ECO:0000250}.
MOD_RES 1417 1417 Sulfotyrosine. {ECO:0000250}.
CARBOHYD 224 224 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 743 743 N-linked (GlcNAc...) asparagine.
CARBOHYD 1324 1324 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17330941}.
CARBOHYD 1387 1387 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 700 726 {ECO:0000250}.
DISULFID 701 733 {ECO:0000250}.
DISULFID 714 734 {ECO:0000250}.
DISULFID 1589 1667 {ECO:0000250}.
DISULFID 1612 1736 {ECO:0000250}.
CROSSLNK 1006 1009 Isoglutamyl cysteine thioester (Cys-Gln).
{ECO:0000250}.
CONFLICT 132 132 F -> Y (in Ref. 1; AAA39557).
{ECO:0000305}.
CONFLICT 177 177 E -> G (in Ref. 4; BAE34429).
{ECO:0000305}.
CONFLICT 283 283 A -> V (in Ref. 4; BAE34429).
{ECO:0000305}.
CONFLICT 327 327 G -> E (in Ref. 1; AAA39557).
{ECO:0000305}.
CONFLICT 440 440 E -> K (in Ref. 7; AAH67394/AAH67409).
{ECO:0000305}.
CONFLICT 570 570 Q -> E (in Ref. 1; AAA39557 and 4;
BAE34280). {ECO:0000305}.
CONFLICT 604 604 M -> T (in Ref. 1; AAA39557, 2; AAA39506,
3; AAA39561, 4; BAE34280/BAE34429 and 7;
AAH67394/AAH67409). {ECO:0000305}.
CONFLICT 639 639 D -> G (in Ref. 4; BAE34429).
{ECO:0000305}.
CONFLICT 758 758 M -> I (in Ref. 4; BAE34280).
{ECO:0000305}.
CONFLICT 838 838 P -> R (in Ref. 1; AAA39557).
{ECO:0000305}.
CONFLICT 916 916 V -> I (in Ref. 4; BAE34280).
{ECO:0000305}.
CONFLICT 1077 1077 F -> S (in Ref. 7; AAH67394/AAH67409).
{ECO:0000305}.
CONFLICT 1119 1119 V -> A (in Ref. 14; AAC42021).
{ECO:0000305}.
CONFLICT 1190 1190 A -> T (in Ref. 14; AAC42021).
{ECO:0000305}.
CONFLICT 1206 1206 R -> Q (in Ref. 4; BAE34280/BAE34429, 7;
AAH67394/AAH67409 and 12; AAA40487).
{ECO:0000305}.
CONFLICT 1290 1290 S -> N (in Ref. 15; AAC42022).
{ECO:0000305}.
CONFLICT 1324 1324 N -> K (in Ref. 2; AAA39506, 3; AAA39561
and 14; AAC42021). {ECO:0000305}.
CONFLICT 1365 1365 K -> E (in Ref. 4; BAE34429).
{ECO:0000305}.
CONFLICT 1401 1401 G -> S (in Ref. 16; AAA39554).
{ECO:0000305}.
CONFLICT 1442 1442 R -> K (in Ref. 1; AAA39557).
{ECO:0000305}.
CONFLICT 1453 1453 V -> A (in Ref. 2; AAA39506, 3; AAA39561,
4; BAE34429 and 16; AAA39554).
{ECO:0000305}.
CONFLICT 1456 1456 Q -> R (in Ref. 4; BAE34429).
{ECO:0000305}.
CONFLICT 1586 1586 E -> Q (in Ref. 10; CAA28936).
{ECO:0000305}.
CONFLICT 1611 1611 A -> T (in Ref. 5; AAC05279).
{ECO:0000305}.
SEQUENCE 1738 AA; 192915 MW; FCC7580209029E88 CRC64;
MRLLWGLAWV FSFCASSLQK PRLLLFSPSV VNLGTPLSVG VQLLDAPPGQ EVKGSVFLRN
PKGGSCSPKK DFKLSSGDDF VLLSLEVPLE DVRSCGLFDL RRAPHIQLVA QSPWLRNTAF
KATETQGVNL LFSSRRGHIF VQTDQPIYNP GQRVRYRVFA LDQKMRPSTD FLTITVENSH
GLRVLKKEIF TSTSIFQDAF TIPDISEPGT WKISARFSDG LESNRSTHFE VKKYVLPNFE
VKITPWKPYI LMVPSNSDEI QLDIQARYIY GKPVQGVAYT RFALMDEQGK RTFLRGLETQ
AKLVEGRTHI SISKDQFQAA LDKINIGVRD LEGLRLYAAT AVIESPGGEM EEAELTSWRF
VSSAFSLDLS RTKRHLVPGA HFLLQALVQE MSGSEASNVP VKVSATLVSG SDSQVLDIQQ
STNGIGQVSI SFPIPPTVTE LRLLVSAGSL YPAIARLTVQ APPSRGTGFL SIEPLDPRSP
SVGDTFILNL QPVGIPAPTF SHYYYMIISR GQIMAMGREP RKTVTSVSVL VDHQLAPSFY
FVAYFYHQGH PVANSLLINI QSRDCEGKLQ LKVDGAKEYR NADMMKLRIQ TDSKALVALG
AVDMALYAVG GRSHKPLDMS KVFEVINSYN VGCGPGGGDD ALQVFQDAGL AFSDGDRLTQ
TREDLSCPKE KKSRQKRNVN FQKAVSEKLG QYSSPDAKRC CQDGMTKLPM KRTCEQRAAR
VPQQACREPF LSCCKFAEDL RRNQTRSQAH LARNNHNMLQ EEDLIDEDDI LVRTSFPENW
LWRVEPVDSS KLLTVWLPDS MTTWEIHGVS LSKSKGLCVA KPTRVRVFRK FHLHLRLPIS
IRRFEQFELR PVLYNYLNDD VAVSVHVTPV EGLCLAGGGM MAQQVTVPAG SARPVAFSVV
PTAAANVPLK VVARGVFDLG DAVSKILQIE KEGAIHREEL VYNLDPLNNL GRTLEIPGSS
DPNIVPDGDF SSLVRVTASE PLETMGSEGA LSPGGVASLL RLPQGCAEQT MIYLAPTLTA
SNYLDRTEQW SKLSPETKDH AVDLIQKGYM RIQQFRKNDG SFGAWLHRDS STWLTAFVLK
ILSLAQEQVG NSPEKLQETA SWLLAQQLGD GSFHDPCPVI HRAMQGGLVG SDETVALTAF
VVIALHHGLD VFQDDDAKQL KNRVEASITK ANSFLGQKAS AGLLGAHAAA ITAYALTLTK
ASEDLRNVAH NSLMAMAEET GEHLYWGLVL GSQDKVVLRP TAPRSPTEPV PQAPALWIET
TAYALLHLLL REGKGKMADK AASWLTHQGS FHGAFRSTQD TVVTLDALSA YWIASHTTEE
KALNVTLSSM GRNGLKTHGL HLNNHQVKGL EEELKFSLGS TISVKVEGNS KGTLKILRTY
NVLDMKNTTC QDLQIEVKVT GAVEYAWDAN EDYEDYYDMP AADDPSVPLQ PVTPLQLFEG
RRSRRRREAP KVVEEQESRV QYTVCIWRNG KLGLSGMAIA DITLLSGFHA LRADLEKLTS
LSDRYVSHFE TDGPHVLLYF DSVPTTRECV GFGASQEVVV GLVQPSSAVL YDYYSPDHKC
SVFYAAPTKS QLLATLCSGD VCQCAEGKCP RLLRSLERRV EDKDGYRMRF ACYYPRVEYG
FTVKVLREDG RAAFRLFESK ITQVLHFRKD TMASIGQTRN FLSRASCRLR LEPNKEYLIM
GMDGETSDNK GDPQYLLDSN TWIEEMPSEQ MCKSTRHRAA CFQLKDFLME FSSRGCQV


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