CO4B_MOUSE
ID CO4B_MOUSE Reviewed; 1738 AA.
AC P01029; E9QKK7; O70346; Q31201; Q3TYY1; Q3TZC9; Q61372; Q61859; Q62353;
AC Q6NWV8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Complement C4-B;
DE Contains:
DE RecName: Full=Complement C4 beta chain;
DE Contains:
DE RecName: Full=Complement C4 alpha chain;
DE Contains:
DE RecName: Full=C4a anaphylatoxin;
DE Contains:
DE RecName: Full=Complement C4 gamma chain;
DE Flags: Precursor;
GN Name=C4b; Synonyms=C4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FM;
RX PubMed=2993295; DOI=10.1016/s0021-9258(17)39125-1;
RA Nonaka M., Nakayama K., Yeul Y.D., Takahashi M.;
RT "Complete nucleotide and derived amino acid sequences of the fourth
RT component of mouse complement (C4). Evolutionary aspects.";
RL J. Biol. Chem. 260:10936-10943(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B10.WR;
RX PubMed=3862104; DOI=10.1073/pnas.82.17.5895;
RA Sepich D.S., Noonan D.J., Ogata R.T.;
RT "Complete cDNA sequence of the fourth component of murine complement.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5895-5899(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B10.WR;
RX PubMed=2777798; DOI=10.1016/s0021-9258(19)84744-0;
RA Ogata R.T., Rosa P.A., Zepf N.E.;
RT "Sequence of the gene for murine complement component C4.";
RL J. Biol. Chem. 264:16565-16572(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Inner ear;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and CD-1; TISSUE=Germ cell, and Neural stem cell;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-128.
RC STRAIN=FM;
RX PubMed=2997024; DOI=10.1111/j.1600-065x.1985.tb01146.x;
RA Nonaka M., Nakayama K., Yeul Y.D., Shimizu A., Takahashi M.;
RT "Molecular cloning and characterization of complementary and genomic DNA
RT clones for mouse C4 and Slp.";
RL Immunol. Rev. 87:81-99(1985).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=3464002; DOI=10.1073/pnas.83.20.7883;
RA Nonaka M., Kimura H., Yeul Y.D., Yokoyama S., Nakayama K., Takahashi M.;
RT "Identification of the 5'-flanking regulatory region responsible for the
RT difference in transcriptional control between mouse complement C4 and Slp
RT genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7883-7887(1986).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 591-1738.
RC STRAIN=C57BL/10 X DBA/2;
RX PubMed=3008092; DOI=10.1093/nar/14.6.2539;
RA Hemenway C., Kalff M., Stavenhagen J., Walthall D., Robins D.;
RT "Sequence comparison of alleles of the fourth component of complement (C4)
RT and sex-limited protein (Slp).";
RL Nucleic Acids Res. 14:2539-2554(1986).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 651-810 AND 924-1083.
RX PubMed=6208559; DOI=10.1073/pnas.81.21.6822;
RA Nonaka M., Takahashi M., Natsuume-Sakai S., Nonaka M., Tanaka S.,
RA Shimizu A., Honjo T.;
RT "Isolation of cDNA clones specifying the fourth component of mouse
RT complement and its isotype, sex-limited protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:6822-6826(1984).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 961-1290.
RX PubMed=2459207;
RA Taillon-Miller P.A., Shreffler D.C.;
RT "Structural basis for the C4d.1/C4d.2 serologic allotypes of murine
RT complement component C4.";
RL J. Immunol. 141:2382-2387(1988).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1099-1142.
RC STRAIN=B10.BR, B10.WR, C3H/He, C57BL/6J, CBA/J, and DBA/2J;
RX PubMed=2387317; DOI=10.1002/eji.1830200730;
RA Ogata R.T., Zepf N.E.;
RT "C4 from C4-high and C4-low mouse strains have identical sequences in the
RT region corresponding to the isotype-specific segment of human C4.";
RL Eur. J. Immunol. 20:1607-1610(1990).
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1105-1449.
RX PubMed=3856857; DOI=10.1073/pnas.82.6.1746;
RA Levi-Strauss M., Tosi M., Steinmetz M., Klein J., Meo T.;
RT "Multiple duplications of complement C4 gene correlate with H-2-controlled
RT testosterone-independent expression of its sex-limited isoform, C4-Slp.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1746-1750(1985).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1257-1376.
RX PubMed=6149581; DOI=10.1098/rstb.1984.0099;
RA Tosi M., Levi-Strauss M., Duponchel C., Meo T.;
RT "Sequence heterogeneity of murine complementary DNA clones related to the
RT C4 and C4-Slp isoforms of the fourth complement component.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 306:389-394(1984).
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1360-1511.
RX PubMed=6192448; DOI=10.1073/pnas.80.16.5061;
RA Ogata R.T., Shreffler D.C., Sepich D.S., Lilly S.P.;
RT "cDNA clone spanning the alpha-gamma subunit junction in the precursor of
RT the murine fourth complement component (C4).";
RL Proc. Natl. Acad. Sci. U.S.A. 80:5061-5065(1983).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1324.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Non-enzymatic component of 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. Catalyzes the transacylation of the thioester
CC carbonyl group to form ester bonds with carbohydrate antigens (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Circulates in blood as a disulfide-linked trimer of an alpha,
CC beta and gamma chain.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C0L5}. Synapse
CC {ECO:0000250|UniProtKB:P0C0L5}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P0C0L5}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P0C0L5}.
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.
CC -!- MISCELLANEOUS: C4 is a major histocompatibility complex class-III
CC protein.
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DR EMBL; M11789; AAA39557.1; -; Genomic_DNA.
DR EMBL; M11729; AAA39506.1; -; mRNA.
DR EMBL; M17440; AAA39561.1; -; Genomic_DNA.
DR EMBL; AK157954; BAE34280.1; -; mRNA.
DR EMBL; AK158256; BAE34429.1; -; mRNA.
DR EMBL; AF049850; AAC05279.1; -; Genomic_DNA.
DR EMBL; CT573030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067394; AAH67394.1; -; mRNA.
DR EMBL; BC067409; AAH67409.1; -; mRNA.
DR EMBL; M12968; AAA39558.1; -; Genomic_DNA.
DR EMBL; M12969; AAA39559.1; -; Genomic_DNA.
DR EMBL; M14225; AAA39563.1; -; Genomic_DNA.
DR EMBL; X05314; CAA28936.1; -; mRNA.
DR EMBL; M12970; AAA39555.1; -; mRNA.
DR EMBL; M12972; AAA39556.1; -; mRNA.
DR EMBL; M23186; AAA40487.1; -; Genomic_DNA.
DR EMBL; X55493; CAA39112.1; -; Genomic_DNA.
DR EMBL; X55495; CAA39114.1; -; Genomic_DNA.
DR EMBL; K02798; AAC42021.1; -; mRNA.
DR EMBL; K02799; AAC42022.1; -; mRNA.
DR EMBL; K00019; AAA39554.1; -; mRNA.
DR CCDS; CCDS28657.1; -.
DR PIR; A24558; A24558.
DR PIR; A29176; A29176.
DR RefSeq; NP_033910.2; NM_009780.2.
DR AlphaFoldDB; P01029; -.
DR SMR; P01029; -.
DR BioGRID; 198420; 14.
DR ComplexPortal; CPX-6198; Classical and lectin pathway C3 convertase complex C4b2a-B.
DR STRING; 10090.ENSMUSP00000069418; -.
DR MEROPS; I39.951; -.
DR GlyConnect; 720; 2 N-Linked glycans (1 site).
DR GlyGen; P01029; 4 sites, 4 N-linked glycans (1 site).
DR iPTMnet; P01029; -.
DR PhosphoSitePlus; P01029; -.
DR SwissPalm; P01029; -.
DR CPTAC; non-CPTAC-3339; -.
DR jPOST; P01029; -.
DR MaxQB; P01029; -.
DR PaxDb; P01029; -.
DR PRIDE; P01029; -.
DR ProteomicsDB; 279132; -.
DR DNASU; 12268; -.
DR Ensembl; ENSMUST00000069507; ENSMUSP00000069418; ENSMUSG00000073418.
DR GeneID; 12268; -.
DR KEGG; mmu:12268; -.
DR UCSC; uc008cdk.2; mouse.
DR CTD; 721; -.
DR MGI; MGI:88228; C4b.
DR VEuPathDB; HostDB:ENSMUSG00000073418; -.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000155739; -.
DR HOGENOM; CLU_001634_4_1_1; -.
DR InParanoid; P01029; -.
DR OMA; PSEKNCQ; -.
DR OrthoDB; 28894at2759; -.
DR PhylomeDB; P01029; -.
DR TreeFam; TF313285; -.
DR Reactome; R-MMU-166663; Initial triggering of complement.
DR Reactome; R-MMU-174577; Activation of C3 and C5.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 12268; 3 hits in 73 CRISPR screens.
DR ChiTaRS; C4b; mouse.
DR PRO; PR:P01029; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P01029; protein.
DR Bgee; ENSMUSG00000073418; Expressed in epididymal fat pad and 57 other tissues.
DR ExpressionAtlas; P01029; baseline and differential.
DR Genevisible; P01029; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005601; C:classical-complement-pathway C3/C5 convertase complex; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0106139; C:symbiont cell surface; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0001848; F:complement binding; ISO:MGI.
DR GO; GO:0001849; F:complement component C1q complex binding; ISO:MGI.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0006956; P:complement activation; IMP:MGI.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; 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; 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 Cell projection; Cleavage on pair of basic residues; Complement pathway;
KW Disulfide bond; Glycoprotein; Immunity; Inflammatory response;
KW Innate immunity; Reference proteome; Secreted; Signal; Sulfation; Synapse;
KW Thioester bond.
FT SIGNAL 1..19
FT CHAIN 20..673
FT /note="Complement C4 beta chain"
FT /id="PRO_0000005973"
FT PROPEP 674..677
FT /id="PRO_0000005974"
FT CHAIN 678..1443
FT /note="Complement C4 alpha chain"
FT /id="PRO_0000005975"
FT CHAIN 678..753
FT /note="C4a anaphylatoxin"
FT /id="PRO_0000005976"
FT PROPEP 1444..1447
FT /id="PRO_0000005977"
FT CHAIN 1448..1738
FT /note="Complement C4 gamma chain"
FT /id="PRO_0000005978"
FT DOMAIN 700..734
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 1589..1736
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT MOD_RES 1413
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 1416
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 1417
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 1324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 1387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 700..726
FT /evidence="ECO:0000250"
FT DISULFID 701..733
FT /evidence="ECO:0000250"
FT DISULFID 714..734
FT /evidence="ECO:0000250"
FT DISULFID 1589..1667
FT /evidence="ECO:0000250"
FT DISULFID 1612..1736
FT /evidence="ECO:0000250"
FT CROSSLNK 1006..1009
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
FT CONFLICT 132
FT /note="F -> Y (in Ref. 1; AAA39557)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="E -> G (in Ref. 4; BAE34429)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="A -> V (in Ref. 4; BAE34429)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="G -> E (in Ref. 1; AAA39557)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="E -> K (in Ref. 7; AAH67394/AAH67409)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="Q -> E (in Ref. 1; AAA39557 and 4; BAE34280)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="M -> T (in Ref. 1; AAA39557, 2; AAA39506, 3;
FT AAA39561, 4; BAE34280/BAE34429 and 7; AAH67394/AAH67409)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="D -> G (in Ref. 4; BAE34429)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="M -> I (in Ref. 4; BAE34280)"
FT /evidence="ECO:0000305"
FT CONFLICT 838
FT /note="P -> R (in Ref. 1; AAA39557)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="V -> I (in Ref. 4; BAE34280)"
FT /evidence="ECO:0000305"
FT CONFLICT 1077
FT /note="F -> S (in Ref. 7; AAH67394/AAH67409)"
FT /evidence="ECO:0000305"
FT CONFLICT 1119
FT /note="V -> A (in Ref. 14; AAC42021)"
FT /evidence="ECO:0000305"
FT CONFLICT 1190
FT /note="A -> T (in Ref. 14; AAC42021)"
FT /evidence="ECO:0000305"
FT CONFLICT 1206
FT /note="R -> Q (in Ref. 4; BAE34280/BAE34429, 7; AAH67394/
FT AAH67409 and 12; AAA40487)"
FT /evidence="ECO:0000305"
FT CONFLICT 1290
FT /note="S -> N (in Ref. 15; AAC42022)"
FT /evidence="ECO:0000305"
FT CONFLICT 1324
FT /note="N -> K (in Ref. 2; AAA39506, 3; AAA39561 and 14;
FT AAC42021)"
FT /evidence="ECO:0000305"
FT CONFLICT 1365
FT /note="K -> E (in Ref. 4; BAE34429)"
FT /evidence="ECO:0000305"
FT CONFLICT 1401
FT /note="G -> S (in Ref. 16; AAA39554)"
FT /evidence="ECO:0000305"
FT CONFLICT 1442
FT /note="R -> K (in Ref. 1; AAA39557)"
FT /evidence="ECO:0000305"
FT CONFLICT 1453
FT /note="V -> A (in Ref. 2; AAA39506, 3; AAA39561, 4;
FT BAE34429 and 16; AAA39554)"
FT /evidence="ECO:0000305"
FT CONFLICT 1456
FT /note="Q -> R (in Ref. 4; BAE34429)"
FT /evidence="ECO:0000305"
FT CONFLICT 1586
FT /note="E -> Q (in Ref. 10; CAA28936)"
FT /evidence="ECO:0000305"
FT CONFLICT 1611
FT /note="A -> T (in Ref. 5; AAC05279)"
FT /evidence="ECO:0000305"
SQ 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
