P01029 (CO4B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Complement C4-B

Cleaved into the following 4 chains:

1. Complement C4 beta chain
2. Complement C4 alpha chain
3. C4a anaphylatoxin
4. Complement C4 gamma chain

Gene names

Name:	C4b
Synonyms:	C4

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1738 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	Circulates in blood as a disulfide-linked trimer of an alpha, beta and gamma chain.
Subcellular location	Secreted.
Post-translational modification	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.
Sequence similarities	Contains 1 anaphylatoxin-like domain. Contains 1 NTR domain.

Ontologies

Keywords
Biological process	Complement pathway Immunity Inflammatory response Innate immunity
Cellular component	Secreted
Domain	Signal
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Sulfation Thioester bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of endopeptidase activity Inferred from electronic annotation. Source: GOC
Cellular_component	extracellular space Inferred from electronic annotation. Source: InterPro
Molecular_function	endopeptidase inhibitor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19
	Chain	20 – 673	654	Complement C4 beta chain		PRO_0000005973
	Propeptide	674 – 677	4			PRO_0000005974
	Chain	678 – 1443	766	Complement C4 alpha chain		PRO_0000005975
	Chain	678 – 753	76	C4a anaphylatoxin		PRO_0000005976
	Propeptide	1444 – 1447	4			PRO_0000005977
	Chain	1448 – 1738	291	Complement C4 gamma chain		PRO_0000005978
Regions
	Domain	700 – 734	35	Anaphylatoxin-like
	Domain	1589 – 1736	148	NTR
Amino acid modifications
	Modified residue	1413	1	Sulfotyrosine
	Modified residue	1416	1	Sulfotyrosine
	Modified residue	1417	1	Sulfotyrosine
	Glycosylation	224	1	N-linked (GlcNAc...) Potential
	Glycosylation	743	1	N-linked (GlcNAc...)
	Glycosylation	1324	1	N-linked (GlcNAc...) Ref.17
	Glycosylation	1387	1	N-linked (GlcNAc...) Potential
	Disulfide bond	700 ↔ 726		By similarity
	Disulfide bond	701 ↔ 733		By similarity
	Disulfide bond	714 ↔ 734		By similarity
	Disulfide bond	1589 ↔ 1667		By similarity
	Disulfide bond	1612 ↔ 1736		By similarity
	Cross-link	1006 ↔ 1009		Isoglutamyl cysteine thioester (Cys-Gln) By similarity
Experimental info
	Sequence conflict	132	1	F → Y in AAA39557. Ref.1
	Sequence conflict	177	1	E → G in BAE34429. Ref.4
	Sequence conflict	283	1	A → V in BAE34429. Ref.4
	Sequence conflict	327	1	G → E in AAA39557. Ref.1
	Sequence conflict	440	1	E → K in AAH67394. Ref.7
	Sequence conflict	440	1	E → K in AAH67409. Ref.7
	Sequence conflict	570	1	Q → E in AAA39557. Ref.1
	Sequence conflict	570	1	Q → E in BAE34280. Ref.4
	Sequence conflict	604	1	M → T in AAA39557. Ref.1
	Sequence conflict	604	1	M → T in AAA39506. Ref.2
	Sequence conflict	604	1	M → T in AAA39561. Ref.3
	Sequence conflict	604	1	M → T in BAE34280. Ref.4
	Sequence conflict	604	1	M → T in BAE34429. Ref.4
	Sequence conflict	604	1	M → T in AAH67394. Ref.7
	Sequence conflict	604	1	M → T in AAH67409. Ref.7
	Sequence conflict	639	1	D → G in BAE34429. Ref.4
	Sequence conflict	758	1	M → I in BAE34280. Ref.4
	Sequence conflict	838	1	P → R in AAA39557. Ref.1
	Sequence conflict	916	1	V → I in BAE34280. Ref.4
	Sequence conflict	1077	1	F → S in AAH67394. Ref.7
	Sequence conflict	1077	1	F → S in AAH67409. Ref.7
	Sequence conflict	1119	1	V → A in AAC42021. Ref.14
	Sequence conflict	1190	1	A → T in AAC42021. Ref.14
	Sequence conflict	1206	1	R → Q in BAE34280. Ref.4
	Sequence conflict	1206	1	R → Q in BAE34429. Ref.4
	Sequence conflict	1206	1	R → Q in AAH67394. Ref.7
	Sequence conflict	1206	1	R → Q in AAH67409. Ref.7
	Sequence conflict	1206	1	R → Q in AAA40487. Ref.12
	Sequence conflict	1290	1	S → N in AAC42022. Ref.15
	Sequence conflict	1324	1	N → K in AAA39506. Ref.2
	Sequence conflict	1324	1	N → K in AAA39561. Ref.3
	Sequence conflict	1324	1	N → K in AAC42021. Ref.14
	Sequence conflict	1365	1	K → E in BAE34429. Ref.4
	Sequence conflict	1401	1	G → S in AAA39554. Ref.16
	Sequence conflict	1442	1	R → K in AAA39557. Ref.1
	Sequence conflict	1453	1	V → A in AAA39506. Ref.2
	Sequence conflict	1453	1	V → A in AAA39561. Ref.3
	Sequence conflict	1453	1	V → A in BAE34429. Ref.4
	Sequence conflict	1453	1	V → A in AAA39554. Ref.16
	Sequence conflict	1456	1	Q → R in BAE34429. Ref.4
	Sequence conflict	1586	1	E → Q in CAA28936. Ref.10
	Sequence conflict	1611	1	A → T in AAC05279. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P01029 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: FCC7580209029E88	FASTA	1,738	192,915
	10 20 30 40 50 60 MRLLWGLAWV FSFCASSLQK PRLLLFSPSV VNLGTPLSVG VQLLDAPPGQ EVKGSVFLRN 70 80 90 100 110 120 PKGGSCSPKK DFKLSSGDDF VLLSLEVPLE DVRSCGLFDL RRAPHIQLVA QSPWLRNTAF 130 140 150 160 170 180 KATETQGVNL LFSSRRGHIF VQTDQPIYNP GQRVRYRVFA LDQKMRPSTD FLTITVENSH 190 200 210 220 230 240 GLRVLKKEIF TSTSIFQDAF TIPDISEPGT WKISARFSDG LESNRSTHFE VKKYVLPNFE 250 260 270 280 290 300 VKITPWKPYI LMVPSNSDEI QLDIQARYIY GKPVQGVAYT RFALMDEQGK RTFLRGLETQ 310 320 330 340 350 360 AKLVEGRTHI SISKDQFQAA LDKINIGVRD LEGLRLYAAT AVIESPGGEM EEAELTSWRF 370 380 390 400 410 420 VSSAFSLDLS RTKRHLVPGA HFLLQALVQE MSGSEASNVP VKVSATLVSG SDSQVLDIQQ 430 440 450 460 470 480 STNGIGQVSI SFPIPPTVTE LRLLVSAGSL YPAIARLTVQ APPSRGTGFL SIEPLDPRSP 490 500 510 520 530 540 SVGDTFILNL QPVGIPAPTF SHYYYMIISR GQIMAMGREP RKTVTSVSVL VDHQLAPSFY 550 560 570 580 590 600 FVAYFYHQGH PVANSLLINI QSRDCEGKLQ LKVDGAKEYR NADMMKLRIQ TDSKALVALG 610 620 630 640 650 660 AVDMALYAVG GRSHKPLDMS KVFEVINSYN VGCGPGGGDD ALQVFQDAGL AFSDGDRLTQ 670 680 690 700 710 720 TREDLSCPKE KKSRQKRNVN FQKAVSEKLG QYSSPDAKRC CQDGMTKLPM KRTCEQRAAR 730 740 750 760 770 780 VPQQACREPF LSCCKFAEDL RRNQTRSQAH LARNNHNMLQ EEDLIDEDDI LVRTSFPENW 790 800 810 820 830 840 LWRVEPVDSS KLLTVWLPDS MTTWEIHGVS LSKSKGLCVA KPTRVRVFRK FHLHLRLPIS 850 860 870 880 890 900 IRRFEQFELR PVLYNYLNDD VAVSVHVTPV EGLCLAGGGM MAQQVTVPAG SARPVAFSVV 910 920 930 940 950 960 PTAAANVPLK VVARGVFDLG DAVSKILQIE KEGAIHREEL VYNLDPLNNL GRTLEIPGSS 970 980 990 1000 1010 1020 DPNIVPDGDF SSLVRVTASE PLETMGSEGA LSPGGVASLL RLPQGCAEQT MIYLAPTLTA 1030 1040 1050 1060 1070 1080 SNYLDRTEQW SKLSPETKDH AVDLIQKGYM RIQQFRKNDG SFGAWLHRDS STWLTAFVLK 1090 1100 1110 1120 1130 1140 ILSLAQEQVG NSPEKLQETA SWLLAQQLGD GSFHDPCPVI HRAMQGGLVG SDETVALTAF 1150 1160 1170 1180 1190 1200 VVIALHHGLD VFQDDDAKQL KNRVEASITK ANSFLGQKAS AGLLGAHAAA ITAYALTLTK 1210 1220 1230 1240 1250 1260 ASEDLRNVAH NSLMAMAEET GEHLYWGLVL GSQDKVVLRP TAPRSPTEPV PQAPALWIET 1270 1280 1290 1300 1310 1320 TAYALLHLLL REGKGKMADK AASWLTHQGS FHGAFRSTQD TVVTLDALSA YWIASHTTEE 1330 1340 1350 1360 1370 1380 KALNVTLSSM GRNGLKTHGL HLNNHQVKGL EEELKFSLGS TISVKVEGNS KGTLKILRTY 1390 1400 1410 1420 1430 1440 NVLDMKNTTC QDLQIEVKVT GAVEYAWDAN EDYEDYYDMP AADDPSVPLQ PVTPLQLFEG 1450 1460 1470 1480 1490 1500 RRSRRRREAP KVVEEQESRV QYTVCIWRNG KLGLSGMAIA DITLLSGFHA LRADLEKLTS 1510 1520 1530 1540 1550 1560 LSDRYVSHFE TDGPHVLLYF DSVPTTRECV GFGASQEVVV GLVQPSSAVL YDYYSPDHKC 1570 1580 1590 1600 1610 1620 SVFYAAPTKS QLLATLCSGD VCQCAEGKCP RLLRSLERRV EDKDGYRMRF ACYYPRVEYG 1630 1640 1650 1660 1670 1680 FTVKVLREDG RAAFRLFESK ITQVLHFRKD TMASIGQTRN FLSRASCRLR LEPNKEYLIM 1690 1700 1710 1720 1730 GMDGETSDNK GDPQYLLDSN TWIEEMPSEQ MCKSTRHRAA CFQLKDFLME FSSRGCQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete nucleotide and derived amino acid sequences of the fourth component of mouse complement (C4). Evolutionary aspects." Nonaka M., Nakayama K., Yeul Y.D., Takahashi M. J. Biol. Chem. 260:10936-10943(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FM.
[2]	"Complete cDNA sequence of the fourth component of murine complement." Sepich D.S., Noonan D.J., Ogata R.T. Proc. Natl. Acad. Sci. U.S.A. 82:5895-5899(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: B10.WR.
[3]	"Sequence of the gene for murine complement component C4." Ogata R.T., Rosa P.A., Zepf N.E. J. Biol. Chem. 264:16565-16572(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B10.WR.
[4]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Inner ear.
[5]	"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse." Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L. Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 129.
[6]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and CD-1. Tissue: Germ cell and Neural stem cell.
[8]	"Molecular cloning and characterization of complementary and genomic DNA clones for mouse C4 and Slp." Nonaka M., Nakayama K., Yeul Y.D., Shimizu A., Takahashi M. Immunol. Rev. 87:81-99(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-128. Strain: FM.
[9]	"Identification of the 5'-flanking regulatory region responsible for the difference in transcriptional control between mouse complement C4 and Slp genes." Nonaka M., Kimura H., Yeul Y.D., Yokoyama S., Nakayama K., Takahashi M. Proc. Natl. Acad. Sci. U.S.A. 83:7883-7887(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[10]	"Sequence comparison of alleles of the fourth component of complement (C4) and sex-limited protein (Slp)." Hemenway C., Kalff M., Stavenhagen J., Walthall D., Robins D. Nucleic Acids Res. 14:2539-2554(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 591-1738. Strain: C57BL/10 X DBA/2.
[11]	"Isolation of cDNA clones specifying the fourth component of mouse complement and its isotype, sex-limited protein." Nonaka M., Takahashi M., Natsuume-Sakai S., Nonaka M., Tanaka S., Shimizu A., Honjo T. Proc. Natl. Acad. Sci. U.S.A. 81:6822-6826(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 651-810 AND 924-1083.
[12]	"Structural basis for the C4d.1/C4d.2 serologic allotypes of murine complement component C4." Taillon-Miller P.A., Shreffler D.C. J. Immunol. 141:2382-2387(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 961-1290.
[13]	"C4 from C4-high and C4-low mouse strains have identical sequences in the region corresponding to the isotype-specific segment of human C4." Ogata R.T., Zepf N.E. Eur. J. Immunol. 20:1607-1610(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1099-1142. Strain: B10.BR, B10.WR, C3H/He, C57BL/6, CBA/J and DBA/2.
[14]	"Multiple duplications of complement C4 gene correlate with H-2-controlled testosterone-independent expression of its sex-limited isoform, C4-Slp." Levi-Strauss M., Tosi M., Steinmetz M., Klein J., Meo T. Proc. Natl. Acad. Sci. U.S.A. 82:1746-1750(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1105-1449.
[15]	"Sequence heterogeneity of murine complementary DNA clones related to the C4 and C4-Slp isoforms of the fourth complement component." Tosi M., Levi-Strauss M., Duponchel C., Meo T. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 306:389-394(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1257-1376.
[16]	"cDNA clone spanning the alpha-gamma subunit junction in the precursor of the murine fourth complement component (C4)." Ogata R.T., Shreffler D.C., Sepich D.S., Lilly S.P. Proc. Natl. Acad. Sci. U.S.A. 80:5061-5065(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1360-1511.
[17]	"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides." Bernhard O.K., Kapp E.A., Simpson R.J. J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1324, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Plasma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M11789 Genomic DNA. Translation: AAA39557.1. M11729 mRNA. Translation: AAA39506.1. M17440 Genomic DNA. Translation: AAA39561.1. AK157954 mRNA. Translation: BAE34280.1. AK158256 mRNA. Translation: BAE34429.1. AF049850 Genomic DNA. Translation: AAC05279.1. CT573030 Genomic DNA. No translation available. BC067394 mRNA. Translation: AAH67394.1. BC067409 mRNA. Translation: AAH67409.1. M12968 Genomic DNA. Translation: AAA39558.1. M12969 Genomic DNA. Translation: AAA39559.1. M14225 Genomic DNA. Translation: AAA39563.1. X05314 mRNA. Translation: CAA28936.1. M12970 mRNA. Translation: AAA39555.1. M12972 mRNA. Translation: AAA39556.1. M23186 Genomic DNA. Translation: AAA40487.1. X55493 Genomic DNA. Translation: CAA39112.1. X55495 Genomic DNA. Translation: CAA39114.1. K02798 mRNA. Translation: AAC42021.1. K02799 mRNA. Translation: AAC42022.1. K00019 mRNA. Translation: AAA39554.1.
IPI	IPI00131091.
PIR	A24558. A29176.
RefSeq	NP_033910.2. NM_009780.2. XP_978162.1. XM_973068.2.
UniGene	Mm.439678. Mm.477109.
3D structure databases
ProteinModelPortal	P01029.
SMR	P01029. Positions 679-1416, 1449-1738.
ModBase	Search...
Protein family/group databases
MEROPS	I39.951.
PTM databases
PhosphoSite	P01029.
Proteomic databases
PaxDb	P01029.
PRIDE	P01029.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000069507; ENSMUSP00000069418; ENSMUSG00000073418.
GeneID	12268. 675521.
KEGG	mmu:12268. mmu:675521.
Organism-specific databases
CTD	721.
MGI	MGI:88228. C4b.
Phylogenomic databases
eggNOG	COG2373.
GeneTree	ENSGT00560000077078.
HOVERGEN	HBG107123.
InParanoid	P01029.
KO	K03989.
OMA	PSERLCQ.
OrthoDB	EOG4JM7NW.
Gene expression databases
ArrayExpress	P01029.
Bgee	P01029.
CleanEx	MM_C4B.
Genevestigator	P01029.
GermOnline	ENSMUSG00000073418. Mus musculus.
Family and domain databases
Gene3D	1.20.91.20. 1 hit. 2.60.40.690. 1 hit.
InterPro	IPR009048. A-macroglobulin_rcpt-bd. IPR011626. A2M_comp. IPR002890. A2M_N. IPR011625. A2M_N_2. IPR000020. Anaphylatoxin/fibulin. IPR018081. Anaphylatoxin_. IPR001840. Anaphylatoxn. IPR001599. Macroglobln_a2. IPR019742. MacrogloblnA2_CS. IPR019565. MacrogloblnA2_thiol-ester-bond. IPR001134. Netrin_domain. IPR018933. Netrin_module_non-TIMP. IPR008930. Terpenoid_cyclase/PrenylTrfase. IPR008993. TIMP-like_OB-fold. [Graphical view]
Pfam	PF00207. A2M. 1 hit. PF07678. A2M_comp. 1 hit. PF01835. A2M_N. 1 hit. PF07703. A2M_N_2. 1 hit. PF07677. A2M_recep. 1 hit. PF01821. ANATO. 1 hit. PF01759. NTR. 1 hit. PF10569. Thiol-ester_cl. 1 hit. [Graphical view]
PRINTS	PR00004. ANAPHYLATOXN.
SMART	SM00104. ANATO. 1 hit. SM00643. C345C. 1 hit. [Graphical view]
SUPFAM	SSF49410. AM_receptor_bind. 1 hit. SSF47686. Anaphylatoxin. 1 hit. SSF48239. Terp_cyc_toroid. 1 hit. SSF50242. TIMP_like. 1 hit.
PROSITE	PS00477. ALPHA_2_MACROGLOBULIN. 1 hit. PS01177. ANAPHYLATOXIN_1. 1 hit. PS01178. ANAPHYLATOXIN_2. 1 hit. PS50189. NTR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	280722.
SOURCE	Search...

Entry information

Entry name

CO4B_MOUSE

Accession

Primary (citable) accession number: P01029
Secondary accession number(s): E9QKK7 , O70346, Q31201, Q3TYY1, Q3TZC9, Q61372, Q61859, Q62353, Q6NWV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 134 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program