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P01029

- CO4B_MOUSE

UniProt

P01029 - CO4B_MOUSE

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Protein

Complement C4-B

Gene

C4b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. endopeptidase inhibitor activity Source: InterPro

GO - Biological processi

  1. complement activation, classical pathway Source: UniProtKB-KW
  2. inflammatory response Source: UniProtKB-KW
  3. innate immune response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Complement pathway, Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_198562. Regulation of Complement cascade.
REACT_202834. Initial triggering of complement.
REACT_213087. Activation of C3 and C5.

Protein family/group databases

MEROPSiI39.951.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C4-B
Cleaved into the following 4 chains:
Gene namesi
Name:C4b
Synonyms:C4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:88228. C4b.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 673654Complement C4 beta chainPRO_0000005973Add
BLAST
Propeptidei674 – 6774PRO_0000005974
Chaini678 – 1443766Complement C4 alpha chainPRO_0000005975Add
BLAST
Chaini678 – 75376C4a anaphylatoxinPRO_0000005976Add
BLAST
Propeptidei1444 – 14474PRO_0000005977
Chaini1448 – 1738291Complement C4 gamma chainPRO_0000005978Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi224 – 2241N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi700 ↔ 726By similarity
Disulfide bondi701 ↔ 733By similarity
Disulfide bondi714 ↔ 734By similarity
Glycosylationi743 – 7431N-linked (GlcNAc...)
Cross-linki1006 ↔ 1009Isoglutamyl cysteine thioester (Cys-Gln)By similarity
Glycosylationi1324 – 13241N-linked (GlcNAc...)1 Publication
Glycosylationi1387 – 13871N-linked (GlcNAc...)Sequence Analysis
Modified residuei1413 – 14131SulfotyrosineBy similarity
Modified residuei1416 – 14161SulfotyrosineBy similarity
Modified residuei1417 – 14171SulfotyrosineBy similarity
Disulfide bondi1589 ↔ 1667By similarity
Disulfide bondi1612 ↔ 1736By similarity

Post-translational modificationi

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.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Sulfation, Thioester bond

Proteomic databases

MaxQBiP01029.
PaxDbiP01029.
PRIDEiP01029.

PTM databases

PhosphoSiteiP01029.

Expressioni

Gene expression databases

BgeeiP01029.
CleanExiMM_C4B.
ExpressionAtlasiP01029. baseline and differential.
GenevestigatoriP01029.

Interactioni

Subunit structurei

Circulates in blood as a disulfide-linked trimer of an alpha, beta and gamma chain.

Protein-protein interaction databases

IntActiP01029. 2 interactions.
MINTiMINT-1857263.

Structurei

3D structure databases

ProteinModelPortaliP01029.
SMRiP01029. Positions 679-1416, 1449-1738.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini700 – 73435Anaphylatoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini1589 – 1736148NTRPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 anaphylatoxin-like domain.PROSITE-ProRule annotation
Contains 1 NTR domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2373.
GeneTreeiENSGT00760000118982.
HOVERGENiHBG107123.
InParanoidiP01029.
KOiK03989.
OMAiTAYFKDE.
OrthoDBiEOG77HDCX.
TreeFamiTF313285.

Family and domain databases

Gene3Di1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
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]
PfamiPF00207. 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]
PRINTSiPR00004. ANAPHYLATOXN.
SMARTiSM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view]
SUPFAMiSSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01029-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLLWGLAWV FSFCASSLQK PRLLLFSPSV VNLGTPLSVG VQLLDAPPGQ
60 70 80 90 100
EVKGSVFLRN PKGGSCSPKK DFKLSSGDDF VLLSLEVPLE DVRSCGLFDL
110 120 130 140 150
RRAPHIQLVA QSPWLRNTAF KATETQGVNL LFSSRRGHIF VQTDQPIYNP
160 170 180 190 200
GQRVRYRVFA LDQKMRPSTD FLTITVENSH GLRVLKKEIF TSTSIFQDAF
210 220 230 240 250
TIPDISEPGT WKISARFSDG LESNRSTHFE VKKYVLPNFE VKITPWKPYI
260 270 280 290 300
LMVPSNSDEI QLDIQARYIY GKPVQGVAYT RFALMDEQGK RTFLRGLETQ
310 320 330 340 350
AKLVEGRTHI SISKDQFQAA LDKINIGVRD LEGLRLYAAT AVIESPGGEM
360 370 380 390 400
EEAELTSWRF VSSAFSLDLS RTKRHLVPGA HFLLQALVQE MSGSEASNVP
410 420 430 440 450
VKVSATLVSG SDSQVLDIQQ STNGIGQVSI SFPIPPTVTE LRLLVSAGSL
460 470 480 490 500
YPAIARLTVQ APPSRGTGFL SIEPLDPRSP SVGDTFILNL QPVGIPAPTF
510 520 530 540 550
SHYYYMIISR GQIMAMGREP RKTVTSVSVL VDHQLAPSFY FVAYFYHQGH
560 570 580 590 600
PVANSLLINI QSRDCEGKLQ LKVDGAKEYR NADMMKLRIQ TDSKALVALG
610 620 630 640 650
AVDMALYAVG GRSHKPLDMS KVFEVINSYN VGCGPGGGDD ALQVFQDAGL
660 670 680 690 700
AFSDGDRLTQ TREDLSCPKE KKSRQKRNVN FQKAVSEKLG QYSSPDAKRC
710 720 730 740 750
CQDGMTKLPM KRTCEQRAAR VPQQACREPF LSCCKFAEDL RRNQTRSQAH
760 770 780 790 800
LARNNHNMLQ EEDLIDEDDI LVRTSFPENW LWRVEPVDSS KLLTVWLPDS
810 820 830 840 850
MTTWEIHGVS LSKSKGLCVA KPTRVRVFRK FHLHLRLPIS IRRFEQFELR
860 870 880 890 900
PVLYNYLNDD VAVSVHVTPV EGLCLAGGGM MAQQVTVPAG SARPVAFSVV
910 920 930 940 950
PTAAANVPLK VVARGVFDLG DAVSKILQIE KEGAIHREEL VYNLDPLNNL
960 970 980 990 1000
GRTLEIPGSS DPNIVPDGDF SSLVRVTASE PLETMGSEGA LSPGGVASLL
1010 1020 1030 1040 1050
RLPQGCAEQT MIYLAPTLTA SNYLDRTEQW SKLSPETKDH AVDLIQKGYM
1060 1070 1080 1090 1100
RIQQFRKNDG SFGAWLHRDS STWLTAFVLK ILSLAQEQVG NSPEKLQETA
1110 1120 1130 1140 1150
SWLLAQQLGD GSFHDPCPVI HRAMQGGLVG SDETVALTAF VVIALHHGLD
1160 1170 1180 1190 1200
VFQDDDAKQL KNRVEASITK ANSFLGQKAS AGLLGAHAAA ITAYALTLTK
1210 1220 1230 1240 1250
ASEDLRNVAH NSLMAMAEET GEHLYWGLVL GSQDKVVLRP TAPRSPTEPV
1260 1270 1280 1290 1300
PQAPALWIET TAYALLHLLL REGKGKMADK AASWLTHQGS FHGAFRSTQD
1310 1320 1330 1340 1350
TVVTLDALSA YWIASHTTEE KALNVTLSSM GRNGLKTHGL HLNNHQVKGL
1360 1370 1380 1390 1400
EEELKFSLGS TISVKVEGNS KGTLKILRTY NVLDMKNTTC QDLQIEVKVT
1410 1420 1430 1440 1450
GAVEYAWDAN EDYEDYYDMP AADDPSVPLQ PVTPLQLFEG RRSRRRREAP
1460 1470 1480 1490 1500
KVVEEQESRV QYTVCIWRNG KLGLSGMAIA DITLLSGFHA LRADLEKLTS
1510 1520 1530 1540 1550
LSDRYVSHFE TDGPHVLLYF DSVPTTRECV GFGASQEVVV GLVQPSSAVL
1560 1570 1580 1590 1600
YDYYSPDHKC SVFYAAPTKS QLLATLCSGD VCQCAEGKCP RLLRSLERRV
1610 1620 1630 1640 1650
EDKDGYRMRF ACYYPRVEYG FTVKVLREDG RAAFRLFESK ITQVLHFRKD
1660 1670 1680 1690 1700
TMASIGQTRN FLSRASCRLR LEPNKEYLIM GMDGETSDNK GDPQYLLDSN
1710 1720 1730
TWIEEMPSEQ MCKSTRHRAA CFQLKDFLME FSSRGCQV
Length:1,738
Mass (Da):192,915
Last modified:July 27, 2011 - v3
Checksum:iFCC7580209029E88
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321F → Y in AAA39557. (PubMed:2993295)Curated
Sequence conflicti177 – 1771E → G in BAE34429. (PubMed:16141072)Curated
Sequence conflicti283 – 2831A → V in BAE34429. (PubMed:16141072)Curated
Sequence conflicti327 – 3271G → E in AAA39557. (PubMed:2993295)Curated
Sequence conflicti440 – 4401E → K in AAH67394. (PubMed:15489334)Curated
Sequence conflicti440 – 4401E → K in AAH67409. (PubMed:15489334)Curated
Sequence conflicti570 – 5701Q → E in AAA39557. (PubMed:2993295)Curated
Sequence conflicti570 – 5701Q → E in BAE34280. (PubMed:16141072)Curated
Sequence conflicti604 – 6041M → T in AAA39557. (PubMed:2993295)Curated
Sequence conflicti604 – 6041M → T in AAA39506. (PubMed:3862104)Curated
Sequence conflicti604 – 6041M → T in AAA39561. (PubMed:2777798)Curated
Sequence conflicti604 – 6041M → T in BAE34280. (PubMed:16141072)Curated
Sequence conflicti604 – 6041M → T in BAE34429. (PubMed:16141072)Curated
Sequence conflicti604 – 6041M → T in AAH67394. (PubMed:15489334)Curated
Sequence conflicti604 – 6041M → T in AAH67409. (PubMed:15489334)Curated
Sequence conflicti639 – 6391D → G in BAE34429. (PubMed:16141072)Curated
Sequence conflicti758 – 7581M → I in BAE34280. (PubMed:16141072)Curated
Sequence conflicti838 – 8381P → R in AAA39557. (PubMed:2993295)Curated
Sequence conflicti916 – 9161V → I in BAE34280. (PubMed:16141072)Curated
Sequence conflicti1077 – 10771F → S in AAH67394. (PubMed:15489334)Curated
Sequence conflicti1077 – 10771F → S in AAH67409. (PubMed:15489334)Curated
Sequence conflicti1119 – 11191V → A in AAC42021. (PubMed:3856857)Curated
Sequence conflicti1190 – 11901A → T in AAC42021. (PubMed:3856857)Curated
Sequence conflicti1206 – 12061R → Q in BAE34280. (PubMed:16141072)Curated
Sequence conflicti1206 – 12061R → Q in BAE34429. (PubMed:16141072)Curated
Sequence conflicti1206 – 12061R → Q in AAH67394. (PubMed:15489334)Curated
Sequence conflicti1206 – 12061R → Q in AAH67409. (PubMed:15489334)Curated
Sequence conflicti1206 – 12061R → Q in AAA40487. (PubMed:2459207)Curated
Sequence conflicti1290 – 12901S → N in AAC42022. (PubMed:6149581)Curated
Sequence conflicti1324 – 13241N → K in AAA39506. (PubMed:3862104)Curated
Sequence conflicti1324 – 13241N → K in AAA39561. (PubMed:2777798)Curated
Sequence conflicti1324 – 13241N → K in AAC42021. (PubMed:3856857)Curated
Sequence conflicti1365 – 13651K → E in BAE34429. (PubMed:16141072)Curated
Sequence conflicti1401 – 14011G → S in AAA39554. (PubMed:6192448)Curated
Sequence conflicti1442 – 14421R → K in AAA39557. (PubMed:2993295)Curated
Sequence conflicti1453 – 14531V → A in AAA39506. (PubMed:3862104)Curated
Sequence conflicti1453 – 14531V → A in AAA39561. (PubMed:2777798)Curated
Sequence conflicti1453 – 14531V → A in BAE34429. (PubMed:16141072)Curated
Sequence conflicti1453 – 14531V → A in AAA39554. (PubMed:6192448)Curated
Sequence conflicti1456 – 14561Q → R in BAE34429. (PubMed:16141072)Curated
Sequence conflicti1586 – 15861E → Q in CAA28936. (PubMed:3008092)Curated
Sequence conflicti1611 – 16111A → T in AAC05279. (PubMed:14656967)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS28657.1.
PIRiA24558.
A29176.
RefSeqiNP_033910.2. NM_009780.2.
XP_006544540.1. XM_006544477.1.
UniGeneiMm.439678.
Mm.477109.

Genome annotation databases

EnsembliENSMUST00000069507; ENSMUSP00000069418; ENSMUSG00000073418.
GeneIDi102643089.
12268.
KEGGimmu:102643089.
mmu:12268.
UCSCiuc008cdk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS28657.1.
PIRi A24558.
A29176.
RefSeqi NP_033910.2. NM_009780.2.
XP_006544540.1. XM_006544477.1.
UniGenei Mm.439678.
Mm.477109.

3D structure databases

ProteinModelPortali P01029.
SMRi P01029. Positions 679-1416, 1449-1738.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P01029. 2 interactions.
MINTi MINT-1857263.

Protein family/group databases

MEROPSi I39.951.

PTM databases

PhosphoSitei P01029.

Proteomic databases

MaxQBi P01029.
PaxDbi P01029.
PRIDEi P01029.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000069507 ; ENSMUSP00000069418 ; ENSMUSG00000073418 .
GeneIDi 102643089.
12268.
KEGGi mmu:102643089.
mmu:12268.
UCSCi uc008cdk.2. mouse.

Organism-specific databases

CTDi 721.
MGIi MGI:88228. C4b.

Phylogenomic databases

eggNOGi COG2373.
GeneTreei ENSGT00760000118982.
HOVERGENi HBG107123.
InParanoidi P01029.
KOi K03989.
OMAi TAYFKDE.
OrthoDBi EOG77HDCX.
TreeFami TF313285.

Enzyme and pathway databases

Reactomei REACT_198562. Regulation of Complement cascade.
REACT_202834. Initial triggering of complement.
REACT_213087. Activation of C3 and C5.

Miscellaneous databases

NextBioi 280722.
PROi P01029.
SOURCEi Search...

Gene expression databases

Bgeei P01029.
CleanExi MM_C4B.
ExpressionAtlasi P01029. baseline and differential.
Genevestigatori P01029.

Family and domain databases

Gene3Di 1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProi IPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
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 ]
Pfami 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 ]
PRINTSi PR00004. ANAPHYLATOXN.
SMARTi SM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view ]
SUPFAMi SSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEi PS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    Strain: C57BL/6.
    Tissue: Plasma.

Entry informationi

Entry nameiCO4B_MOUSE
AccessioniPrimary (citable) accession number: P01029
Secondary accession number(s): E9QKK7
, O70346, Q31201, Q3TYY1, Q3TZC9, Q61372, Q61859, Q62353, Q6NWV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

C4 is a major histocompatibility complex class-III protein.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3