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Protein

Complement C4

Gene

C4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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 (By similarity).By similarity
Derived from proteolytic degradation of complement C4, C4a anaphylatoxin is a mediator of local inflammatory processes. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Complement pathway, Immunity, Inflammatory response, Innate immunity

Protein family/group databases

MEROPSiI39.951.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C4
Cleaved into the following 4 chains:
Gene namesi
Name:C4
Synonyms:C4a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620005. C4a.

Subcellular locationi

  • Secreted By similarity
  • Cell junctionsynapse By similarity
  • Cell projectionaxon By similarity
  • Cell projectiondendrite By similarity

GO - Cellular componenti

  • axon Source: UniProtKB-SubCell
  • cell junction Source: UniProtKB-KW
  • dendrite Source: UniProtKB-SubCell
  • extracellular region Source: UniProtKB
  • extracellular space Source: RGD
  • synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Secreted, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000000597920 – 673Complement C4 beta chainBy similarityAdd BLAST654
PropeptideiPRO_0000005980674 – 677By similarity4
ChainiPRO_0000005981678 – 1442Complement C4 alpha chainBy similarityAdd BLAST765
ChainiPRO_0000005982678 – 753C4a anaphylatoxinAdd BLAST76
PropeptideiPRO_00000059831443 – 1446By similarity4
ChainiPRO_00000059841447 – 1737Complement C4 gamma chainBy similarityAdd BLAST291

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi224N-linked (GlcNAc...)Sequence analysis1
Glycosylationi664N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi700 ↔ 726By similarity
Disulfide bondi701 ↔ 733By similarity
Disulfide bondi714 ↔ 734By similarity
Glycosylationi743N-linked (GlcNAc...)1
Cross-linki1005 ↔ 1008Isoglutamyl cysteine thioester (Cys-Gln)By similarity
Glycosylationi1323N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1386N-linked (GlcNAc...)Sequence analysis1
Modified residuei1412SulfotyrosineBy similarity1
Modified residuei1414SulfotyrosineBy similarity1
Modified residuei1416SulfotyrosineBy similarity1
Disulfide bondi1588 ↔ 1666By similarity
Disulfide bondi1611 ↔ 1735By similarity
Modified residuei1676SulfotyrosineSequence analysis1

Keywords - PTMi

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

Proteomic databases

PaxDbiP08649.
PRIDEiP08649.

PTM databases

iPTMnetiP08649.
PhosphoSitePlusiP08649.

Miscellaneous databases

PMAP-CutDBP08649.

Expressioni

Inductioni

Induced in hepatic stellate cells by iron overload and by gamma-interferon.1 Publication

Interactioni

Subunit structurei

This protein is synthesized as a single-chain precursor and, prior to secretion, is enzymatically cleaved to form a trimer of non-identical chains alpha, beta and gamma.

Protein-protein interaction databases

IntActiP08649. 1 interactor.
STRINGi10116.ENSRNOP00000037902.

Structurei

3D structure databases

ProteinModelPortaliP08649.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini700 – 734Anaphylatoxin-likePROSITE-ProRule annotationAdd BLAST35
Domaini1588 – 1735NTRPROSITE-ProRule annotationAdd BLAST148

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
HOGENOMiHOG000290712.
HOVERGENiHBG107123.
InParanoidiP08649.
KOiK03989.
PhylomeDBiP08649.

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.
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 1 hit.
SM00104. 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.

P08649-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLWGLAWA FSFFASSLQK PRLLLFSPSV VNLGTPLSVG VQLLDAPAGQ
60 70 80 90 100
EVKGSVYLRN PTSGPCSPKK DFKLSSGNDF VLLRLEVPLK DVRSCGLFGL
110 120 130 140 150
RRAPHIQLVA HSPWLKNTAS KATETQGVNL LFSSRRGHIF VQTDQPIYNP
160 170 180 190 200
GQRVRYRVFA LDQKMRPSTD TLTVTVENSH GLRVRKKEVF APTSIFQDDF
210 220 230 240 250
IIPDISEPGT WKISARFSDG LESNRSTHFE VKKYVLPNFE VKLTPWKPYI
260 270 280 290 300
LTVPSYREEI QLDVQARYVY GKPVQGVAYT RFALMDEQGK KSFLRGLETQ
310 320 330 340 350
TKLVEGQTHI SISRDQFQAA LGKVNTEIGD LEGLRLYAAV AVIESPGGEM
360 370 380 390 400
EEAELTSWPF VSSAFSLDLS HTKQHLVPGA PFLLQALVRE MSGSEASDVP
410 420 430 440 450
VKVSATLLSG SDSKVLDFQQ NTNGIGQVSF SIHVPPTITE LRLLVSAGSL
460 470 480 490 500
YPAVAKLTVQ APPSRGPGFL SIEPLDLRSP RVGDTFVLSL RTVGIPMPTF
510 520 530 540 550
SHYYYMIISR GQIMAMSREP RRALTSISVL VDHHLAPSFY FVAYFYHQGL
560 570 580 590 600
PVANSLLINV QPGDCEGKLE LKVDGAKEYR NGDSMKLQLQ TDSEALVALG
610 620 630 640 650
AVDTALYAVG GRSHKPLDMS KVFEVMNSYN LGCGPGGGDD ALQVFQTAGL
660 670 680 690 700
AFSDGDRLTQ TKENLSCPKE KKSRQKRNVN FQKAISEKLG QYSSPDTKRC
710 720 730 740 750
CQDGMTKLPM ARTCEQRAAR VPQPACREPF LSCCKFAEDL RRNQTRSQAG
760 770 780 790 800
LARAQDMLQE EDLIDEDDIL VRSFFPENWL WRVEPVDRSK LLTVWLPDSL
810 820 830 840 850
TTWEIHGVSL SKSKGLCVAK PTRVRVFREF HLHLRLPISV RRFEQLELRP
860 870 880 890 900
VLYNYLSEDV TVSVHVSPVE GLCLAGGGLL AQQVSVPAGS ARPVAFSVVP
910 920 930 940 950
TAAASIPLKV VARGSFTIGD AVSKILQIEK EGAIHREEIV YNLDPLNNLG
960 970 980 990 1000
RSLEIPGSSD PNVIPDGDFS SFVRVTASEP LETLGSEGAL SPGGVASLLR
1010 1020 1030 1040 1050
LPRGCAEQTM IYLAPTLTAS HYLDRTEQWS KLPPETKDHA VDLIQKGHMR
1060 1070 1080 1090 1100
IQQFRKKDGS FGAWLHRDSS TWLTAFVLKI LSLAQEQIGD SPEKLQETAG
1110 1120 1130 1140 1150
WLLGQQLDDG SFHDPCPVIH RGMQGGLVGT DETVALTAFV VIALHHGLAV
1160 1170 1180 1190 1200
FQDENSQQLK KRVEASITKA NSFLGQKASA GLLGAHASAI TAYALTLTKA
1210 1220 1230 1240 1250
SEDLQNVAHN SLMAMAEETG ENLYWGSAIG SQDNVVSSTP APRNPSEPVP
1260 1270 1280 1290 1300
QAPALWIETT AYGLLHLLLR EGKGEMADKV ATWLTHQGSF QGGFRSTQDT
1310 1320 1330 1340 1350
VVTLDALSAY WIASHTTEEK ALNVTLSSMG RNGYKSHLLQ LNNHQVKGLE
1360 1370 1380 1390 1400
EELKFSLGST INVKVGGNSK GTLKILRTYN VLDMKNTTCQ DLRIEVTVTG
1410 1420 1430 1440 1450
YVEYTREANE DYEYDYDMPA ADDPSVHSQP VTPLQLFEGR RSRRRREAPK
1460 1470 1480 1490 1500
AADEQESRVQ YTVCIWRNGN LGLSGMAIAD ITLLSGFQAL RADLEKLTSL
1510 1520 1530 1540 1550
SDRYVSHFET DGPHVLLYFD SVPTTRECVG FGALQEVAVG LVQPASAVLY
1560 1570 1580 1590 1600
DYYSPDHKCS VFYAAPTKSK LLSTLCSADV CQCAEGKCPR QRRSLERGVE
1610 1620 1630 1640 1650
DKDGYRMKFA CYYPRVEYGF QVKVLREDSR AAFRLFETKI TQVLHFTKDA
1660 1670 1680 1690 1700
KASIGQTRNF LVRASCRLRL EPSKEYLIMG MDGVTSDLKG DPQYLLDSNT
1710 1720 1730
WIEEMPSERL CRSTRQRAAC GQLNDFLQEY SSQGCQV
Length:1,737
Mass (Da):192,163
Last modified:March 25, 2003 - v3
Checksum:i67FA7BFA27A3DDFA
GO

Sequence cautioni

The sequence AAA91231 differs from that shown. Reason: Frameshift at position 1721.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti706T → A AA sequence (Ref. 5) Curated1
Sequence conflicti1700T → S in AAA91231 (PubMed:8805663).Curated1
Sequence conflicti1709R → H in AAA91231 (PubMed:8805663).Curated1
Sequence conflicti1731S → R in AAA91231 (PubMed:8805663).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY149995 mRNA. Translation: AAN72415.1.
AY091787 Genomic DNA. Translation: AAM14719.1.
U42719 mRNA. Translation: AAA91231.1. Frameshift.
PIRiJL0036.
RefSeqiNP_113692.2. NM_031504.3.
UniGeneiRn.155573.
Rn.81052.

Genome annotation databases

GeneIDi24233.
KEGGirno:24233.
UCSCiRGD:620005. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY149995 mRNA. Translation: AAN72415.1.
AY091787 Genomic DNA. Translation: AAM14719.1.
U42719 mRNA. Translation: AAA91231.1. Frameshift.
PIRiJL0036.
RefSeqiNP_113692.2. NM_031504.3.
UniGeneiRn.155573.
Rn.81052.

3D structure databases

ProteinModelPortaliP08649.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP08649. 1 interactor.
STRINGi10116.ENSRNOP00000037902.

Protein family/group databases

MEROPSiI39.951.

PTM databases

iPTMnetiP08649.
PhosphoSitePlusiP08649.

Proteomic databases

PaxDbiP08649.
PRIDEiP08649.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24233.
KEGGirno:24233.
UCSCiRGD:620005. rat.

Organism-specific databases

CTDi720.
RGDi620005. C4a.

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
HOGENOMiHOG000290712.
HOVERGENiHBG107123.
InParanoidiP08649.
KOiK03989.
PhylomeDBiP08649.

Miscellaneous databases

PMAP-CutDBP08649.
PROiP08649.

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.
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 1 hit.
SM00104. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiCO4_RAT
AccessioniPrimary (citable) accession number: P08649
Secondary accession number(s): Q62895, Q8R403
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: March 25, 2003
Last modified: November 2, 2016
This is version 140 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.