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

 CO4_RAT                 Reviewed;        1737 AA.
P08649; Q62895; Q8R403;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
25-MAR-2003, sequence version 3.
25-OCT-2017, entry version 144.
RecName: Full=Complement C4;
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=C4; Synonyms=C4a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
Chen C.-B., Wallis R.;
"Substrate recognition by zymogen and activated forms of mannose-
binding protein-associated serine proteases.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-266.
STRAIN=Brown Norway;
PubMed=12136338; DOI=10.1007/s00251-002-0460-x;
Walter L., Hurt P., Himmelbauer H., Sudbrak R., Guenther E.;
"Physical mapping of the major histocompatibility complex class II and
class III regions of the rat.";
Immunogenetics 54:268-275(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1656-1737, AND INDUCTION.
STRAIN=Sprague-Dawley; TISSUE=Hepatic stellate cell;
PubMed=8805663;
Fimmel C.J., Brown K.E., O'Neill R., Kladney R.D.;
"Complement C4 protein expression by rat hepatic stellate cells.";
J. Immunol. 157:2601-2609(1996).
[4]
PROTEIN SEQUENCE OF 678-753.
PubMed=3262196; DOI=10.1016/0161-5890(88)90101-0;
Cui L.-X., Ferreri K., Hugli T.E.;
"Structural characterization of the C4a anaphylatoxin from rat.";
Mol. Immunol. 25:663-671(1988).
[5]
PROTEIN SEQUENCE OF 678-753.
Cui L.-X., Ferreri K., Hugli T.E.;
"Characterization of rat anaphylatoxins C4a and C5a.";
Fed. Proc. 44:991-991(1985).
-!- 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 (By similarity).
{ECO:0000250}.
-!- FUNCTION: 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.
-!- SUBUNIT: 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.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C0L4}.
Cell junction, synapse {ECO:0000250|UniProtKB:P0C0L4}. Cell
projection, axon {ECO:0000250|UniProtKB:P0C0L4}. Cell projection,
dendrite {ECO:0000250|UniProtKB:P0C0L4}.
-!- INDUCTION: Induced in hepatic stellate cells by iron overload and
by gamma-interferon. {ECO:0000269|PubMed:8805663}.
-!- MISCELLANEOUS: C4 is a major histocompatibility complex class-III
protein.
-!- SEQUENCE CAUTION:
Sequence=AAA91231.1; Type=Frameshift; Positions=1721; Evidence={ECO:0000305};
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EMBL; AY149995; AAN72415.1; -; mRNA.
EMBL; AY091787; AAM14719.1; -; Genomic_DNA.
EMBL; U42719; AAA91231.1; ALT_FRAME; mRNA.
PIR; JL0036; JL0036.
RefSeq; NP_113692.2; NM_031504.3.
UniGene; Rn.155573; -.
UniGene; Rn.81052; -.
ProteinModelPortal; P08649; -.
SMR; P08649; -.
IntAct; P08649; 1.
STRING; 10116.ENSRNOP00000037902; -.
MEROPS; I39.951; -.
iPTMnet; P08649; -.
PhosphoSitePlus; P08649; -.
PaxDb; P08649; -.
PRIDE; P08649; -.
GeneID; 24233; -.
KEGG; rno:24233; -.
UCSC; RGD:620005; rat.
CTD; 720; -.
RGD; 620005; C4a.
eggNOG; KOG1366; Eukaryota.
eggNOG; ENOG410XRED; LUCA.
HOGENOM; HOG000290712; -.
HOVERGEN; HBG107123; -.
InParanoid; P08649; -.
KO; K03989; -.
PhylomeDB; P08649; -.
PMAP-CutDB; P08649; -.
PRO; PR:P08649; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
GO; GO:0006956; P:complement activation; TAS:RGD.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
Gene3D; 1.20.91.20; -; 1.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 2.60.40.690; -; 2.
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; 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.
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; Direct protein sequencing;
Disulfide bond; Glycoprotein; Immunity; Inflammatory response;
Innate immunity; Reference proteome; Secreted; Signal; Sulfation;
Synapse; Thioester bond.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 673 Complement C4 beta chain. {ECO:0000250}.
/FTId=PRO_0000005979.
PROPEP 674 677 {ECO:0000250}.
/FTId=PRO_0000005980.
CHAIN 678 1442 Complement C4 alpha chain. {ECO:0000250}.
/FTId=PRO_0000005981.
CHAIN 678 753 C4a anaphylatoxin.
/FTId=PRO_0000005982.
PROPEP 1443 1446 {ECO:0000250}.
/FTId=PRO_0000005983.
CHAIN 1447 1737 Complement C4 gamma chain. {ECO:0000250}.
/FTId=PRO_0000005984.
DOMAIN 700 734 Anaphylatoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00022}.
DOMAIN 1588 1735 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
MOD_RES 1412 1412 Sulfotyrosine. {ECO:0000250}.
MOD_RES 1414 1414 Sulfotyrosine. {ECO:0000250}.
MOD_RES 1416 1416 Sulfotyrosine. {ECO:0000250}.
MOD_RES 1676 1676 Sulfotyrosine. {ECO:0000255}.
CARBOHYD 224 224 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 664 664 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 743 743 N-linked (GlcNAc...) asparagine.
CARBOHYD 1323 1323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1386 1386 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 700 726 {ECO:0000250}.
DISULFID 701 733 {ECO:0000250}.
DISULFID 714 734 {ECO:0000250}.
DISULFID 1588 1666 {ECO:0000250}.
DISULFID 1611 1735 {ECO:0000250}.
CROSSLNK 1005 1008 Isoglutamyl cysteine thioester (Cys-Gln).
{ECO:0000250}.
CONFLICT 706 706 T -> A (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 1700 1700 T -> S (in Ref. 3; AAA91231).
{ECO:0000305}.
CONFLICT 1709 1709 R -> H (in Ref. 3; AAA91231).
{ECO:0000305}.
CONFLICT 1731 1731 S -> R (in Ref. 3; AAA91231).
{ECO:0000305}.
SEQUENCE 1737 AA; 192163 MW; 67FA7BFA27A3DDFA CRC64;
MRLLWGLAWA FSFFASSLQK PRLLLFSPSV VNLGTPLSVG VQLLDAPAGQ EVKGSVYLRN
PTSGPCSPKK DFKLSSGNDF VLLRLEVPLK DVRSCGLFGL RRAPHIQLVA HSPWLKNTAS
KATETQGVNL LFSSRRGHIF VQTDQPIYNP GQRVRYRVFA LDQKMRPSTD TLTVTVENSH
GLRVRKKEVF APTSIFQDDF IIPDISEPGT WKISARFSDG LESNRSTHFE VKKYVLPNFE
VKLTPWKPYI LTVPSYREEI QLDVQARYVY GKPVQGVAYT RFALMDEQGK KSFLRGLETQ
TKLVEGQTHI SISRDQFQAA LGKVNTEIGD LEGLRLYAAV AVIESPGGEM EEAELTSWPF
VSSAFSLDLS HTKQHLVPGA PFLLQALVRE MSGSEASDVP VKVSATLLSG SDSKVLDFQQ
NTNGIGQVSF SIHVPPTITE LRLLVSAGSL YPAVAKLTVQ APPSRGPGFL SIEPLDLRSP
RVGDTFVLSL RTVGIPMPTF SHYYYMIISR GQIMAMSREP RRALTSISVL VDHHLAPSFY
FVAYFYHQGL PVANSLLINV QPGDCEGKLE LKVDGAKEYR NGDSMKLQLQ TDSEALVALG
AVDTALYAVG GRSHKPLDMS KVFEVMNSYN LGCGPGGGDD ALQVFQTAGL AFSDGDRLTQ
TKENLSCPKE KKSRQKRNVN FQKAISEKLG QYSSPDTKRC CQDGMTKLPM ARTCEQRAAR
VPQPACREPF LSCCKFAEDL RRNQTRSQAG LARAQDMLQE EDLIDEDDIL VRSFFPENWL
WRVEPVDRSK LLTVWLPDSL TTWEIHGVSL SKSKGLCVAK PTRVRVFREF HLHLRLPISV
RRFEQLELRP VLYNYLSEDV TVSVHVSPVE GLCLAGGGLL AQQVSVPAGS ARPVAFSVVP
TAAASIPLKV VARGSFTIGD AVSKILQIEK EGAIHREEIV YNLDPLNNLG RSLEIPGSSD
PNVIPDGDFS SFVRVTASEP LETLGSEGAL SPGGVASLLR LPRGCAEQTM IYLAPTLTAS
HYLDRTEQWS KLPPETKDHA VDLIQKGHMR IQQFRKKDGS FGAWLHRDSS TWLTAFVLKI
LSLAQEQIGD SPEKLQETAG WLLGQQLDDG SFHDPCPVIH RGMQGGLVGT DETVALTAFV
VIALHHGLAV FQDENSQQLK KRVEASITKA NSFLGQKASA GLLGAHASAI TAYALTLTKA
SEDLQNVAHN SLMAMAEETG ENLYWGSAIG SQDNVVSSTP APRNPSEPVP QAPALWIETT
AYGLLHLLLR EGKGEMADKV ATWLTHQGSF QGGFRSTQDT VVTLDALSAY WIASHTTEEK
ALNVTLSSMG RNGYKSHLLQ LNNHQVKGLE EELKFSLGST INVKVGGNSK GTLKILRTYN
VLDMKNTTCQ DLRIEVTVTG YVEYTREANE DYEYDYDMPA ADDPSVHSQP VTPLQLFEGR
RSRRRREAPK AADEQESRVQ YTVCIWRNGN LGLSGMAIAD ITLLSGFQAL RADLEKLTSL
SDRYVSHFET DGPHVLLYFD SVPTTRECVG FGALQEVAVG LVQPASAVLY DYYSPDHKCS
VFYAAPTKSK LLSTLCSADV CQCAEGKCPR QRRSLERGVE DKDGYRMKFA CYYPRVEYGF
QVKVLREDSR AAFRLFETKI TQVLHFTKDA KASIGQTRNF LVRASCRLRL EPSKEYLIMG
MDGVTSDLKG DPQYLLDSNT WIEEMPSERL CRSTRQRAAC GQLNDFLQEY SSQGCQV


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