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CO4_RAT
ID   CO4_RAT                 Reviewed;        1737 AA.
AC   P08649; Q62895; Q8R403;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 3.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Complement C4;
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=C4; Synonyms=C4a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Chen C.-B., Wallis R.;
RT   "Substrate recognition by zymogen and activated forms of mannose-binding
RT   protein-associated serine proteases.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-266.
RC   STRAIN=Brown Norway;
RX   PubMed=12136338; DOI=10.1007/s00251-002-0460-x;
RA   Walter L., Hurt P., Himmelbauer H., Sudbrak R., Guenther E.;
RT   "Physical mapping of the major histocompatibility complex class II and
RT   class III regions of the rat.";
RL   Immunogenetics 54:268-275(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1656-1737, AND INDUCTION.
RC   STRAIN=Sprague-Dawley; TISSUE=Hepatic stellate cell;
RX   PubMed=8805663;
RA   Fimmel C.J., Brown K.E., O'Neill R., Kladney R.D.;
RT   "Complement C4 protein expression by rat hepatic stellate cells.";
RL   J. Immunol. 157:2601-2609(1996).
RN   [4]
RP   PROTEIN SEQUENCE OF 678-753.
RX   PubMed=3262196; DOI=10.1016/0161-5890(88)90101-0;
RA   Cui L.-X., Ferreri K., Hugli T.E.;
RT   "Structural characterization of the C4a anaphylatoxin from rat.";
RL   Mol. Immunol. 25:663-671(1988).
RN   [5]
RP   PROTEIN SEQUENCE OF 678-753.
RA   Cui L.-X., Ferreri K., Hugli T.E.;
RT   "Characterization of rat anaphylatoxins C4a and C5a.";
RL   Fed. Proc. 44:991-991(1985).
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 (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Derived from proteolytic degradation of complement C4, C4a
CC       anaphylatoxin is a mediator of local inflammatory processes. It induces
CC       the contraction of smooth muscle, increases vascular permeability and
CC       causes histamine release from mast cells and basophilic leukocytes.
CC   -!- SUBUNIT: This protein is synthesized as a single-chain precursor and,
CC       prior to secretion, is enzymatically cleaved to form a trimer of non-
CC       identical chains alpha, beta and gamma.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C0L4}. Synapse
CC       {ECO:0000250|UniProtKB:P0C0L4}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:P0C0L4}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:P0C0L4}.
CC   -!- INDUCTION: Induced in hepatic stellate cells by iron overload and by
CC       gamma-interferon. {ECO:0000269|PubMed:8805663}.
CC   -!- MISCELLANEOUS: C4 is a major histocompatibility complex class-III
CC       protein.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA91231.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY149995; AAN72415.1; -; mRNA.
DR   EMBL; AY091787; AAM14719.1; -; Genomic_DNA.
DR   EMBL; U42719; AAA91231.1; ALT_FRAME; mRNA.
DR   PIR; JL0036; JL0036.
DR   RefSeq; NP_113692.2; NM_031504.3.
DR   AlphaFoldDB; P08649; -.
DR   SMR; P08649; -.
DR   BioGRID; 246420; 1.
DR   IntAct; P08649; 2.
DR   MINT; P08649; -.
DR   STRING; 10116.ENSRNOP00000037902; -.
DR   MEROPS; I39.951; -.
DR   GlyGen; P08649; 5 sites.
DR   iPTMnet; P08649; -.
DR   PhosphoSitePlus; P08649; -.
DR   jPOST; P08649; -.
DR   PaxDb; P08649; -.
DR   PRIDE; P08649; -.
DR   GeneID; 24233; -.
DR   KEGG; rno:24233; -.
DR   UCSC; RGD:620005; rat.
DR   CTD; 720; -.
DR   RGD; 620005; C4a.
DR   eggNOG; KOG1366; Eukaryota.
DR   InParanoid; P08649; -.
DR   OrthoDB; 28894at2759; -.
DR   PhylomeDB; P08649; -.
DR   Reactome; R-RNO-166663; Initial triggering of complement.
DR   Reactome; R-RNO-174577; Activation of C3 and C5.
DR   Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR   Reactome; R-RNO-977606; Regulation of Complement cascade.
DR   SABIO-RK; P08649; -.
DR   PRO; PR:P08649; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030424; C:axon; ISO:RGD.
DR   GO; GO:0005601; C:classical-complement-pathway C3/C5 convertase complex; ISO:RGD.
DR   GO; GO:0030425; C:dendrite; ISO:RGD.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0001849; F:complement component C1q complex binding; ISO:RGD.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0006956; P:complement activation; ISO:RGD.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:2000427; P:positive regulation of apoptotic cell clearance; ISO:RGD.
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; IPR040839; MG4.
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; PF17789; MG4; 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   Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW   Inflammatory response; Innate immunity; Reference proteome; Secreted;
KW   Signal; Sulfation; Synapse; Thioester bond.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..673
FT                   /note="Complement C4 beta chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000005979"
FT   PROPEP          674..677
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000005980"
FT   CHAIN           678..1442
FT                   /note="Complement C4 alpha chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000005981"
FT   CHAIN           678..753
FT                   /note="C4a anaphylatoxin"
FT                   /id="PRO_0000005982"
FT   PROPEP          1443..1446
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000005983"
FT   CHAIN           1447..1737
FT                   /note="Complement C4 gamma chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000005984"
FT   DOMAIN          700..734
FT                   /note="Anaphylatoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT   DOMAIN          1588..1735
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   MOD_RES         1412
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1414
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1416
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1676
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        664
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        743
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        1323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1386
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        1588..1666
FT                   /evidence="ECO:0000250"
FT   DISULFID        1611..1735
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        1005..1008
FT                   /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        706
FT                   /note="T -> A (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1700
FT                   /note="T -> S (in Ref. 3; AAA91231)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1709
FT                   /note="R -> H (in Ref. 3; AAA91231)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1731
FT                   /note="S -> R (in Ref. 3; AAA91231)"
FT                   /evidence="ECO:0000305"
SQ   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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