CO4_BOVIN
ID CO4_BOVIN Reviewed; 920 AA.
AC P01030; Q27992; Q27993;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Complement C4;
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; Fragments;
GN Name=C4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE OF 1-77.
RX PubMed=6760852; DOI=10.1042/bj2070253;
RA Smith M.A., Gerrie L.M., Dunbar B., Fothergill J.E.;
RT "Primary structure of bovine complement activation fragment C4a, the third
RT anaphylatoxin. Purification and complete amino acid sequence.";
RL Biochem. J. 207:253-260(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-920.
RC TISSUE=Liver;
RA Groth D.M.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
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 process. 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 -!- MISCELLANEOUS: C4 is a major histocompatibility complex class-III
CC protein.
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DR EMBL; U16750; AAA52751.1; -; mRNA.
DR EMBL; U16749; AAA52750.1; -; mRNA.
DR PIR; A01265; A01265.
DR MEROPS; I39.951; -.
DR PaxDb; P01030; -.
DR PeptideAtlas; P01030; -.
DR PRIDE; P01030; -.
DR eggNOG; KOG1366; Eukaryota.
DR InParanoid; P01030; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0006956; P:complement activation; IBA:GO_Central.
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 CDD; cd00017; ANATO; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
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; IPR019742; MacrogloblnA2_CS.
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; PF07677; A2M_recep; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF07678; TED_complement; 1.
DR PRINTS; PR00004; ANAPHYLATOXN.
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 Sulfation; Synapse; Thioester bond.
FT CHAIN 1..622
FT /note="Complement C4 alpha chain"
FT /id="PRO_0000005962"
FT CHAIN 1..77
FT /note="C4a anaphylatoxin"
FT /id="PRO_0000005963"
FT PROPEP 623..629
FT /id="PRO_0000005964"
FT CHAIN 630..920
FT /note="Complement C4 gamma chain"
FT /id="PRO_0000005965"
FT DOMAIN 23..57
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 771..918
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT MOD_RES 593
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 596
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 598
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..49
FT /evidence="ECO:0000250"
FT DISULFID 24..56
FT /evidence="ECO:0000250"
FT DISULFID 37..57
FT /evidence="ECO:0000250"
FT DISULFID 771..849
FT /evidence="ECO:0000250"
FT DISULFID 794..918
FT /evidence="ECO:0000250"
FT CROSSLNK 191..194
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT NON_CONS 77..78
FT /evidence="ECO:0000305"
FT NON_CONS 342..343
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 920 AA; 101885 MW; 1425A0BD945F5497 CRC64;
NVNFQKAIHE KLGQYTSPVA KRCCQDGLTR LPMARTCEQR AARVQQPACR EPFLSCCQFA
ESLRKKARTR GQVGLARVGF SVVPIAAAAV SLKVVARGSF DFPVGDAISK ILQVEREGAL
HREEMVYELN PLDPLGRTLE IPGNSDPNII PEGDFKSFVR VTASDPLEAL GSEGALSPGG
LASLLRLPQG CAEQTMTLLA PTLAASRYLD KTEQWSMLPP ETKDRAVDLI QKGYTRIQEF
RKRDGSYGAW LHRDSSTWLT AFVLKILSLA QDQVXGSAEK LQETATWLLS QQRDDGPFHD
PCPVIHREMQ GGLVGSDETV ALTAFVVIAL HHGLAVLPDK NSRVENSISR ANTFLGAKAT
SGLLGSHASA ITAYALSLTE APEDLRRVAH NNLMAMAKDI GDKLYWGSVT TSPSNVLSPT
PAPRSPADPI PQAPAMSIET TAYGLLHLLL WEGKAELADQ AASWLTRQGS FQGGFRSTQD
TVVALDALSA YWIASYTAEE KGLNVTLSSL GRSGLKSHVL QLTNHQVHRL EEELQFSLGS
KINVEVRGNS KGTLKVLRSY NVMDMTNTTC QDLQIEVTVM GHVEYTMEAE EDYEDYEYED
LLAGDDPEAH SRXVTPLQLF DGRRNRRRRE APKAAEERES RVQYTVCIWR TGKVGLSGMA
IADITLLSGF HALRADLEKL TSLSDRYVSH FETEGPHVLL YFDSVPTSRE CVGFGAVQEV
PVGLVQPASA ILYDYYNPEH KCSVFYGAPR KSKLLSTLCS ADVCQCAEGK CPRQRRALER
GQQDLEGYRM KFACYSPRVD YGFQVKVLRE DSRAAFRLFE TRITQVLHFT KDAGATADQT
RNFLVRASCR LQLEPGKEYL IMGLDGATYD LKGDPQYLLD SNSWIEEMPS ERMCQSTRHR
TPCAQLNSFL QEYGTQXCQV
