C4b-binding protein alpha chain

Details

Name
C4b-binding protein alpha chain
Synonyms
  • C4BP
  • Proline-rich protein
  • PRP
Gene Name
C4BPA
Organism
Humans
Amino acid sequence
>lcl|BSEQ0049812|C4b-binding protein alpha chain
MHPPKTPSGALHRKRKMAAWPFSRLWKVSDPILFQMTLIAALLPAVLGNCGPPPTLSFAA
PMDITLTETRFKTGTTLKYTCLPGYVRSHSTQTLTCNSDGEWVYNTFCIYKRCRHPGELR
NGQVEIKTDLSFGSQIEFSCSEGFFLIGSTTSRCEVQDRGVGWSHPLPQCEIVKCKPPPD
IRNGRHSGEENFYAYGFSVTYSCDPRFSLLGHASISCTVENETIGVWRPSPPTCEKITCR
KPDVSHGEMVSGFGPIYNYKDTIVFKCQKGFVLRGSSVIHCDADSKWNPSPPACEPNSCI
NLPDIPHASWETYPRPTKEDVYVVGTVLRYRCHPGYKPTTDEPTTVICQKNLRWTPYQGC
EALCCPEPKLNNGEITQHRKSRPANHCVYFYGDEISFSCHETSRFSAICQGDGTWSPRTP
SCGDICNFPPKIAHGHYKQSSSYSFFKEEIIYECDKGYILVGQAKLSCSYSHWSAPAPQC
KALCRKPELVNGRLSVDKDQYVEPENVTIQCDSGYGVVGPQSITCSGNRTWYPEVPKCEW
ETPEGCEQVLTGKRLMQCLPNPEDVKMALEVYKLSLEIEQLELQRDSARQSTLDKEL
Number of residues
597
Molecular Weight
67032.63
Theoretical pI
Not Available
GO Classification
Functions
RNA binding
Processes
complement activation, classical pathway / innate immune response / negative regulation of complement activation, classical pathway / positive regulation of protein catabolic process / regulation of complement activation / regulation of opsonization
Components
blood microparticle / extracellular region / extracellular space / other organism cell / plasma membrane
General Function
Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component.
Specific Function
Rna binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0049813|C4b-binding protein alpha chain (C4BPA)
ATGCACCCCCCAAAAACTCCATCTGGGGCTCTTCATAGAAAAAGGAAAATGGCAGCCTGG
CCCTTCTCCAGGCTGTGGAAAGTCTCTGATCCAATTCTCTTCCAAATGACCTTGATCGCT
GCTCTGTTGCCTGCTGTTCTTGGCAATTGTGGTCCTCCACCCACTTTATCATTTGCTGCC
CCGATGGATATTACGTTGACTGAGACACGCTTCAAAACTGGAACTACTCTGAAATACACC
TGCCTCCCTGGCTACGTCAGATCCCATTCAACTCAGACGCTTACCTGTAATTCTGATGGC
GAATGGGTGTATAACACCTTCTGTATCTACAAACGATGCAGACACCCAGGAGAGTTACGT
AATGGGCAAGTAGAGATTAAGACAGATTTATCTTTTGGATCACAAATAGAATTCAGCTGT
TCAGAAGGATTTTTCTTAATTGGCTCAACCACTAGTCGTTGTGAAGTCCAAGATAGAGGA
GTTGGCTGGAGTCATCCTCTCCCACAATGTGAAATTGTCAAGTGTAAGCCTCCTCCAGAC
ATCAGGAATGGAAGGCACAGCGGTGAAGAAAATTTCTACGCATACGGCTTTTCTGTCACC
TACAGCTGTGACCCCCGCTTCTCACTCTTGGGCCATGCCTCCATTTCTTGCACTGTGGAG
AATGAAACAATAGGTGTTTGGAGACCAAGCCCTCCTACCTGTGAAAAAATCACCTGTCGC
AAGCCAGATGTTTCACATGGGGAAATGGTCTCTGGATTTGGACCCATCTATAATTACAAA
GACACTATTGTGTTTAAGTGCCAAAAAGGTTTTGTTCTCAGAGGCAGCAGTGTAATTCAT
TGTGATGCTGATAGCAAATGGAATCCTTCTCCTCCTGCTTGTGAGCCCAATAGTTGTATT
AATTTACCAGACATTCCACATGCTTCCTGGGAAACATATCCTAGGCCGACAAAAGAGGAT
GTGTATGTTGTTGGGACTGTGTTAAGGTACCGCTGTCATCCTGGCTACAAACCCACTACA
GATGAGCCTACGACTGTGATTTGTCAGAAAAATTTGAGATGGACCCCATACCAAGGATGT
GAGGCGTTATGTTGCCCTGAACCAAAGCTAAATAATGGTGAAATCACTCAACACAGGAAA
AGTCGTCCTGCCAATCACTGTGTTTATTTCTATGGAGATGAGATTTCATTTTCATGTCAT
GAGACCAGTAGGTTTTCAGCTATATGCCAAGGAGATGGCACGTGGAGTCCCCGAACACCA
TCATGTGGAGACATTTGCAATTTTCCTCCTAAAATTGCCCATGGGCATTATAAACAATCT
AGTTCATACAGCTTTTTCAAAGAAGAGATTATATATGAATGTGATAAAGGCTACATTCTG
GTCGGACAGGCGAAACTCTCCTGCAGTTATTCACACTGGTCAGCTCCAGCCCCTCAATGT
AAAGCTCTGTGTCGGAAACCAGAATTAGTGAATGGAAGGTTGTCTGTGGATAAGGATCAG
TATGTTGAGCCTGAAAATGTCACCATCCAATGTGATTCTGGCTATGGTGTGGTTGGTCCC
CAAAGTATCACTTGCTCTGGGAACAGAACCTGGTACCCAGAGGTGCCCAAGTGTGAGTGG
GAGACCCCCGAAGGCTGTGAACAAGTGCTCACAGGCAAAAGACTCATGCAGTGTCTCCCA
AACCCAGAGGATGTGAAAATGGCCCTGGAGGTATATAAGCTGTCTCTGGAAATTGAACAA
CTGGAACTACAGAGAGACAGCGCAAGACAATCCACTTTGGATAAAGAACTATAA
Chromosome Location
1
Locus
1q32.2
External Identifiers
ResourceLink
UniProtKB IDP04003
UniProtKB Entry NameC4BPA_HUMAN
HGNC IDHGNC:1325
General References
  1. Matsuguchi T, Okamura S, Aso T, Sata T, Niho Y: Molecular cloning of the cDNA coding for proline-rich protein (PRP): identity of PRP as C4b-binding protein. Biochem Biophys Res Commun. 1989 Nov 30;165(1):138-44. [Article]
  2. Aso T, Okamura S, Matsuguchi T, Sakamoto N, Sata T, Niho Y: Genomic organization of the alpha chain of the human C4b-binding protein gene. Biochem Biophys Res Commun. 1991 Jan 15;174(1):222-7. [Article]
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  5. Lintin SJ, Lewin AR, Reid KB: Derivation of the sequence of the signal peptide in human C4b-binding protein and interspecies cross-hybridisation of the C4bp cDNA sequence. FEBS Lett. 1988 May 23;232(2):328-32. [Article]
  6. Lintin SJ, Reid KB: Studies on the structure of the human C4b-binding protein gene. FEBS Lett. 1986 Aug 11;204(1):77-81. [Article]
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  8. Chung LP, Gagnon J, Reid KB: Amino acid sequence studies of human C4b-binding protein: N-terminal sequence analysis and alignment of the fragments produced by limited proteolysis with chymotrypsin and the peptides produced by cyanogen bromide treatment. Mol Immunol. 1985 Apr;22(4):427-35. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB09130Copperapproved, investigationalunknownDetails
DB01593Zincapproved, investigationalunknownDetails
DB14487Zinc acetateapproved, investigationalunknownDetails
DB14533Zinc chlorideapproved, investigationalunknownmodulatorDetails
DB14548Zinc sulfate, unspecified formapproved, experimentalunknownmodulatorDetails