C4b-binding protein alpha chain precursor

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Reviewed, UniProtKB/Swiss-Prot P04003 (C4BPA_HUMAN)

Last modified January 19, 2010. Version 109. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    C4b-binding protein alpha chain
      Short name=C4bp
Alternative name(s):
    Proline-rich protein
      Short name=PRP

Gene names

Name:	C4BPA
Synonyms:	C4BP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	597 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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.
Subunit structure	Disulfide-linked complex of alpha and beta chains of 3 possible sorts: a 570 kDa complex of 7 alpha chains and 1 beta chain, a 530 kDa homoheptamer of alpha chains or a 500 kDa complex of 6 alpha chains and 1 beta chain. The central body of the alpha chain homopolymer supports tentacles, each with the binding site for C4b at the end.
Subcellular location	Secreted.
Tissue specificity	Chylomicrons in the plasma.
Sequence similarities	Contains 8 Sushi (CCP/SCR) domains.
Caution	It is uncertain whether Met-1 or Met-17 is the initiator.

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Ontologies

Keywords
Biological process	Complement pathway Immune response Innate immunity
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Sushi
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Non-traceable author statement. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
arp4	P13050	3	EBI-978348,EBI-978341	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 48

Ref.7

Chain

49 – 597

549

C4b-binding protein alpha chain

PRO_0000005888

Regions

Domain

49 – 110

Sushi 1

Domain

111 – 172

Sushi 2

Domain

173 – 236

Sushi 3

Domain

237 – 296

Sushi 4

Domain

297 – 362

Sushi 5

Domain

363 – 424

Sushi 6

Domain

425 – 482

Sushi 7

Domain

483 – 540

Sushi 8

Amino acid modifications

Glycosylation

221

N-linked (GlcNAc...) Ref.9 Ref.10 Ref.6

Glycosylation

506

N-linked (GlcNAc...) Ref.9 Ref.10 Ref.8 Ref.6

Glycosylation

528

N-linked (GlcNAc...) Ref.8 Ref.6

Disulfide bond

50 ↔ 96

By similarity

Disulfide bond

81 ↔ 108

By similarity

Disulfide bond

113 ↔ 154

By similarity

Disulfide bond

140 ↔ 170

By similarity

Disulfide bond

175 ↔ 217

By similarity

Disulfide bond

203 ↔ 234

By similarity

Disulfide bond

239 ↔ 281

By similarity

Disulfide bond

267 ↔ 294

By similarity

Disulfide bond

299 ↔ 348

By similarity

Disulfide bond

332 ↔ 360

By similarity

Disulfide bond

365 ↔ 409

By similarity

Disulfide bond

399 ↔ 422

By similarity

Disulfide bond

426 ↔ 468

By similarity

Disulfide bond

454 ↔ 480

By similarity

Disulfide bond

484 ↔ 525

By similarity

Disulfide bond

511 ↔ 538

By similarity

Disulfide bond

546

Interchain (with beta chain) Potential

Disulfide bond

558

Interchain (with beta chain) Potential

Natural variations

Natural variant

P → Q: dbSNP rs55867570.

VAR_061123

Natural variant

A → V: dbSNP rs17020956.

VAR_048815

Natural variant

240

R → H: dbSNP rs45574833.

VAR_061124

Natural variant

300

I → T: dbSNP rs4844573.

VAR_024420

Natural variant

357

Y → H

VAR_001978

Natural variant

473

W → L: dbSNP rs1801341.

VAR_012038

Secondary structure

597

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P04003-1 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 67E03F2EA85A16DD
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FASTA

597

67,033

        10         20         30         40         50         60 
MHPPKTPSGA LHRKRKMAAW PFSRLWKVSD PILFQMTLIA ALLPAVLGNC GPPPTLSFAA 

        70         80         90        100        110        120 
PMDITLTETR FKTGTTLKYT CLPGYVRSHS TQTLTCNSDG EWVYNTFCIY KRCRHPGELR 

       130        140        150        160        170        180 
NGQVEIKTDL SFGSQIEFSC SEGFFLIGST TSRCEVQDRG VGWSHPLPQC EIVKCKPPPD 

       190        200        210        220        230        240 
IRNGRHSGEE NFYAYGFSVT YSCDPRFSLL GHASISCTVE NETIGVWRPS PPTCEKITCR 

       250        260        270        280        290        300 
KPDVSHGEMV SGFGPIYNYK DTIVFKCQKG FVLRGSSVIH CDADSKWNPS PPACEPNSCI 

       310        320        330        340        350        360 
NLPDIPHASW ETYPRPTKED VYVVGTVLRY RCHPGYKPTT DEPTTVICQK NLRWTPYQGC 

       370        380        390        400        410        420 
EALCCPEPKL NNGEITQHRK SRPANHCVYF YGDEISFSCH ETSRFSAICQ GDGTWSPRTP 

       430        440        450        460        470        480 
SCGDICNFPP KIAHGHYKQS SSYSFFKEEI IYECDKGYIL VGQAKLSCSY SHWSAPAPQC 

       490        500        510        520        530        540 
KALCRKPELV NGRLSVDKDQ YVEPENVTIQ CDSGYGVVGP QSITCSGNRT WYPEVPKCEW 

       550        560        570        580        590 
ETPEGCEQVL TGKRLMQCLP NPEDVKMALE VYKLSLEIEQ LELQRDSARQ STLDKEL

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the cDNA coding for proline-rich protein (PRP): identity of PRP as C4b-binding protein." Matsuguchi T., Okamura S., Aso T., Sata T., Niho Y. Biochem. Biophys. Res. Commun. 165:138-144(1989) [PubMed: 2590215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Genomic organization of the alpha chain of the human C4b-binding protein gene." Aso T., Okamura S., Matsuguchi T., Sakamoto N., Sata T., Niho Y. Biochem. Biophys. Res. Commun. 174:222-227(1991) [PubMed: 1989602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[4]	"Derivation of the sequence of the signal peptide in human C4b-binding protein and interspecies cross-hybridisation of the C4bp cDNA sequence." Lintin S.J., Lewin A.R., Reid K.B.M. FEBS Lett. 232:328-332(1988) [PubMed: 3378624] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-81.
[5]	"Studies on the structure of the human C4b-binding protein gene." Lintin S.J., Reid K.B.M. FEBS Lett. 204:77-81(1986) [PubMed: 3017751] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-288.
[6]	"Molecular cloning and characterization of the cDNA coding for C4b-binding protein, a regulatory protein of the classical pathway of the human complement system." Chung L.P., Bentley D.R., Reid K.B.M. Biochem. J. 230:133-141(1985) [PubMed: 3840370] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 80-597.
[7]	"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." Chung L.P., Gagnon J., Reid K.B.M. Mol. Immunol. 22:427-435(1985) [PubMed: 4033666] [Abstract] Cited for: PROTEIN SEQUENCE OF 49-88.
[8]	"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry." Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R. Proteomics 4:454-465(2004) [PubMed: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-506 AND ASN-528, MASS SPECTROMETRY. Tissue: Plasma.
[9]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221 AND ASN-506, MASS SPECTROMETRY. Tissue: Plasma.
[10]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221 AND ASN-506, MASS SPECTROMETRY. Tissue: Liver.
[11]	"Visualization of human C4b-binding protein and its complexes with vitamin K-dependent protein S and complement protein C4b." Dahlback B., Smith C.A., Mueller-Eberhard H.J. Proc. Natl. Acad. Sci. U.S.A. 80:3461-3465(1983) [PubMed: 6222381] [Abstract] Cited for: ELECTRON MICROSCOPY, 3D-STRUCTURE, LIGAND-BINDING.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M31452 mRNA. Translation: AAA36507.1.
M62486

M62485 Genomic DNA. Translation: AAA36506.1.
BC022312 mRNA. Translation: AAH22312.1.
X07853 mRNA. Translation: CAA30701.1.
X04284 Genomic DNA. Translation: CAB51244.1.
X04296 Genomic DNA. Translation: CAA27839.1.
X02865 mRNA. Translation: CAA26617.1.

IPI

IPI00021727.

PIR

NBHUC4. A33568.

RefSeq

NP_000706.1.

UniGene

Hs.1012

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A55	NMR	-	A	49-172	[»]

SMR

P04003. Positions 49-360, 111-423.

ModBase

Search...

Protein-protein interaction databases

IntAct

P04003. 1 interaction.

STRING

P04003.

Proteomic databases

PeptideAtlas

P04003.

PRIDE

P04003.

Genome annotation databases

Ensembl

ENST00000367070; ENSP00000356037; ENSG00000123838; Homo sapiens. [Genome view]

GeneID

722.

KEGG

hsa:722.

UCSC

uc001hfo.1. human.

Organism-specific databases

CTD

722.

GeneCards

GC01P205344.

H-InvDB

HIX0001537.

HGNC

HGNC:1325. C4BPA.

HPA

HPA000926.
HPA001578.

MIM

120830. gene.

PharmGKB

PA25905.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG125832.

HOVERGEN

P04003.

InParanoid

P04003.

OMA

TCSENRT.

OrthoDB

EOG9BP3X9.

PhylomeDB

P04003.

Gene expression databases

ArrayExpress

P04003.

Bgee

P04003.

CleanEx

HS_C4BPA.

Genevestigator

P04003.

GermOnline

ENSG00000123838. Homo sapiens.

Family and domain databases

InterPro

IPR016060. Complement_control_module.
IPR000436. Sushi_SCR_CCP.
[Graphical view]

Gene3D

G3DSA:2.10.70.10. Complement_control_module. 8 hits.

Pfam

PF00084. Sushi. 8 hits.
[Graphical view]

SMART

SM00032. CCP. 8 hits.
[Graphical view]

PROSITE

PS50923. SUSHI. 8 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

2938.

SOURCE

Search...

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Entry information

Entry name

C4BPA_HUMAN

Accession

Primary (citable) accession number: P04003

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 1986
Last sequence update:	October 1, 1993
Last modified:	January 19, 2010
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents