ID   C4BPB_BOVIN             Reviewed;         198 AA.
AC   Q28066; Q2KIR2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=C4b-binding protein beta chain;
DE   Flags: Precursor;
GN   Name=C4BPB;
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   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7930621;
RA   Hillarp A., Thern A., Dahlbaech B.;
RT   "Bovine C4b binding protein. Molecular cloning of the alpha- and beta-
RT   chains provides structural background for lack of complex formation with
RT   protein S.";
RL   J. Immunol. 153:4190-4199(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Controls the classical pathway of complement activation. It
CC       binds as a cofactor to C3b/C4b inactivator (C3bINA), which then
CC       hydrolyzes the complement fragment C4b. It also accelerates the
CC       degradation of the C4bC2a complex (C3 convertase) by dissociating the
CC       complement fragment C2a. It also interacts with serum amyloid P
CC       component.
CC   -!- SUBUNIT: Disulfide-linked complex of alpha and beta chains.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   EMBL; Z31694; CAA83499.1; -; mRNA.
DR   EMBL; BC112543; AAI12544.1; -; mRNA.
DR   PIR; I46002; I46002.
DR   RefSeq; NP_776678.2; NM_174253.3.
DR   AlphaFoldDB; Q28066; -.
DR   SMR; Q28066; -.
DR   STRING; 9913.ENSBTAP00000023558; -.
DR   PaxDb; Q28066; -.
DR   PRIDE; Q28066; -.
DR   GeneID; 281652; -.
DR   KEGG; bta:281652; -.
DR   CTD; 725; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   InParanoid; Q28066; -.
DR   OrthoDB; 1110574at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IBA:GO_Central.
DR   CDD; cd00033; CCP; 1.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   Pfam; PF00084; Sushi; 1.
DR   SMART; SM00032; CCP; 2.
DR   SUPFAM; SSF57535; SSF57535; 2.
DR   PROSITE; PS50923; SUSHI; 1.
PE   2: Evidence at transcript level;
KW   Complement pathway; Disulfide bond; Glycoprotein; Immunity;
KW   Innate immunity; Reference proteome; Repeat; Secreted; Signal; Sushi.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..198
FT                   /note="C4b-binding protein beta chain"
FT                   /id="PRO_0000005891"
FT   DOMAIN          22..77
FT                   /note="Sushi 1; atypical; lacks a Cys"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          79..135
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        81..121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        107..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        161
FT                   /note="Interchain (with alpha chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   CONFLICT        108
FT                   /note="E -> Q (in Ref. 2; AAI12544)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="M -> T (in Ref. 2; AAI12544)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   198 AA;  22829 MW;  039BBF7A5D673A9D CRC64;
     MFFWLMCYLV DVWLISASDV GHCPDPLLVT DEFSSLEPVN VNDTFMFKCN EHCIFKGSNW
     SQCRENHTRV THSPVSKSRD CGPPETPTHG YFEGRDFKSG STITYYCEAR YRLVGTQHQQ
     CIDGEWTSAP PICELIQEAP KPAELELEKA FLAFQESKEL CKAIKKFTQR LKKSDLTMEK
     VKYSLERKKA KLKAKMLL