ID   C4BPB_RAT               Reviewed;         258 AA.
AC   Q63515;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=C4b-binding protein beta chain;
DE   Flags: Precursor;
GN   Name=C4bpb;
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; TISSUE=Liver;
RX   PubMed=9013975;
RA   Hillarp A., Wiklund H., Thern A., Dahlback B.;
RT   "Molecular cloning of rat C4b binding protein alpha- and beta-chains:
RT   structural and functional relationships among human, bovine, rabbit, mouse,
RT   and rat proteins.";
RL   J. Immunol. 158:1315-1323(1997).
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 interacts also with anticoagulant protein S
CC       and with serum amyloid P component.
CC   -!- SUBUNIT: Disulfide-linked complex of alpha and beta chains.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   EMBL; Z50052; CAA90392.1; -; mRNA.
DR   PIR; S57960; S57960.
DR   AlphaFoldDB; Q63515; -.
DR   SMR; Q63515; -.
DR   STRING; 10116.ENSRNOP00000005505; -.
DR   GlyGen; Q63515; 6 sites.
DR   PaxDb; Q63515; -.
DR   PRIDE; Q63515; -.
DR   UCSC; RGD:2236; rat.
DR   RGD; 2236; C4bpb.
DR   eggNOG; KOG4297; Eukaryota.
DR   InParanoid; Q63515; -.
DR   PhylomeDB; Q63515; -.
DR   PRO; PR:Q63515; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
DR   GO; GO:1903027; P:regulation of opsonization; ISO:RGD.
DR   GO; GO:0009609; P:response to symbiotic bacterium; ISO:RGD.
DR   CDD; cd00033; CCP; 3.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   Pfam; PF00084; Sushi; 2.
DR   SMART; SM00032; CCP; 3.
DR   SUPFAM; SSF57535; SSF57535; 3.
DR   PROSITE; PS50923; SUSHI; 3.
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..15
FT                   /evidence="ECO:0000250"
FT   CHAIN           16..258
FT                   /note="C4b-binding protein beta chain"
FT                   /id="PRO_0000005893"
FT   DOMAIN          18..75
FT                   /note="Sushi 1; atypical; lacks a Cys"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          76..133
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          134..190
FT                   /note="Sushi 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        78..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        104..131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        136..176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        162..188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        217
FT                   /note="Interchain (with alpha chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   258 AA;  28642 MW;  636F99908A85DC1C CRC64;
     MLCLVVCCLI WLISALDGSC SEPPPVNNSV FVGKETEEQI LGIYLCIKGY HLVGKKSLVF
     DPSKEWNSTL PECLLGHCPD PVLENGKINS SGPVNISGKI MFECNDGYIL KGSNWSQCLE
     DHTWAPPLPI CRSRDCEPPE TPVHGYFEGE TFTSGSVVTY YCEDGYHLVG TQKVQCSDGE
     WSPSYPTCES IQEPPKSAEQ SALEKAILAF QESKDLCNAT ENFVRQLREG GITMEELKCS
     LEMKKTKLKS DILLNYHS