C4BPA_RAT
ID C4BPA_RAT Reviewed; 558 AA.
AC Q63514;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=C4b-binding protein alpha chain;
DE Short=C4bp;
DE Flags: Precursor;
GN Name=C4bpa;
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. Alpha chain binds C4b. It interacts also with
CC anticoagulant protein S 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; Z50051; CAA90391.1; -; mRNA.
DR PIR; S57953; S57953.
DR AlphaFoldDB; Q63514; -.
DR SMR; Q63514; -.
DR STRING; 10116.ENSRNOP00000005461; -.
DR CarbonylDB; Q63514; -.
DR GlyGen; Q63514; 5 sites.
DR PaxDb; Q63514; -.
DR PeptideAtlas; Q63514; -.
DR PRIDE; Q63514; -.
DR UCSC; RGD:2235; rat.
DR RGD; 2235; C4bpa.
DR eggNOG; ENOG502SHRK; Eukaryota.
DR InParanoid; Q63514; -.
DR PRO; PR:Q63514; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043159; C:acrosomal matrix; ISO:RGD.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0002081; C:outer acrosomal membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0002199; C:zona pellucida receptor complex; ISO:RGD.
DR GO; GO:0001848; F:complement binding; TAS:RGD.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISO:RGD.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; TAS:RGD.
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 GO; GO:0007338; P:single fertilization; ISO:RGD.
DR CDD; cd00033; CCP; 8.
DR InterPro; IPR040514; C4bp_oligo.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF18453; C4bp_oligo; 1.
DR Pfam; PF00084; Sushi; 8.
DR SMART; SM00032; CCP; 8.
DR SUPFAM; SSF57535; SSF57535; 8.
DR PROSITE; PS50923; SUSHI; 8.
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..13
FT /evidence="ECO:0000250"
FT CHAIN 14..558
FT /note="C4b-binding protein alpha chain"
FT /id="PRO_0000005890"
FT DOMAIN 14..74
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 75..136
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 137..201
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 202..260
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 261..326
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 327..388
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 389..445
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 446..503
FT /note="Sushi 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 15..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 45..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 77..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 104..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 139..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 168..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 204..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 232..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 263..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 296..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 329..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 363..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 390..431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 417..443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 447..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 474..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 509
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 521
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 558 AA; 62266 MW; 592F0C667ED1E5FF CRC64;
MSLTAALWVA VFGKCGPPPD LPYALPASEM NQTDFESHTT LRYNCRPGYS RASSSQSLYC
KPLGKWQINI ACVKKSCRNP GDLQNGKVEV KTDFLFGSQI EFSCSEGYIL IGSSTSYCEI
QGKGVSWSDP LPECVIAKCG MPPDISNGKH NGREEEFFTY RSSVTYKCDP DFTLLGNASI
TCTVVNKTVG VWSPSPPTCE RIICPWPKVL HGTINSGFKH TYKYKDSVRF VCQKGFVLRG
SGVIHCEADG SWSPVPVCEL NSCTDIPDIP NAALITSPRP RKEDVYPVGT VLRYICRPGY
EPATRQPMTV ICQKDLSWSM LRGCKEICCP VPDPKSVRVI QHEKAHPDND CTYFFGDEVS
YTCQNDIMLT ATCKSDGTWH PRTPSCHQSC DFPPAIAHGR YTKSSSYYVR TQVTYECEEG
YRLVGEATIS CWYSQWTPAA PQCKALCRKP EIGNGVLSTN KDQYVETENV TIQCDSGFVM
LGSQSITCSE NGTWYPKVSR CEQEVPKDCE HVFAGKKLMQ CLPNSNDVKM ALEVYKLTLE
IKQLQLQIDK AKHVDREL
