APOH_RAT
ID APOH_RAT Reviewed; 297 AA.
AC P26644;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Beta-2-glycoprotein 1;
DE AltName: Full=Apolipoprotein H;
DE Short=Apo-H;
DE AltName: Full=Beta-2-glycoprotein I;
DE Short=B2GPI;
DE Short=Beta(2)GPI;
DE Flags: Precursor;
GN Name=Apoh;
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;
RX PubMed=2771654; DOI=10.1093/nar/17.15.6401;
RA Aoyama Y., Chan Y.L., Wool I.G.;
RT "The primary structure of rat beta 2-glycoprotein I.";
RL Nucleic Acids Res. 17:6401-6401(1989).
CC -!- FUNCTION: Binds to various kinds of negatively charged substances such
CC as heparin, phospholipids, and dextran sulfate. May prevent activation
CC of the intrinsic blood coagulation cascade by binding to phospholipids
CC on the surface of damaged cells.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
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DR EMBL; X15551; CAA33556.1; -; mRNA.
DR PIR; S05310; NBRT.
DR AlphaFoldDB; P26644; -.
DR SMR; P26644; -.
DR IntAct; P26644; 1.
DR GlyGen; P26644; 5 sites.
DR iPTMnet; P26644; -.
DR PhosphoSitePlus; P26644; -.
DR PRIDE; P26644; -.
DR RGD; 1310625; Apoh.
DR InParanoid; P26644; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR PRO; PR:P26644; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0042627; C:chylomicron; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; IDA:RGD.
DR GO; GO:0060230; F:lipoprotein lipase activator activity; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IMP:RGD.
DR GO; GO:0007596; P:blood coagulation; IMP:RGD.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; ISO:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0030195; P:negative regulation of blood coagulation; ISO:RGD.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; ISO:RGD.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; ISO:RGD.
DR GO; GO:0060268; P:negative regulation of respiratory burst; IDA:RGD.
DR GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; ISO:RGD.
DR GO; GO:0031639; P:plasminogen activation; ISO:RGD.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; ISO:RGD.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:RGD.
DR GO; GO:0030193; P:regulation of blood coagulation; ISO:RGD.
DR GO; GO:0051917; P:regulation of fibrinolysis; ISO:RGD.
DR GO; GO:0034014; P:response to triglyceride; IEP:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR GO; GO:0034197; P:triglyceride transport; IDA:BHF-UCL.
DR CDD; cd00033; CCP; 3.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR015104; Sushi_2.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 3.
DR Pfam; PF09014; Sushi_2; 1.
DR SMART; SM00032; CCP; 3.
DR SUPFAM; SSF57535; SSF57535; 4.
DR PROSITE; PS50923; SUSHI; 3.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Heparin-binding; Reference proteome; Repeat;
KW Secreted; Signal; Sushi.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..297
FT /note="Beta-2-glycoprotein 1"
FT /id="PRO_0000002062"
FT DOMAIN 20..32
FT /note="Sushi 1; incomplete"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 34..91
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 92..154
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 155..214
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 215..297
FT /note="Sushi-like"
FT CARBOHYD 69
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 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 62..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 94..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 126..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 157..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 186..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 216..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 252..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 259..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 297 AA; 33197 MW; 911209DA6C119D59 CRC64;
MISPALIFFS AFLCHVAIAG RRMWPINTLK CTPRVCPFAG ILENGVVRYT TFEYPNTIGF
ACNPGYYLNG TSSSKCTEEG KWSPELPVCA RITCPPPPIP KFAALKEYKT SVGNSSFYQD
TVVFKCLPHF AMFGNDTVTC TAHGNWTQLP ECREVKCPFP SRPDNGFVNY PAKPVLSYKD
KAVFGCHETY KLDGPEEVEC TKTGNWSALP SCKASCKLSV KKATVLYQGQ RVKIQDQFKN
GMMHGDKVHF YCKNKEKKCS YTEEAQCIDG TIEIPKCFKE HSSLAFWKTD ASDVTPC
