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Beta-2-glycoprotein 1 (Apolipoprotein H) (Apo-H) (Beta-2-glycoprotein I) (B2GPI) (Beta(2)GPI)

 APOH_CANLF              Reviewed;         345 AA.
P33703;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
12-SEP-2018, entry version 108.
RecName: Full=Beta-2-glycoprotein 1;
AltName: Full=Apolipoprotein H;
Short=Apo-H;
AltName: Full=Beta-2-glycoprotein I;
Short=B2GPI;
Short=Beta(2)GPI;
Flags: Precursor;
Name=APOH;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Beagle; TISSUE=Liver;
PubMed=7682067; DOI=10.1006/bbrc.1993.1357;
Sellar G.C., Keane J., Mehdi H., Peeples M.E., Browne N.,
Whitehead A.S.;
"Characterization and acute phase modulation of canine apolipoprotein
H (beta 2-glycoprotein I).";
Biochem. Biophys. Res. Commun. 191:1288-1293(1993).
-!- FUNCTION: Binds to various kinds of negatively charged substances
such as heparin, phospholipids, and dextran sulfate. May prevent
activation of the intrinsic blood coagulation cascade by binding
to phospholipids on the surface of damaged cells.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
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EMBL; X72933; CAA51438.1; -; mRNA.
PIR; JN0465; JN0465.
RefSeq; NP_001003265.1; NM_001003265.2.
UniGene; Cfa.3805; -.
ProteinModelPortal; P33703; -.
SMR; P33703; -.
STRING; 9615.ENSCAFP00000016597; -.
PaxDb; P33703; -.
PRIDE; P33703; -.
Ensembl; ENSCAFT00000017923; ENSCAFP00000016597; ENSCAFG00000011281.
GeneID; 403945; -.
KEGG; cfa:403945; -.
CTD; 350; -.
VGNC; VGNC:38004; APOH.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00910000143999; -.
HOGENOM; HOG000034008; -.
HOVERGEN; HBG004271; -.
InParanoid; P33703; -.
KO; K17305; -.
OMA; KNKEKKC; -.
OrthoDB; EOG091G0AFE; -.
TreeFam; TF334137; -.
Reactome; R-CFA-114608; Platelet degranulation.
Proteomes; UP000002254; Chromosome 9.
Bgee; ENSCAFG00000011281; Expressed in 3 organ(s), highest expression level in liver.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0042627; C:chylomicron; IEA:Ensembl.
GO; GO:0034364; C:high-density lipoprotein particle; IEA:Ensembl.
GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0060230; F:lipoprotein lipase activator activity; IEA:Ensembl.
GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
GO; GO:0007597; P:blood coagulation, intrinsic pathway; IEA:Ensembl.
GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
GO; GO:0030195; P:negative regulation of blood coagulation; IEA:Ensembl.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:0051918; P:negative regulation of fibrinolysis; IEA:Ensembl.
GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IEA:Ensembl.
GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0031639; P:plasminogen activation; IEA:Ensembl.
GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IEA:Ensembl.
GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
CDD; cd00033; CCP; 4.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR015104; Sushi_2.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00084; Sushi; 4.
Pfam; PF09014; Sushi_2; 1.
ProDom; PD012422; Sushi_2; 1.
SMART; SM00032; CCP; 4.
SUPFAM; SSF57535; SSF57535; 5.
PROSITE; PS50923; SUSHI; 4.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Heparin-binding;
Reference proteome; Repeat; Secreted; Signal; Sushi.
SIGNAL 1 19 {ECO:0000250}.
CHAIN 20 345 Beta-2-glycoprotein 1.
/FTId=PRO_0000002058.
DOMAIN 21 81 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 82 139 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 140 202 Sushi 3. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 203 262 Sushi 4. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 263 345 Sushi-like.
CARBOHYD 33 33 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:P17690}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 162 162 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 193 193 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 23 66 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 51 79 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 84 124 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 110 137 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 142 188 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 174 200 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 205 248 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 234 260 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 264 315 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 300 325 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 307 345 {ECO:0000255|PROSITE-ProRule:PRU00302}.
SEQUENCE 345 AA; 38403 MW; E0B2624879B74FEA CRC64;
MISLGLILFS SVLCHVATAG RTCPKPDDIP FATVVPLKTF YDPGEQIAYT CQPGYVFRGL
TRRFTCPLTG VWPTNTVRCI PRVCPFAGIL ENGAVRYTTF EYPNTISFAC NTGFYLNGSS
SAKCTEEGKW SVDLPVCTRV TCPPPSVPKF ATLSVFKPLA TNNSLYGNKA VFECLPHYAM
FGNDTITCTA HGNWTTLPEC REVKCPFPSR PDNGFVNYPA KQILYYKDKA MYGCHDTYTL
DGPEVVECNK FGNWSAQPSC KASCKLSVKK ATVLYQGERV KLQEKFKDGM LHGQKVSFYC
KNKEKKCSYT EDAECIDGTI EIPKCFKEHS SLAFWKTDAS DVKPC


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