APOH_CANLF
ID APOH_CANLF Reviewed; 345 AA.
AC P33703;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Beagle; TISSUE=Liver;
RX PubMed=7682067; DOI=10.1006/bbrc.1993.1357;
RA Sellar G.C., Keane J., Mehdi H., Peeples M.E., Browne N., Whitehead A.S.;
RT "Characterization and acute phase modulation of canine apolipoprotein H
RT (beta 2-glycoprotein I).";
RL Biochem. Biophys. Res. Commun. 191:1288-1293(1993).
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; X72933; CAA51438.1; -; mRNA.
DR PIR; JN0465; JN0465.
DR RefSeq; NP_001003265.1; NM_001003265.2.
DR AlphaFoldDB; P33703; -.
DR SMR; P33703; -.
DR STRING; 9612.ENSCAFP00000016597; -.
DR PaxDb; P33703; -.
DR PRIDE; P33703; -.
DR Ensembl; ENSCAFT00040038309; ENSCAFP00040033406; ENSCAFG00040020697.
DR Ensembl; ENSCAFT00845049681; ENSCAFP00845038964; ENSCAFG00845028150.
DR GeneID; 403945; -.
DR KEGG; cfa:403945; -.
DR CTD; 350; -.
DR VEuPathDB; HostDB:ENSCAFG00845028150; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000157228; -.
DR HOGENOM; CLU_020107_2_0_1; -.
DR InParanoid; P33703; -.
DR OMA; TEDAECI; -.
DR OrthoDB; 784427at2759; -.
DR TreeFam; TF334137; -.
DR Reactome; R-CFA-114608; Platelet degranulation.
DR Proteomes; UP000002254; Chromosome 9.
DR Bgee; ENSCAFG00000011281; Expressed in liver and 27 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0042627; C:chylomicron; IEA:Ensembl.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0060230; F:lipoprotein lipase activator activity; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0030195; P:negative regulation of blood coagulation; IEA:Ensembl.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; IEA:Ensembl.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IEA:Ensembl.
DR GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0031639; P:plasminogen activation; IEA:Ensembl.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR CDD; cd00033; CCP; 4.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR015104; Sushi_2.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 4.
DR Pfam; PF09014; Sushi_2; 1.
DR SMART; SM00032; CCP; 4.
DR SUPFAM; SSF57535; SSF57535; 5.
DR PROSITE; PS50923; SUSHI; 4.
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:0000250"
FT CHAIN 20..345
FT /note="Beta-2-glycoprotein 1"
FT /id="PRO_0000002058"
FT DOMAIN 21..81
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 82..139
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 140..202
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 203..262
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 263..345
FT /note="Sushi-like"
FT CARBOHYD 33
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P17690"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 51..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 84..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 110..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 142..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 174..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 205..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 234..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 264..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 300..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 307..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ 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
