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Beta-2-glycoprotein 1 (APC inhibitor) (Activated protein C-binding protein) (Anticardiolipin cofactor) (Apolipoprotein H) (Apo-H) (Beta-2-glycoprotein I) (B2GPI) (Beta(2)GPI)

 APOH_HUMAN              Reviewed;         345 AA.
P02749; B2R9M3; Q9UCN7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 3.
20-JUN-2018, entry version 206.
RecName: Full=Beta-2-glycoprotein 1;
AltName: Full=APC inhibitor;
AltName: Full=Activated protein C-binding protein;
AltName: Full=Anticardiolipin cofactor;
AltName: Full=Apolipoprotein H;
Short=Apo-H;
AltName: Full=Beta-2-glycoprotein I;
Short=B2GPI;
Short=Beta(2)GPI;
Flags: Precursor;
Name=APOH; Synonyms=B2G1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1650181; DOI=10.1042/bj2770387;
Steinkasserer A., Estaller C., Weiss E., Sim R.B., Day A.J.;
"Complete nucleotide and deduced amino acid sequence of human beta 2-
glycoprotein I.";
Biochem. J. 277:387-391(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1655523; DOI=10.1016/0014-5793(91)81065-G;
Kristensen T., Schousboe I., Boel E., Mulvihill E.M., Hansen R.R.,
Moeller K.B., Moeller N.P.H., Sottrup-Jensen L.;
"Molecular cloning and mammalian expression of human beta 2-
glycoprotein I cDNA.";
FEBS Lett. 289:183-186(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1748314; DOI=10.1016/0378-1119(91)90449-L;
Mehdi H., Nunn M., Steel D.M., Whitehead A.S., Perez M., Walker L.,
Peeples M.E.;
"Nucleotide sequence and expression of the human gene encoding
apolipoprotein H (beta 2-glycoprotein I).";
Gene 108:293-298(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1339416; DOI=10.1007/BF02591656;
Day J.R., O'Hara P.J., Grant F.J., Lofton-Day C.E., Berkaw M.N.,
Werner P., Arnaud P.;
"Molecular cloning and sequence analysis of the cDNA encoding human
apolipoprotein H (beta 2-glycoprotein I).";
Int. J. Clin. Lab. Res. 21:256-263(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1777418; DOI=10.1093/intimm/3.12.1217;
Matsuura E., Igarashi M., Igarashi Y., Nagae H., Ichikawa K.,
Yasuda T., Koike T.;
"Molecular definition of human beta 2-glycoprotein I (beta 2-GPI) by
cDNA cloning and inter-species differences of beta 2-GPI in
alternation of anticardiolipin binding.";
Int. Immunol. 3:1217-1221(1991).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9914524; DOI=10.1046/j.1432-1327.1999.00063.x;
Okkels H., Rasmussen T.E., Sanghera D.K., Kamboh M.I., Kristensen T.;
"Structure of the human beta2-glycoprotein I (apolipoprotein H)
gene.";
Eur. J. Biochem. 259:435-440(1999).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-107.
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-107; HIS-154;
LEU-266 AND SER-335.
SeattleSNPs variation discovery resource;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 20-345, GLYCOSYLATION AT ASN-162; ASN-183; ASN-193
AND ASN-253, AND DISULFIDE BONDS.
PubMed=6587378; DOI=10.1073/pnas.81.12.3640;
Lozier J., Takahashi N., Putnam F.W.;
"Complete amino acid sequence of human plasma beta 2-glycoprotein I.";
Proc. Natl. Acad. Sci. U.S.A. 81:3640-3644(1984).
[11]
PROTEIN SEQUENCE OF 20-44.
PubMed=1602135;
Matsuura E., Igarashi Y., Fujimoto M., Ichikawa K., Suzuki T.,
Sumida T., Yasuda T., Koike T.;
"Heterogeneity of anticardiolipin antibodies defined by the
anticardiolipin cofactor.";
J. Immunol. 148:3885-3891(1992).
[12]
PROTEIN SEQUENCE OF 20-43.
PubMed=2349221; DOI=10.1073/pnas.87.11.4120;
McNeil H.P., Simpson R.J., Chesterman C.N., Krilis S.A.;
"Anti-phospholipid antibodies are directed against a complex antigen
that includes a lipid-binding inhibitor of coagulation: beta 2-
glycoprotein I (apolipoprotein H).";
Proc. Natl. Acad. Sci. U.S.A. 87:4120-4124(1990).
[13]
PROTEIN SEQUENCE OF 20-38.
TISSUE=Ovarian follicular fluid;
PubMed=11250549; DOI=10.1016/S1096-4959(00)00359-6;
Aleporou-Marinou V., Pappa H., Yalouris P., Patargias T.;
"Purification of apolipoprotein H (beta 2-glycoprotein I)-like protein
from human follicular fluid.";
Comp. Biochem. Physiol. 128B:537-542(2001).
[14]
DISULFIDE BONDS IN C-TERMINAL DOMAIN.
PubMed=1426288; DOI=10.1016/0014-5793(92)81442-O;
Steinkkasserer A., Barlow P.N., Willis A.C., Kertesz Z.,
Campbell I.D., Sim R.B., Norman D.G.;
"Activity, disulphide mapping and structural modelling of the fifth
domain of human beta 2-glycoprotein I.";
FEBS Lett. 313:193-197(1992).
[15]
STRUCTURE OF CARBOHYDRATES.
PubMed=9155091; DOI=10.1023/A:1026378825391;
Gambino R., Ruiu G., Pagano G., Cassader M.;
"Qualitative analysis of the carbohydrate composition of
apolipoprotein H.";
J. Protein Chem. 16:205-212(1997).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-253.
TISSUE=Bile;
PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
"A proteomic analysis of human bile.";
Mol. Cell. Proteomics 3:715-728(2004).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183 AND ASN-193.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183; ASN-193 AND
ASN-253.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-253.
TISSUE=Saliva;
PubMed=16740002; DOI=10.1021/pr050492k;
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
Loo J.A.;
"Identification of N-linked glycoproteins in human saliva by
glycoprotein capture and mass spectrometry.";
J. Proteome Res. 5:1493-1503(2006).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183; ASN-193 AND
ASN-253.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[21]
GLYCOSYLATION AT ASN-162.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162, AND STRUCTURE OF
CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
TISSUE=Plasma;
PubMed=10508150; DOI=10.1093/emboj/18.19.5166;
Bouma B., de Groot P.G., van Den Elsen J.M.H., Ravelli R.B.G.,
Schouten A., Simmelink M.J.A., Derksen R.H.W.M., Kroon J., Gros P.;
"Adhesion mechanism of human beta(2)-glycoprotein I to phospholipids
based on its crystal structure.";
EMBO J. 18:5166-5174(1999).
[26]
X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS).
PubMed=10562535; DOI=10.1093/emboj/18.22.6228;
Schwarzenbacher R., Zeth K., Diederichs K., Gries A., Kostner G.M.,
Laggner P., Prassl R.;
"Crystal structure of human beta2-glycoprotein I: implications for
phospholipid binding and the antiphospholipid syndrome.";
EMBO J. 18:6228-6239(1999).
[27]
VARIANT LEU-266.
PubMed=8099061; DOI=10.1007/BF00217367;
Steinkasserer A., Doerner C., Wuerzner R., Sim R.B.;
"Human beta 2-glycoprotein I: molecular analysis of DNA and amino acid
polymorphism.";
Hum. Genet. 91:401-402(1993).
[28]
VARIANT ASN-107.
PubMed=9225969; DOI=10.1007/s004390050465;
Sanghera D.K., Kristensen T., Hamman R.F., Kamboh M.I.;
"Molecular basis of the apolipoprotein H (beta 2-glycoprotein I)
protein polymorphism.";
Hum. Genet. 100:57-62(1997).
[29]
VARIANTS GLY-325 AND SER-335.
PubMed=9063752; DOI=10.1093/hmg/6.2.311;
Sanghera D.K., Wagenknecht D.R., McIntyre J.A., Kamboh M.I.;
"Identification of structural mutations in the fifth domain of
apolipoprotein H (beta-2-glycoprotein I) which affect phospholipid
binding.";
Hum. Mol. Genet. 6:311-316(1997).
-!- 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.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-2114682, EBI-2114682;
P01130:LDLR; NbExp=3; IntAct=EBI-2114682, EBI-988319;
P08519:LPA; NbExp=4; IntAct=EBI-2114682, EBI-9232288;
Q924X6:Lrp8 (xeno); NbExp=2; IntAct=EBI-2114682, EBI-432319;
P02776:PF4; NbExp=2; IntAct=EBI-2114682, EBI-2565740;
P00747:PLG; NbExp=2; IntAct=EBI-2114682, EBI-999394;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- PTM: N- and O-glycosylated. PubMed:6587378 also reports
glycosylation on 'Asn-188' for their allele.
{ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:6587378}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/apoh/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=APOH";
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EMBL; X58100; CAA41113.1; -; mRNA.
EMBL; X53595; CAA37664.1; -; mRNA.
EMBL; X57847; CAA40977.1; -; mRNA.
EMBL; M62839; AAA51766.1; -; mRNA.
EMBL; S80305; AAB21330.1; -; mRNA.
EMBL; Y11493; CAA72279.1; -; Genomic_DNA.
EMBL; Y11494; CAA72279.1; JOINED; Genomic_DNA.
EMBL; Y11495; CAA72279.1; JOINED; Genomic_DNA.
EMBL; X53595; CAA72279.1; JOINED; mRNA.
EMBL; Y11496; CAA72279.1; JOINED; Genomic_DNA.
EMBL; Y11497; CAA72279.1; JOINED; Genomic_DNA.
EMBL; Y11498; CAA72279.1; JOINED; Genomic_DNA.
EMBL; Y17754; CAA76845.1; -; Genomic_DNA.
EMBL; AK313838; BAG36570.1; -; mRNA.
EMBL; AY322156; AAP72014.1; -; Genomic_DNA.
EMBL; BC020703; AAH20703.1; -; mRNA.
EMBL; BC026283; AAH26283.1; -; mRNA.
CCDS; CCDS11663.1; -.
PIR; S17178; NBHU.
RefSeq; NP_000033.2; NM_000042.2.
UniGene; Hs.445358; -.
PDB; 1C1Z; X-ray; 2.87 A; A=20-345.
PDB; 1G4F; NMR; -; A=261-345.
PDB; 1G4G; NMR; -; A=261-345.
PDB; 1QUB; X-ray; 2.70 A; A=20-345.
PDB; 2KRI; NMR; -; A=263-345.
PDB; 3OP8; X-ray; 1.90 A; A/B=263-345.
PDB; 4JHS; X-ray; 3.00 A; A=203-345.
PDBsum; 1C1Z; -.
PDBsum; 1G4F; -.
PDBsum; 1G4G; -.
PDBsum; 1QUB; -.
PDBsum; 2KRI; -.
PDBsum; 3OP8; -.
PDBsum; 4JHS; -.
ProteinModelPortal; P02749; -.
SMR; P02749; -.
BioGrid; 106847; 13.
DIP; DIP-46878N; -.
IntAct; P02749; 15.
MINT; P02749; -.
STRING; 9606.ENSP00000205948; -.
DrugBank; DB05446; LJP 1082.
GlyConnect; 678; -.
iPTMnet; P02749; -.
PhosphoSitePlus; P02749; -.
BioMuta; APOH; -.
DMDM; 543826; -.
MaxQB; P02749; -.
PaxDb; P02749; -.
PeptideAtlas; P02749; -.
PRIDE; P02749; -.
ProteomicsDB; 51565; -.
TopDownProteomics; P02749; -.
DNASU; 350; -.
Ensembl; ENST00000205948; ENSP00000205948; ENSG00000091583.
GeneID; 350; -.
KEGG; hsa:350; -.
UCSC; uc002jfn.5; human.
CTD; 350; -.
DisGeNET; 350; -.
EuPathDB; HostDB:ENSG00000091583.10; -.
GeneCards; APOH; -.
HGNC; HGNC:616; APOH.
HPA; CAB022214; -.
HPA; HPA001654; -.
HPA; HPA003732; -.
MIM; 138700; gene.
neXtProt; NX_P02749; -.
OpenTargets; ENSG00000091583; -.
PharmGKB; PA24903; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00910000143999; -.
HOGENOM; HOG000034008; -.
HOVERGEN; HBG004271; -.
InParanoid; P02749; -.
KO; K17305; -.
OMA; KNKEKKC; -.
OrthoDB; EOG091G0AFE; -.
PhylomeDB; P02749; -.
TreeFam; TF334137; -.
Reactome; R-HSA-114608; Platelet degranulation.
ChiTaRS; APOH; human.
EvolutionaryTrace; P02749; -.
GeneWiki; Apolipoprotein_H; -.
GenomeRNAi; 350; -.
PMAP-CutDB; P02749; -.
PRO; PR:P02749; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000091583; -.
CleanEx; HS_APOH; -.
ExpressionAtlas; P02749; baseline and differential.
Genevisible; P02749; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0042627; C:chylomicron; IDA:BHF-UCL.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0031089; C:platelet dense granule lumen; TAS:Reactome.
GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008289; F:lipid binding; IDA:BHF-UCL.
GO; GO:0060230; F:lipoprotein lipase activator activity; IDA:BHF-UCL.
GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
GO; GO:0007597; P:blood coagulation, intrinsic pathway; IDA:BHF-UCL.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:BHF-UCL.
GO; GO:0030195; P:negative regulation of blood coagulation; IDA:BHF-UCL.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IDA:BHF-UCL.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:BHF-UCL.
GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:BHF-UCL.
GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IDA:BHF-UCL.
GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; IDA:BHF-UCL.
GO; GO:0031639; P:plasminogen activation; IDA:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0030194; P:positive regulation of blood coagulation; TAS:BHF-UCL.
GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:BHF-UCL.
GO; GO:0051917; P:regulation of fibrinolysis; IDA:BHF-UCL.
GO; GO:0006641; P:triglyceride metabolic process; IDA:BHF-UCL.
GO; GO:0034197; P:triglyceride transport; ISS:BHF-UCL.
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.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Heparin-binding; Polymorphism;
Reference proteome; Repeat; Secreted; Signal; Sushi.
SIGNAL 1 19 {ECO:0000269|PubMed:11250549,
ECO:0000269|PubMed:1602135,
ECO:0000269|PubMed:2349221,
ECO:0000269|PubMed:6587378}.
CHAIN 20 345 Beta-2-glycoprotein 1.
/FTId=PRO_0000002059.
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 149 149 O-linked (GalNAc...) threonine.
CARBOHYD 162 162 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:6587378}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:6587378}.
CARBOHYD 193 193 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:6587378}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:6587378}.
DISULFID 23 66
DISULFID 51 79
DISULFID 84 124
DISULFID 110 137
DISULFID 142 188
DISULFID 174 200
DISULFID 205 248
DISULFID 234 260
DISULFID 264 315
DISULFID 300 325
DISULFID 307 345
VARIANT 5 5 V -> A (in dbSNP:rs3826358).
/FTId=VAR_048316.
VARIANT 107 107 S -> N (in allele APOH*1;
dbSNP:rs1801692).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:9225969,
ECO:0000269|Ref.8}.
/FTId=VAR_008169.
VARIANT 154 154 R -> H (in dbSNP:rs8178847).
{ECO:0000269|Ref.8}.
/FTId=VAR_019155.
VARIANT 266 266 V -> L (in 23% of the population;
dbSNP:rs4581).
{ECO:0000269|PubMed:8099061,
ECO:0000269|Ref.8}.
/FTId=VAR_000673.
VARIANT 325 325 C -> G (loss of phosphatidylserine-
binding; dbSNP:rs1801689).
{ECO:0000269|PubMed:9063752}.
/FTId=VAR_008170.
VARIANT 335 335 W -> S (in allele APOH*3W; loss of
phosphatidylserine-binding;
dbSNP:rs1801690).
{ECO:0000269|PubMed:9063752,
ECO:0000269|Ref.8}.
/FTId=VAR_008171.
CONFLICT 121 121 S -> C (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 188 188 C -> N (in Ref. 10; AA sequence).
{ECO:0000305}.
STRAND 22 24 {ECO:0000244|PDB:1QUB}.
STRAND 32 36 {ECO:0000244|PDB:1QUB}.
STRAND 39 41 {ECO:0000244|PDB:1QUB}.
STRAND 46 51 {ECO:0000244|PDB:1QUB}.
STRAND 55 57 {ECO:0000244|PDB:1QUB}.
STRAND 62 65 {ECO:0000244|PDB:1QUB}.
STRAND 79 81 {ECO:0000244|PDB:1QUB}.
STRAND 93 96 {ECO:0000244|PDB:1QUB}.
STRAND 105 110 {ECO:0000244|PDB:1QUB}.
STRAND 114 118 {ECO:0000244|PDB:1QUB}.
STRAND 120 124 {ECO:0000244|PDB:1QUB}.
STRAND 130 132 {ECO:0000244|PDB:1QUB}.
STRAND 136 139 {ECO:0000244|PDB:1QUB}.
STRAND 151 155 {ECO:0000244|PDB:1QUB}.
STRAND 163 165 {ECO:0000244|PDB:1QUB}.
STRAND 169 174 {ECO:0000244|PDB:1QUB}.
STRAND 178 182 {ECO:0000244|PDB:1QUB}.
STRAND 184 188 {ECO:0000244|PDB:1QUB}.
STRAND 192 195 {ECO:0000244|PDB:1QUB}.
STRAND 199 202 {ECO:0000244|PDB:1QUB}.
STRAND 214 217 {ECO:0000244|PDB:1QUB}.
STRAND 222 225 {ECO:0000244|PDB:1QUB}.
STRAND 229 234 {ECO:0000244|PDB:1QUB}.
STRAND 238 242 {ECO:0000244|PDB:1QUB}.
STRAND 244 248 {ECO:0000244|PDB:1QUB}.
STRAND 252 255 {ECO:0000244|PDB:1QUB}.
STRAND 260 262 {ECO:0000244|PDB:1QUB}.
STRAND 267 270 {ECO:0000244|PDB:3OP8}.
STRAND 272 275 {ECO:0000244|PDB:3OP8}.
STRAND 278 281 {ECO:0000244|PDB:3OP8}.
HELIX 282 285 {ECO:0000244|PDB:3OP8}.
TURN 286 288 {ECO:0000244|PDB:3OP8}.
STRAND 295 302 {ECO:0000244|PDB:3OP8}.
TURN 303 306 {ECO:0000244|PDB:3OP8}.
STRAND 307 316 {ECO:0000244|PDB:3OP8}.
TURN 331 333 {ECO:0000244|PDB:1C1Z}.
HELIX 339 341 {ECO:0000244|PDB:3OP8}.
SEQUENCE 345 AA; 38298 MW; 63101704F8EDFE3F CRC64;
MISPVLILFS SFLCHVAIAG RTCPKPDDLP FSTVVPLKTF YEPGEEITYS CKPGYVSRGG
MRKFICPLTG LWPINTLKCT PRVCPFAGIL ENGAVRYTTF EYPNTISFSC NTGFYLNGAD
SAKCTEEGKW SPELPVCAPI ICPPPSIPTF ATLRVYKPSA GNNSLYRDTA VFECLPQHAM
FGNDTITCTT HGNWTKLPEC REVKCPFPSR PDNGFVNYPA KPTLYYKDKA TFGCHDGYSL
DGPEEIECTK LGNWSAMPSC KASCKVPVKK ATVVYQGERV KIQEKFKNGM LHGDKVSFFC
KNKEKKCSYT EDAQCIDGTI EVPKCFKEHS SLAFWKTDAS DVKPC


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