ID APOH_HUMAN Reviewed; 345 AA. AC P02749; B2R9M3; Q9UCN7; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 3. DT 16-MAR-2016, entry version 186. DE RecName: Full=Beta-2-glycoprotein 1; DE AltName: Full=APC inhibitor; DE AltName: Full=Activated protein C-binding protein; DE AltName: Full=Anticardiolipin cofactor; 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; Synonyms=B2G1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=1650181; RA Steinkasserer A., Estaller C., Weiss E., Sim R.B., Day A.J.; RT "Complete nucleotide and deduced amino acid sequence of human beta 2- RT glycoprotein I."; RL Biochem. J. 277:387-391(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=1655523; DOI=10.1016/0014-5793(91)81065-G; RA Kristensen T., Schousboe I., Boel E., Mulvihill E.M., Hansen R.R., RA Moeller K.B., Moeller N.P.H., Sottrup-Jensen L.; RT "Molecular cloning and mammalian expression of human beta 2- RT glycoprotein I cDNA."; RL FEBS Lett. 289:183-186(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=1748314; DOI=10.1016/0378-1119(91)90449-L; RA Mehdi H., Nunn M., Steel D.M., Whitehead A.S., Perez M., Walker L., RA Peeples M.E.; RT "Nucleotide sequence and expression of the human gene encoding RT apolipoprotein H (beta 2-glycoprotein I)."; RL Gene 108:293-298(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1339416; DOI=10.1007/BF02591656; RA Day J.R., O'Hara P.J., Grant F.J., Lofton-Day C.E., Berkaw M.N., RA Werner P., Arnaud P.; RT "Molecular cloning and sequence analysis of the cDNA encoding human RT apolipoprotein H (beta 2-glycoprotein I)."; RL Int. J. Clin. Lab. Res. 21:256-263(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1777418; DOI=10.1093/intimm/3.12.1217; RA Matsuura E., Igarashi M., Igarashi Y., Nagae H., Ichikawa K., RA Yasuda T., Koike T.; RT "Molecular definition of human beta 2-glycoprotein I (beta 2-GPI) by RT cDNA cloning and inter-species differences of beta 2-GPI in RT alternation of anticardiolipin binding."; RL Int. Immunol. 3:1217-1221(1991). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9914524; DOI=10.1046/j.1432-1327.1999.00063.x; RA Okkels H., Rasmussen T.E., Sanghera D.K., Kamboh M.I., Kristensen T.; RT "Structure of the human beta2-glycoprotein I (apolipoprotein H) RT gene."; RL Eur. J. Biochem. 259:435-440(1999). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-107. RC TISSUE=Liver; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-107; HIS-154; RP LEU-266 AND SER-335. RG SeattleSNPs variation discovery resource; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP PROTEIN SEQUENCE OF 20-345, GLYCOSYLATION AT ASN-162; ASN-183; ASN-193 RP AND ASN-253, AND DISULFIDE BONDS. RX PubMed=6587378; DOI=10.1073/pnas.81.12.3640; RA Lozier J., Takahashi N., Putnam F.W.; RT "Complete amino acid sequence of human plasma beta 2-glycoprotein I."; RL Proc. Natl. Acad. Sci. U.S.A. 81:3640-3644(1984). RN [11] RP PROTEIN SEQUENCE OF 20-44. RX PubMed=1602135; RA Matsuura E., Igarashi Y., Fujimoto M., Ichikawa K., Suzuki T., RA Sumida T., Yasuda T., Koike T.; RT "Heterogeneity of anticardiolipin antibodies defined by the RT anticardiolipin cofactor."; RL J. Immunol. 148:3885-3891(1992). RN [12] RP PROTEIN SEQUENCE OF 20-43. RX PubMed=2349221; DOI=10.1073/pnas.87.11.4120; RA McNeil H.P., Simpson R.J., Chesterman C.N., Krilis S.A.; RT "Anti-phospholipid antibodies are directed against a complex antigen RT that includes a lipid-binding inhibitor of coagulation: beta 2- RT glycoprotein I (apolipoprotein H)."; RL Proc. Natl. Acad. Sci. U.S.A. 87:4120-4124(1990). RN [13] RP PROTEIN SEQUENCE OF 20-38. RC TISSUE=Ovarian follicular fluid; RX PubMed=11250549; DOI=10.1016/S1096-4959(00)00359-6; RA Aleporou-Marinou V., Pappa H., Yalouris P., Patargias T.; RT "Purification of apolipoprotein H (beta 2-glycoprotein I)-like protein RT from human follicular fluid."; RL Comp. Biochem. Physiol. 128B:537-542(2001). RN [14] RP DISULFIDE BONDS IN C-TERMINAL DOMAIN. RX PubMed=1426288; DOI=10.1016/0014-5793(92)81442-O; RA Steinkkasserer A., Barlow P.N., Willis A.C., Kertesz Z., RA Campbell I.D., Sim R.B., Norman D.G.; RT "Activity, disulphide mapping and structural modelling of the fifth RT domain of human beta 2-glycoprotein I."; RL FEBS Lett. 313:193-197(1992). RN [15] RP STRUCTURE OF CARBOHYDRATES. RX PubMed=9155091; DOI=10.1023/A:1026378825391; RA Gambino R., Ruiu G., Pagano G., Cassader M.; RT "Qualitative analysis of the carbohydrate composition of RT apolipoprotein H."; RL J. Protein Chem. 16:205-212(1997). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-253. RC TISSUE=Bile; RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200; RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; RT "A proteomic analysis of human bile."; RL Mol. Cell. Proteomics 3:715-728(2004). RN [17] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183 AND ASN-193. RC TISSUE=Plasma; RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183; ASN-193 AND RP ASN-253. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [19] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-253. RC TISSUE=Saliva; RX PubMed=16740002; DOI=10.1021/pr050492k; RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., RA Loo J.A.; RT "Identification of N-linked glycoproteins in human saliva by RT glycoprotein capture and mass spectrometry."; RL J. Proteome Res. 5:1493-1503(2006). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183; ASN-193 AND RP ASN-253. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [21] RP GLYCOSYLATION AT ASN-162. RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core RT fucosylated glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [22] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162, AND STRUCTURE OF RP CARBOHYDRATES. RC TISSUE=Cerebrospinal fluid; RX PubMed=19838169; DOI=10.1038/nmeth.1392; RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., RA Brinkmalm G., Larson G.; RT "Enrichment of glycopeptides for glycan structure and attachment site RT identification."; RL Nat. Methods 6:809-811(2009). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RC TISSUE=Plasma; RX PubMed=10508150; DOI=10.1093/emboj/18.19.5166; RA Bouma B., de Groot P.G., van Den Elsen J.M.H., Ravelli R.B.G., RA Schouten A., Simmelink M.J.A., Derksen R.H.W.M., Kroon J., Gros P.; RT "Adhesion mechanism of human beta(2)-glycoprotein I to phospholipids RT based on its crystal structure."; RL EMBO J. 18:5166-5174(1999). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS). RX PubMed=10562535; DOI=10.1093/emboj/18.22.6228; RA Schwarzenbacher R., Zeth K., Diederichs K., Gries A., Kostner G.M., RA Laggner P., Prassl R.; RT "Crystal structure of human beta2-glycoprotein I: implications for RT phospholipid binding and the antiphospholipid syndrome."; RL EMBO J. 18:6228-6239(1999). RN [27] RP VARIANT LEU-266. RX PubMed=8099061; DOI=10.1007/BF00217367; RA Steinkasserer A., Doerner C., Wuerzner R., Sim R.B.; RT "Human beta 2-glycoprotein I: molecular analysis of DNA and amino acid RT polymorphism."; RL Hum. Genet. 91:401-402(1993). RN [28] RP VARIANT ASN-107. RX PubMed=9225969; DOI=10.1007/s004390050465; RA Sanghera D.K., Kristensen T., Hamman R.F., Kamboh M.I.; RT "Molecular basis of the apolipoprotein H (beta 2-glycoprotein I) RT protein polymorphism."; RL Hum. Genet. 100:57-62(1997). RN [29] RP VARIANTS GLY-325 AND SER-335. RX PubMed=9063752; DOI=10.1093/hmg/6.2.311; RA Sanghera D.K., Wagenknecht D.R., McIntyre J.A., Kamboh M.I.; RT "Identification of structural mutations in the fifth domain of RT apolipoprotein H (beta-2-glycoprotein I) which affect phospholipid RT binding."; RL Hum. Mol. Genet. 6:311-316(1997). CC -!- FUNCTION: Binds to various kinds of negatively charged substances CC such as heparin, phospholipids, and dextran sulfate. May prevent CC activation of the intrinsic blood coagulation cascade by binding CC to phospholipids on the surface of damaged cells. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-2114682, EBI-2114682; CC P08519:LPA; NbExp=4; IntAct=EBI-2114682, EBI-9232288; CC P00747:PLG; NbExp=2; IntAct=EBI-2114682, EBI-999394; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- PTM: N- and O-glycosylated. PubMed:6587378 also reports CC glycosylation on 'Asn-188' for their allele. CC {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:6587378}. CC -!- SIMILARITY: Contains 4 Sushi (CCP/SCR) domains. CC {ECO:0000255|PROSITE-ProRule:PRU00302}. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/apoh/"; CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and CC polymorphism database; CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=APOH"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X58100; CAA41113.1; -; mRNA. DR EMBL; X53595; CAA37664.1; -; mRNA. DR EMBL; X57847; CAA40977.1; -; mRNA. DR EMBL; M62839; AAA51766.1; -; mRNA. DR EMBL; S80305; AAB21330.1; -; mRNA. DR EMBL; Y11493; CAA72279.1; -; Genomic_DNA. DR EMBL; Y11494; CAA72279.1; JOINED; Genomic_DNA. DR EMBL; Y11495; CAA72279.1; JOINED; Genomic_DNA. DR EMBL; X53595; CAA72279.1; JOINED; mRNA. DR EMBL; Y11496; CAA72279.1; JOINED; Genomic_DNA. DR EMBL; Y11497; CAA72279.1; JOINED; Genomic_DNA. DR EMBL; Y11498; CAA72279.1; JOINED; Genomic_DNA. DR EMBL; Y17754; CAA76845.1; -; Genomic_DNA. DR EMBL; AK313838; BAG36570.1; -; mRNA. DR EMBL; AY322156; AAP72014.1; -; Genomic_DNA. DR EMBL; BC020703; AAH20703.1; -; mRNA. DR EMBL; BC026283; AAH26283.1; -; mRNA. DR CCDS; CCDS11663.1; -. DR PIR; S17178; NBHU. DR RefSeq; NP_000033.2; NM_000042.2. DR UniGene; Hs.445358; -. DR PDB; 1C1Z; X-ray; 2.87 A; A=20-345. DR PDB; 1G4F; NMR; -; A=261-345. DR PDB; 1G4G; NMR; -; A=261-345. DR PDB; 1QUB; X-ray; 2.70 A; A=20-345. DR PDB; 2KRI; NMR; -; A=263-345. DR PDB; 3OP8; X-ray; 1.90 A; A/B=263-345. DR PDB; 4JHS; X-ray; 3.00 A; A=203-345. DR PDBsum; 1C1Z; -. DR PDBsum; 1G4F; -. DR PDBsum; 1G4G; -. DR PDBsum; 1QUB; -. DR PDBsum; 2KRI; -. DR PDBsum; 3OP8; -. DR PDBsum; 4JHS; -. DR ProteinModelPortal; P02749; -. DR SMR; P02749; 20-345. DR BioGrid; 106847; 12. DR DIP; DIP-46878N; -. DR IntAct; P02749; 10. DR MINT; MINT-6743724; -. DR STRING; 9606.ENSP00000205948; -. DR PhosphoSite; P02749; -. DR BioMuta; APOH; -. DR DMDM; 543826; -. DR MaxQB; P02749; -. DR PaxDb; P02749; -. DR PeptideAtlas; P02749; -. DR PRIDE; P02749; -. DR TopDownProteomics; P02749; -. DR DNASU; 350; -. DR Ensembl; ENST00000205948; ENSP00000205948; ENSG00000091583. DR GeneID; 350; -. DR KEGG; hsa:350; -. DR UCSC; uc002jfn.5; human. DR CTD; 350; -. DR GeneCards; APOH; -. DR HGNC; HGNC:616; APOH. DR HPA; CAB022214; -. DR HPA; HPA001654; -. DR HPA; HPA003732; -. DR MIM; 138700; gene. DR neXtProt; NX_P02749; -. DR PharmGKB; PA24903; -. DR eggNOG; KOG4297; Eukaryota. DR eggNOG; ENOG410XPJ1; LUCA. DR GeneTree; ENSGT00780000121907; -. DR HOGENOM; HOG000034008; -. DR HOVERGEN; HBG004271; -. DR InParanoid; P02749; -. DR KO; K17305; -. DR OMA; RFTCPLT; -. DR OrthoDB; EOG7K6PV8; -. DR PhylomeDB; P02749; -. DR TreeFam; TF334137; -. DR ChiTaRS; APOH; human. DR EvolutionaryTrace; P02749; -. DR GeneWiki; Apolipoprotein_H; -. DR GenomeRNAi; 350; -. DR NextBio; 1441; -. DR PMAP-CutDB; P02749; -. DR PRO; PR:P02749; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; P02749; -. DR CleanEx; HS_APOH; -. DR ExpressionAtlas; P02749; baseline and differential. DR Genevisible; P02749; HS. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0042627; C:chylomicron; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL. DR GO; GO:0001948; F:glycoprotein binding; IPI:BHF-UCL. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008289; F:lipid binding; IDA:BHF-UCL. DR GO; GO:0060230; F:lipoprotein lipase activator activity; IDA:BHF-UCL. DR GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IDA:BHF-UCL. DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:BHF-UCL. DR GO; GO:0030195; P:negative regulation of blood coagulation; IDA:BHF-UCL. DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IDA:BHF-UCL. DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:BHF-UCL. DR GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:BHF-UCL. DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IDA:BHF-UCL. DR GO; GO:0060268; P:negative regulation of respiratory burst; IEA:Ensembl. DR GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; IDA:BHF-UCL. DR GO; GO:0031100; P:organ regeneration; IEA:Ensembl. DR GO; GO:0031639; P:plasminogen activation; IDA:BHF-UCL. DR GO; GO:0030194; P:positive regulation of blood coagulation; TAS:BHF-UCL. DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:BHF-UCL. DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IEA:Ensembl. DR GO; GO:0051917; P:regulation of fibrinolysis; IDA:BHF-UCL. DR GO; GO:0034014; P:response to triglyceride; IEA:Ensembl. DR GO; GO:0006641; P:triglyceride metabolic process; IDA:BHF-UCL. DR GO; GO:0034197; P:triglyceride transport; ISS:BHF-UCL. DR InterPro; IPR015104; Sushi_2. DR InterPro; IPR000436; Sushi_SCR_CCP_dom. DR Pfam; PF00084; Sushi; 4. DR Pfam; PF09014; Sushi_2; 1. DR ProDom; PD012422; Sushi_2; 1. DR SMART; SM00032; CCP; 4. DR SUPFAM; SSF57535; SSF57535; 5. DR PROSITE; PS50923; SUSHI; 4. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Heparin-binding; Polymorphism; KW Reference proteome; Repeat; Secreted; Signal; Sushi. FT SIGNAL 1 19 {ECO:0000269|PubMed:11250549, FT ECO:0000269|PubMed:1602135, FT ECO:0000269|PubMed:2349221, FT ECO:0000269|PubMed:6587378}. FT CHAIN 20 345 Beta-2-glycoprotein 1. FT /FTId=PRO_0000002059. FT DOMAIN 21 81 Sushi 1. {ECO:0000255|PROSITE- FT ProRule:PRU00302}. FT DOMAIN 82 139 Sushi 2. {ECO:0000255|PROSITE- FT ProRule:PRU00302}. FT DOMAIN 140 202 Sushi 3. {ECO:0000255|PROSITE- FT ProRule:PRU00302}. FT DOMAIN 203 262 Sushi 4. {ECO:0000255|PROSITE- FT ProRule:PRU00302}. FT REGION 263 345 Sushi-like. FT CARBOHYD 33 33 O-linked (GalNAc...). FT {ECO:0000250|UniProtKB:P17690}. FT CARBOHYD 149 149 O-linked (GalNAc...). FT CARBOHYD 162 162 N-linked (GlcNAc...) (complex). FT {ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:15084671, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:16740002, FT ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19838169, FT ECO:0000269|PubMed:6587378}. FT CARBOHYD 183 183 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:6587378}. FT CARBOHYD 193 193 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:6587378}. FT CARBOHYD 253 253 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:15084671, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:16740002, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:6587378}. FT DISULFID 23 66 FT DISULFID 51 79 FT DISULFID 84 124 FT DISULFID 110 137 FT DISULFID 142 188 FT DISULFID 174 200 FT DISULFID 205 248 FT DISULFID 234 260 FT DISULFID 264 315 FT DISULFID 300 325 FT DISULFID 307 345 FT VARIANT 5 5 V -> A (in dbSNP:rs3826358). FT /FTId=VAR_048316. FT VARIANT 107 107 S -> N (in allele APOH*1; FT dbSNP:rs1801692). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9225969, FT ECO:0000269|Ref.8}. FT /FTId=VAR_008169. FT VARIANT 154 154 R -> H (in dbSNP:rs8178847). FT {ECO:0000269|Ref.8}. FT /FTId=VAR_019155. FT VARIANT 266 266 V -> L (in 23% of the population; FT dbSNP:rs4581). FT {ECO:0000269|PubMed:8099061, FT ECO:0000269|Ref.8}. FT /FTId=VAR_000673. FT VARIANT 325 325 C -> G (loss of phosphatidylserine- FT binding; dbSNP:rs1801689). FT {ECO:0000269|PubMed:9063752}. FT /FTId=VAR_008170. FT VARIANT 335 335 W -> S (in allele APOH*3W; loss of FT phosphatidylserine-binding; FT dbSNP:rs1801690). FT {ECO:0000269|PubMed:9063752, FT ECO:0000269|Ref.8}. FT /FTId=VAR_008171. FT CONFLICT 121 121 S -> C (in Ref. 10; AA sequence). FT {ECO:0000305}. FT CONFLICT 188 188 C -> N (in Ref. 10; AA sequence). FT {ECO:0000305}. FT STRAND 22 24 {ECO:0000244|PDB:1QUB}. FT STRAND 32 36 {ECO:0000244|PDB:1QUB}. FT STRAND 39 41 {ECO:0000244|PDB:1QUB}. FT STRAND 46 51 {ECO:0000244|PDB:1QUB}. FT STRAND 55 57 {ECO:0000244|PDB:1QUB}. FT STRAND 62 65 {ECO:0000244|PDB:1QUB}. FT STRAND 79 81 {ECO:0000244|PDB:1QUB}. FT STRAND 93 96 {ECO:0000244|PDB:1QUB}. FT STRAND 105 110 {ECO:0000244|PDB:1QUB}. FT STRAND 114 118 {ECO:0000244|PDB:1QUB}. FT STRAND 120 124 {ECO:0000244|PDB:1QUB}. FT STRAND 130 132 {ECO:0000244|PDB:1QUB}. FT STRAND 136 139 {ECO:0000244|PDB:1QUB}. FT STRAND 151 155 {ECO:0000244|PDB:1QUB}. FT STRAND 163 165 {ECO:0000244|PDB:1QUB}. FT STRAND 169 174 {ECO:0000244|PDB:1QUB}. FT STRAND 178 182 {ECO:0000244|PDB:1QUB}. FT STRAND 184 188 {ECO:0000244|PDB:1QUB}. FT STRAND 192 195 {ECO:0000244|PDB:1QUB}. FT STRAND 199 202 {ECO:0000244|PDB:1QUB}. FT STRAND 214 217 {ECO:0000244|PDB:1QUB}. FT STRAND 222 225 {ECO:0000244|PDB:1QUB}. FT STRAND 229 234 {ECO:0000244|PDB:1QUB}. FT STRAND 238 242 {ECO:0000244|PDB:1QUB}. FT STRAND 244 248 {ECO:0000244|PDB:1QUB}. FT STRAND 252 255 {ECO:0000244|PDB:1QUB}. FT STRAND 260 262 {ECO:0000244|PDB:1QUB}. FT STRAND 267 270 {ECO:0000244|PDB:3OP8}. FT STRAND 272 275 {ECO:0000244|PDB:3OP8}. FT STRAND 278 281 {ECO:0000244|PDB:3OP8}. FT HELIX 282 285 {ECO:0000244|PDB:3OP8}. FT TURN 286 288 {ECO:0000244|PDB:3OP8}. FT STRAND 295 302 {ECO:0000244|PDB:3OP8}. FT TURN 303 306 {ECO:0000244|PDB:3OP8}. FT STRAND 307 316 {ECO:0000244|PDB:3OP8}. FT TURN 331 333 {ECO:0000244|PDB:1C1Z}. FT HELIX 339 341 {ECO:0000244|PDB:3OP8}. SQ 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 //