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 24-JAN-2024, entry version 240. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=1650181; DOI=10.1042/bj2770387; 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-glycoprotein I RT 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., Werner P., RA 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., Yasuda T., RA Koike T.; RT "Molecular definition of human beta 2-glycoprotein I (beta 2-GPI) by cDNA RT cloning and inter-species differences of beta 2-GPI in alternation of RT 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) 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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; LEU-266 RP 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 project: RT 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 AND RP 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., Sumida T., RA Yasuda T., Koike T.; RT "Heterogeneity of anticardiolipin antibodies defined by the anticardiolipin RT 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 that RT includes a lipid-binding inhibitor of coagulation: beta 2-glycoprotein I RT (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 from RT 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., Campbell I.D., RA Sim R.B., Norman D.G.; RT "Activity, disulphide mapping and structural modelling of the fifth domain RT 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 apolipoprotein RT 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., Thuluvath P.J., RA 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., Moore R.J., RA 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., Loo J.A.; RT "Identification of N-linked glycoproteins in human saliva by glycoprotein RT 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 multiple RT 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., Zheng Z.B., RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., RA Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core fucosylated RT 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., Brinkmalm G., RA 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., Buerckstuemmer T., RA 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT 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., Schouten A., RA Simmelink M.J.A., Derksen R.H.W.M., Kroon J., Gros P.; RT "Adhesion mechanism of human beta(2)-glycoprotein I to phospholipids based RT 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) protein RT 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 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 -!- INTERACTION: CC P02749; P02749: APOH; NbExp=2; IntAct=EBI-2114682, EBI-2114682; CC P02749; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2114682, EBI-21591415; CC P02749; P01130: LDLR; NbExp=3; IntAct=EBI-2114682, EBI-988319; CC P02749; P08519: LPA; NbExp=4; IntAct=EBI-2114682, EBI-9232288; CC P02749; P11226: MBL2; NbExp=3; IntAct=EBI-2114682, EBI-5325353; CC P02749; P02776: PF4; NbExp=2; IntAct=EBI-2114682, EBI-2565740; CC P02749; P00747: PLG; NbExp=2; IntAct=EBI-2114682, EBI-999394; CC P02749; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-2114682, EBI-2623095; CC P02749; Q924X6: Lrp8; Xeno; NbExp=2; IntAct=EBI-2114682, EBI-432319; CC PRO_0000002059; PRO_0000002059 [P02749]: APOH; NbExp=2; IntAct=EBI-11809989, EBI-11809989; CC PRO_0000002059; PRO_0000005068 [P02776]: PF4; NbExp=4; IntAct=EBI-11809989, EBI-11809981; 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 glycosylation CC on 'Asn-188' for their allele. {ECO:0000269|PubMed:14760718, CC ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, CC ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490, CC ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, CC ECO:0000269|PubMed:6587378}. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/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 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 PDB; 6V06; X-ray; 2.40 A; A=20-345. DR PDB; 6V08; X-ray; 2.58 A; A=20-345. DR PDB; 6V09; X-ray; 2.99 A; A=20-345. DR PDB; 6XSD; X-ray; 2.54 A; A=20-345. DR PDB; 6XST; X-ray; 2.92 A; A=20-345. DR PDB; 7JIK; X-ray; 2.69 A; A=20-345. DR PDB; 7KG4; X-ray; 3.30 A; A/B=20-345. DR PDBsum; 1C1Z; -. DR PDBsum; 1G4F; -. DR PDBsum; 1G4G; -. DR PDBsum; 1QUB; -. DR PDBsum; 2KRI; -. DR PDBsum; 3OP8; -. DR PDBsum; 4JHS; -. DR PDBsum; 6V06; -. DR PDBsum; 6V08; -. DR PDBsum; 6V09; -. DR PDBsum; 6XSD; -. DR PDBsum; 6XST; -. DR PDBsum; 7JIK; -. DR PDBsum; 7KG4; -. DR AlphaFoldDB; P02749; -. DR BMRB; P02749; -. DR SMR; P02749; -. DR BioGRID; 106847; 28. DR DIP; DIP-46878N; -. DR IntAct; P02749; 20. DR MINT; P02749; -. DR STRING; 9606.ENSP00000205948; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB05446; LJP 1082. DR GlyConnect; 678; 41 N-Linked glycans (4 sites). DR GlyCosmos; P02749; 7 sites, 53 glycans. DR GlyGen; P02749; 7 sites, 59 N-linked glycans (3 sites), 1 O-linked glycan (1 site). DR iPTMnet; P02749; -. DR PhosphoSitePlus; P02749; -. DR SwissPalm; P02749; -. DR BioMuta; APOH; -. DR DMDM; 543826; -. DR CPTAC; CPTAC-654; -. DR CPTAC; non-CPTAC-1090; -. DR EPD; P02749; -. DR jPOST; P02749; -. DR MassIVE; P02749; -. DR MaxQB; P02749; -. DR PaxDb; 9606-ENSP00000205948; -. DR PeptideAtlas; P02749; -. DR PRIDE; P02749; -. DR ProteomicsDB; 51565; -. DR TopDownProteomics; P02749; -. DR ABCD; P02749; 4 sequenced antibodies. DR Antibodypedia; 874; 608 antibodies from 40 providers. DR DNASU; 350; -. DR Ensembl; ENST00000205948.11; ENSP00000205948.6; ENSG00000091583.11. DR GeneID; 350; -. DR KEGG; hsa:350; -. DR MANE-Select; ENST00000205948.11; ENSP00000205948.6; NM_000042.3; NP_000033.2. DR UCSC; uc002jfn.5; human. DR AGR; HGNC:616; -. DR CTD; 350; -. DR DisGeNET; 350; -. DR GeneCards; APOH; -. DR HGNC; HGNC:616; APOH. DR HPA; ENSG00000091583; Tissue enriched (liver). DR MIM; 138700; gene. DR neXtProt; NX_P02749; -. DR OpenTargets; ENSG00000091583; -. DR PharmGKB; PA24903; -. DR VEuPathDB; HostDB:ENSG00000091583; -. DR eggNOG; KOG4297; Eukaryota. DR GeneTree; ENSGT00940000157228; -. DR HOGENOM; CLU_020107_2_0_1; -. DR InParanoid; P02749; -. DR OMA; IAGRRMW; -. DR OrthoDB; 4131542at2759; -. DR PhylomeDB; P02749; -. DR TreeFam; TF334137; -. DR PathwayCommons; P02749; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR SignaLink; P02749; -. DR SIGNOR; P02749; -. DR BioGRID-ORCS; 350; 9 hits in 1151 CRISPR screens. DR ChiTaRS; APOH; human. DR EvolutionaryTrace; P02749; -. DR GeneWiki; Apolipoprotein_H; -. DR GenomeRNAi; 350; -. DR Pharos; P02749; Tbio. DR PRO; PR:P02749; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P02749; Protein. DR Bgee; ENSG00000091583; Expressed in liver and 126 other cell types or tissues. DR ExpressionAtlas; P02749; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0042627; C:chylomicron; IDA:BHF-UCL. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL. DR GO; GO:0031089; C:platelet dense granule lumen; TAS:Reactome. DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA: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: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:0034392; P:negative regulation of smooth muscle cell apoptotic process; IDA:BHF-UCL. 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:0051917; P:regulation of fibrinolysis; IDA:BHF-UCL. DR GO; GO:0006641; P:triglyceride metabolic process; IDA:BHF-UCL. DR GO; GO:0034197; P:triglyceride transport; ISS:BHF-UCL. DR CDD; cd00033; CCP; 4. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 5. DR IDEAL; IID00647; -. DR InterPro; IPR035976; Sushi/SCR/CCP_sf. DR InterPro; IPR015104; Sushi_2. DR InterPro; IPR000436; Sushi_SCR_CCP_dom. DR PANTHER; PTHR19325:SF549; BETA-2-GLYCOPROTEIN 1; 1. DR PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1. DR Pfam; PF00084; Sushi; 4. DR Pfam; PF09014; Sushi_2; 1. DR SMART; SM00032; CCP; 4. DR SUPFAM; SSF57535; Complement control module/SCR domain; 5. DR PROSITE; PS50923; SUSHI; 4. DR Genevisible; P02749; HS. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Heparin-binding; Reference proteome; Repeat; Secreted; Signal; Sushi. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:11250549, FT ECO:0000269|PubMed:1602135, ECO:0000269|PubMed:2349221, FT ECO:0000269|PubMed:6587378" FT CHAIN 20..345 FT /note="Beta-2-glycoprotein 1" FT /id="PRO_0000002059" 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 149 FT /note="O-linked (GalNAc...) threonine" FT CARBOHYD 162 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, FT ECO:0000269|PubMed:6587378" FT CARBOHYD 183 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:6587378" FT CARBOHYD 193 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:6587378" FT CARBOHYD 253 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15084671, FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, FT ECO:0000269|PubMed:19159218, 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 FT /note="V -> A (in dbSNP:rs3826358)" FT /id="VAR_048316" FT VARIANT 107 FT /note="S -> N (in allele APOH*1; dbSNP:rs1801692)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9225969, ECO:0000269|Ref.8" FT /id="VAR_008169" FT VARIANT 154 FT /note="R -> H (in dbSNP:rs8178847)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_019155" FT VARIANT 266 FT /note="V -> L (in dbSNP:rs4581)" FT /evidence="ECO:0000269|PubMed:8099061, ECO:0000269|Ref.8" FT /id="VAR_000673" FT VARIANT 325 FT /note="C -> G (loss of phosphatidylserine-binding; FT dbSNP:rs1801689)" FT /evidence="ECO:0000269|PubMed:9063752" FT /id="VAR_008170" FT VARIANT 335 FT /note="W -> S (in allele APOH*3W; loss of FT phosphatidylserine-binding; dbSNP:rs1801690)" FT /evidence="ECO:0000269|PubMed:9063752, ECO:0000269|Ref.8" FT /id="VAR_008171" FT CONFLICT 121 FT /note="S -> C (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 188 FT /note="C -> N (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:6XSD" FT STRAND 32..36 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 46..51 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 62..65 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:7KG4" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 93..96 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:7JIK" FT STRAND 105..110 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 114..118 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 120..124 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 128..132 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 136..139 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 151..155 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 163..165 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 169..174 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 178..182 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 184..188 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 192..195 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 199..202 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 214..217 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 229..234 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 238..242 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 244..248 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 252..255 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:6V06" FT STRAND 267..270 FT /evidence="ECO:0007829|PDB:3OP8" FT STRAND 272..275 FT /evidence="ECO:0007829|PDB:3OP8" FT STRAND 278..281 FT /evidence="ECO:0007829|PDB:3OP8" FT HELIX 282..285 FT /evidence="ECO:0007829|PDB:3OP8" FT TURN 286..288 FT /evidence="ECO:0007829|PDB:3OP8" FT STRAND 295..302 FT /evidence="ECO:0007829|PDB:3OP8" FT TURN 303..306 FT /evidence="ECO:0007829|PDB:3OP8" FT STRAND 307..316 FT /evidence="ECO:0007829|PDB:3OP8" FT TURN 331..333 FT /evidence="ECO:0007829|PDB:1C1Z" FT HELIX 339..341 FT /evidence="ECO:0007829|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 //