APOH_HUMAN
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 03-AUG-2022, entry version 232.
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/";
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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; 27.
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 GlyGen; P02749; 6 sites, 55 N-linked glycans (3 sites).
DR iPTMnet; P02749; -.
DR PhosphoSitePlus; 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; P02749; -.
DR PeptideAtlas; P02749; -.
DR PRIDE; P02749; -.
DR ProteomicsDB; 51565; -.
DR TopDownProteomics; P02749; -.
DR ABCD; P02749; 4 sequenced antibodies.
DR Antibodypedia; 874; 559 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 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; QRYFNPG; -.
DR OrthoDB; 784427at2759; -.
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 1071 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 125 other tissues.
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: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 IDEAL; IID00647; -.
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 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
