APOH_MOUSE
ID APOH_MOUSE Reviewed; 345 AA.
AC Q01339;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Beta-2-glycoprotein 1;
DE AltName: Full=APC inhibitor;
DE AltName: Full=Activated protein C-binding protein;
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=B2gp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1339387; DOI=10.1016/0888-7543(92)90022-k;
RA Nonaka M., Matsuda Y., Shiroishi T., Moriwak K., Natsuume-Sakai S.;
RT "Molecular cloning of mouse beta 2-glycoprotein I and mapping of the gene
RT to chromosome 11.";
RL Genomics 13:1082-1087(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CBA/J; TISSUE=Liver;
RX PubMed=7514402; DOI=10.1006/bbrc.1994.1623;
RA Sellar G.C., Steel D.M., Zafiropoulos A., Seery L.T., Whitehead A.S.;
RT "Characterization, expression and evolution of mouse beta 2-glycoprotein I
RT (apolipoprotein H).";
RL Biochem. Biophys. Res. Commun. 200:1521-1528(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Kristensen T.;
RT "Structure of the human beta-2-glycoprotein I gene.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-117 AND ASN-162.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105; ASN-117; ASN-162; ASN-183
RP AND ASN-193.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Binds to various kinds of negatively charged substances such
CC as heparin, phospholipids, and dextran sulfate. May prevent activation
CC of the intrinsic blood coagulation cascade by binding to phospholipids
CC on the surface of damaged cells.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
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DR EMBL; D10056; BAA00945.1; -; mRNA.
DR EMBL; S70439; AAB30789.1; -; mRNA.
DR EMBL; Y11356; CAA72190.1; -; mRNA.
DR EMBL; BC019811; AAH19811.1; -; mRNA.
DR EMBL; BC053338; AAH53338.1; -; mRNA.
DR CCDS; CCDS25574.1; -.
DR PIR; A43286; NBMS.
DR RefSeq; NP_038503.4; NM_013475.4.
DR AlphaFoldDB; Q01339; -.
DR SMR; Q01339; -.
DR BioGRID; 198165; 8.
DR IntAct; Q01339; 1.
DR STRING; 10090.ENSMUSP00000000049; -.
DR GlyConnect; 652; 1 N-Linked glycan (1 site).
DR GlyGen; Q01339; 6 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q01339; -.
DR PhosphoSitePlus; Q01339; -.
DR SwissPalm; Q01339; -.
DR CPTAC; non-CPTAC-3894; -.
DR jPOST; Q01339; -.
DR MaxQB; Q01339; -.
DR PaxDb; Q01339; -.
DR PeptideAtlas; Q01339; -.
DR PRIDE; Q01339; -.
DR ProteomicsDB; 281901; -.
DR Antibodypedia; 874; 559 antibodies from 40 providers.
DR DNASU; 11818; -.
DR Ensembl; ENSMUST00000000049; ENSMUSP00000000049; ENSMUSG00000000049.
DR GeneID; 11818; -.
DR KEGG; mmu:11818; -.
DR UCSC; uc007mbp.2; mouse.
DR CTD; 350; -.
DR MGI; MGI:88058; Apoh.
DR VEuPathDB; HostDB:ENSMUSG00000000049; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000157228; -.
DR HOGENOM; CLU_020107_2_0_1; -.
DR InParanoid; Q01339; -.
DR OMA; TEDAECI; -.
DR OrthoDB; 784427at2759; -.
DR PhylomeDB; Q01339; -.
DR TreeFam; TF334137; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 11818; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Apoh; mouse.
DR PRO; PR:Q01339; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q01339; protein.
DR Bgee; ENSMUSG00000000049; Expressed in left lobe of liver and 62 other tissues.
DR ExpressionAtlas; Q01339; baseline and differential.
DR Genevisible; Q01339; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0042627; C:chylomicron; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
DR GO; GO:0060230; F:lipoprotein lipase activator activity; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0031100; P:animal organ regeneration; ISO:MGI.
DR GO; GO:0007596; P:blood coagulation; ISO:MGI.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; ISO:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0030195; P:negative regulation of blood coagulation; ISO:MGI.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; ISO:MGI.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; ISO:MGI.
DR GO; GO:0060268; P:negative regulation of respiratory burst; ISO:MGI.
DR GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0031639; P:plasminogen activation; ISO:MGI.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; ISO:MGI.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISO:MGI.
DR GO; GO:0030193; P:regulation of blood coagulation; IMP:MGI.
DR GO; GO:0051917; P:regulation of fibrinolysis; ISO:MGI.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:MGI.
DR GO; GO:0034197; P:triglyceride transport; ISO:MGI.
DR CDD; cd00033; CCP; 4.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR015104; Sushi_2.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 4.
DR Pfam; PF09014; Sushi_2; 1.
DR SMART; SM00032; CCP; 5.
DR SUPFAM; SSF57535; SSF57535; 5.
DR PROSITE; PS50923; SUSHI; 4.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Heparin-binding; Reference proteome; Repeat;
KW Secreted; Signal; Sushi.
FT SIGNAL 1..19
FT CHAIN 20..345
FT /note="Beta-2-glycoprotein 1"
FT /id="PRO_0000002060"
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 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT DISULFID 23..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 51..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 84..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 110..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 142..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 174..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 205..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 234..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 264..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 300..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 307..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CONFLICT 252
FT /note="G -> R (in Ref. 2; AAB30789)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 38619 MW; C83F8A6EBD51C940 CRC64;
MVSPVLALFS AFLCHVAIAG RICPKPDDLP FATVVPLKTS YDPGEQIVYS CKPGYVSRGG
MRRFTCPLTG MWPINTLRCV PRVCPFAGIL ENGIVRYTSF EYPKNISFAC NPGFFLNGTS
SSKCTEEGKW SPDIPACARI TCPPPPVPKF ALLKDYRPSA GNNSLYQDTV VFKCLPHFAM
IGNDTVMCTE QGNWTRLPEC LEVKCPFPPR PENGYVNYPA KPVLLYKDKA TFGCHETYKL
DGPEEAECTK TGTWSFLPTC RESCKLPVKK ATVLYQGMRV KIQEQFKNGM MHGDKIHFYC
KNKEKKCSYT VEAHCRDGTI EIPSCFKEHS SLAFWKTDAS ELTPC
