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   27-MAR-2024, entry version 179.
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,
RC   Spleen, 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   GlyCosmos; Q01339; 6 sites, 2 glycans.
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; 10090-ENSMUSP00000000049; -.
DR   PeptideAtlas; Q01339; -.
DR   ProteomicsDB; 281901; -.
DR   Antibodypedia; 874; 608 antibodies from 40 providers.
DR   DNASU; 11818; -.
DR   Ensembl; ENSMUST00000000049.6; ENSMUSP00000000049.6; ENSMUSG00000000049.12.
DR   GeneID; 11818; -.
DR   KEGG; mmu:11818; -.
DR   UCSC; uc007mbp.2; mouse.
DR   AGR; MGI:88058; -.
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; TFAVMRQ; -.
DR   OrthoDB; 4131542at2759; -.
DR   PhylomeDB; Q01339; -.
DR   TreeFam; TF334137; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   BioGRID-ORCS; 11818; 1 hit in 80 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 63 other cell types or tissues.
DR   ExpressionAtlas; Q01339; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0042627; C:chylomicron; 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: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: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: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   Gene3D; 2.10.70.10; Complement Module, domain 1; 5.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR015104; Sushi_2.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR19325:SF567; LOCOMOTION-RELATED PROTEIN HIKARU GENKI; 1.
DR   Pfam; PF00084; Sushi; 4.
DR   Pfam; PF09014; Sushi_2; 1.
DR   SMART; SM00032; CCP; 5.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 5.
DR   PROSITE; PS50923; SUSHI; 4.
DR   Genevisible; Q01339; MM.
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
//