APOH_BOVIN
ID APOH_BOVIN Reviewed; 345 AA.
AC P17690; Q148G1; Q28052;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 4.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Beta-2-glycoprotein 1;
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Gao B., Virmani M., Romm E., Lazar-Wesley E., Sakaguchi K., Appella E.,
RA Kunos G., Takacs L.;
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-345, PARTIAL PROTEIN SEQUENCE, AND
RP DISULFIDE BONDS.
RC TISSUE=Liver;
RX PubMed=1567819; DOI=10.1021/bi00129a009;
RA Bendixen E., Halkier T., Magnusson S., Sottrup-Jensen L., Kristensen T.;
RT "Complete primary structure of bovine beta 2-glycoprotein I: localization
RT of the disulfide bridges.";
RL Biochemistry 31:3611-3617(1992).
RN [4]
RP PROTEIN SEQUENCE OF 20-345, GLYCOSYLATION AT ASN-92; ASN-162; ASN-183;
RP ASN-193 AND ASN-253, AND DISULFIDE BONDS.
RC TISSUE=Plasma;
RX PubMed=1751487; DOI=10.1021/bi00114a012;
RA Kato H., Enjyoji K.;
RT "Amino acid sequence and location of the disulfide bonds in bovine beta 2
RT glycoprotein I: the presence of five Sushi domains.";
RL Biochemistry 30:11687-11694(1991).
RN [5]
RP PROTEIN SEQUENCE OF 20-41.
RX PubMed=2327984; DOI=10.1042/bj2670261;
RA Li Q., Blacher R., Esch F., Congote L.F.;
RT "Isolation from fetal bovine serum of an apolipoprotein-H-like protein
RT which inhibits thymidine incorporation in fetal calf erythroid cells.";
RL Biochem. J. 267:261-264(1990).
RN [6]
RP GLYCOSYLATION AT THR-33, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19674964; DOI=10.1074/mcp.m900211-mcp200;
RA Darula Z., Medzihradszky K.F.;
RT "Affinity enrichment and characterization of mucin core-1 type
RT glycopeptides from bovine serum.";
RL Mol. Cell. Proteomics 8:2515-2526(2009).
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; L07303; AAA30382.1; -; mRNA.
DR EMBL; BC118364; AAI18365.1; -; mRNA.
DR EMBL; X60065; CAA42669.1; -; mRNA.
DR PIR; JN0502; NBBO.
DR RefSeq; NP_776417.1; NM_173992.2.
DR AlphaFoldDB; P17690; -.
DR SMR; P17690; -.
DR STRING; 9913.ENSBTAP00000002492; -.
DR GlyConnect; 756; 1 O-Linked glycan (1 site).
DR iPTMnet; P17690; -.
DR PaxDb; P17690; -.
DR PeptideAtlas; P17690; -.
DR PRIDE; P17690; -.
DR GeneID; 281006; -.
DR KEGG; bta:281006; -.
DR CTD; 350; -.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_020107_2_0_1; -.
DR InParanoid; P17690; -.
DR OrthoDB; 784427at2759; -.
DR TreeFam; TF334137; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
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; 4.
DR SUPFAM; SSF57535; SSF57535; 5.
DR PROSITE; PS50923; SUSHI; 4.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heparin-binding;
KW Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1751487,
FT ECO:0000269|PubMed:2327984"
FT CHAIN 20..345
FT /note="Beta-2-glycoprotein 1"
FT /evidence="ECO:0000269|PubMed:1567819"
FT /id="PRO_0000002057"
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:0000269|PubMed:19674964"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1567819,
FT ECO:0000269|PubMed:1751487"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1567819,
FT ECO:0000269|PubMed:1751487"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1567819,
FT ECO:0000269|PubMed:1751487"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1567819,
FT ECO:0000269|PubMed:1751487"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1567819,
FT ECO:0000269|PubMed:1751487"
FT DISULFID 23..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:1567819"
FT DISULFID 51..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:1567819"
FT DISULFID 84..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:1567819"
FT DISULFID 110..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:1567819"
FT DISULFID 142..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:1567819"
FT DISULFID 174..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:1567819"
FT DISULFID 205..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:1567819"
FT DISULFID 234..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:1567819"
FT DISULFID 264..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:1567819"
FT DISULFID 300..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:1567819"
FT DISULFID 307..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:1567819"
FT CONFLICT 2
FT /note="P -> L (in Ref. 2; AAI18365)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="E -> G (in Ref. 1; AAA30382)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="F -> S (in Ref. 1; AAA30382)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="H -> R (in Ref. 1; AAA30382)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="H -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="W -> C (in Ref. 1; AAA30382)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="S -> N (in Ref. 1; AAA30382)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="H -> N (in Ref. 1; AAA30382 and 2; AAI18365)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="K -> R (in Ref. 1; AAA30382)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="H -> R (in Ref. 1; AAA30382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 38252 MW; E117DAB609461C33 CRC64;
MPPPALVLLL GFLCHVAIAG RTCPKPDELP FSTVVPLKRT YEPGEQIVFS CQPGYVSRGG
IRRFTCPLTG LWPINTLKCM PRVCPFAGIL ENGTVRYTTF EYPNTISFSC HTGFYLKGAS
SAKCTEEGKW SPDLPVCAPI TCPPPPIPKF ASLSVYKPLA GNNSFYGSKA VFKCLPHHAM
FGNDTVTCTE HGNWTQLPEC REVRCPFPSR PDNGFVNHPA NPVLYYKDTA TFGCHETYSL
DGPEEVECSK FGNWSAQPSC KASCKLSIKR ATVIYEGERV AIQNKFKNGM LHGQKVSFFC
KHKEKKCSYT EDAQCIDGTI EIPKCFKEHS SLAFWKTDAS DVKPC
