ID APOH_PANTR Reviewed; 345 AA.
AC Q95LB0;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 121.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-229.
RX PubMed=11479737; DOI=10.1007/s004390100549;
RA Sanghera D.K., Nestlerode C.S., Ferrell R.E., Kamboh M.I.;
RT "Chimpanzee apolipoprotein H (beta2-glycoprotein I): report on the gene
RT structure, a common polymorphism, and a high prevalence of antiphospholipid
RT antibodies.";
RL Hum. Genet. 109:63-72(2001).
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 {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
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DR EMBL; AF358415; AAK71538.1; -; Genomic_DNA.
DR EMBL; AF358408; AAK71538.1; JOINED; Genomic_DNA.
DR EMBL; AF358409; AAK71538.1; JOINED; Genomic_DNA.
DR EMBL; AF358410; AAK71538.1; JOINED; Genomic_DNA.
DR EMBL; AF358411; AAK71538.1; JOINED; Genomic_DNA.
DR EMBL; AF358412; AAK71538.1; JOINED; Genomic_DNA.
DR EMBL; AF358413; AAK71538.1; JOINED; Genomic_DNA.
DR EMBL; AF358414; AAK71538.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001009118.1; NM_001009118.3.
DR AlphaFoldDB; Q95LB0; -.
DR BMRB; Q95LB0; -.
DR SMR; Q95LB0; -.
DR STRING; 9598.ENSPTRP00000016233; -.
DR GlyCosmos; Q95LB0; 6 sites, No reported glycans.
DR PaxDb; 9598-ENSPTRP00000016233; -.
DR Ensembl; ENSPTRT00000017524.4; ENSPTRP00000016233.3; ENSPTRG00000009556.5.
DR GeneID; 468459; -.
DR KEGG; ptr:468459; -.
DR CTD; 350; -.
DR VGNC; VGNC:6341; APOH.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000157228; -.
DR HOGENOM; CLU_020107_2_0_1; -.
DR InParanoid; Q95LB0; -.
DR OMA; IAGRRMW; -.
DR OrthoDB; 4131542at2759; -.
DR TreeFam; TF334137; -.
DR Proteomes; UP000002277; Chromosome 17.
DR Bgee; ENSPTRG00000009556; Expressed in liver and 16 other cell types or tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0042627; C:chylomicron; IEA:Ensembl.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0060230; F:lipoprotein lipase activator activity; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0030195; P:negative regulation of blood coagulation; IEA:Ensembl.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; IEA:Ensembl.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IEA:Ensembl.
DR GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0031639; P:plasminogen activation; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
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: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.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Heparin-binding; Reference proteome; Repeat;
KW Secreted; Signal; Sushi.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..345
FT /note="Beta-2-glycoprotein 1"
FT /id="PRO_0000002061"
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 /evidence="ECO:0000250"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 VARIANT 229
FT /note="K -> E (in allele APOH*4)"
FT /evidence="ECO:0000269|PubMed:11479737"
FT /id="VAR_018697"
SQ SEQUENCE 345 AA; 38267 MW; 712A3EDA2AD4FD36 CRC64;
MISPVLILFS SFLCHVAIAG RTCPKPDDLP FSTVVPLKTF YEPGEEITYS CKPGYVSRGG
MRKFICPLTG LWPINTLKCT PRVCPFAGIL ENGAVRYTTF EYPNTISFSC NTGFYLNGAD
SAKCTEEGKW SPELPVCAPI TCPPPSIPTF ATLHVYKPSA GNNSLYRDTA VFECLPQHAM
FGNDTITCTT HGNWTKLPEC REVKCPFPSR PDNGFVNYPA KPTLYYKDKA TFGCHDGYSL
DGPEEIECTK LGNWSAMPSC KASCKVPVKK ATVVYQGERV KIQEKFKNGM LHGDKVSFFC
KNKEKKCSYT EDAQCIDGTI EVPKCFKEHS SLAFWKTDAS DVKPC
//
