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APOH_PANTR
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   03-AUG-2022, entry version 115.
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   PaxDb; Q95LB0; -.
DR   PRIDE; Q95LB0; -.
DR   Ensembl; ENSPTRT00000017524; ENSPTRP00000016233; ENSPTRG00000009556.
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; QRYFNPG; -.
DR   OrthoDB; 784427at2759; -.
DR   TreeFam; TF334137; -.
DR   Proteomes; UP000002277; Chromosome 17.
DR   Bgee; ENSPTRG00000009556; Expressed in liver and 16 other 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:0051006; P:positive regulation of lipoprotein lipase activity; IEA:Ensembl.
DR   GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
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   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
 
 
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