ID A0A3B3I3M0_ORYLA Unreviewed; 373 AA.
AC A0A3B3I3M0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Beta-2-glycoprotein 1 {ECO:0000256|ARBA:ARBA00020104};
DE AltName: Full=Apolipoprotein H {ECO:0000256|ARBA:ARBA00029855};
DE AltName: Full=Beta-2-glycoprotein I {ECO:0000256|ARBA:ARBA00033414};
GN Name=ntd5 {ECO:0000313|Ensembl:ENSORLP00000038725.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000038725.1, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000038725.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000038725.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000038725.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000038725.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00003651}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR AlphaFoldDB; A0A3B3I3M0; -.
DR Ensembl; ENSORLT00000043154.1; ENSORLP00000038725.1; ENSORLG00000011418.2.
DR GeneTree; ENSGT00940000154967; -.
DR InParanoid; A0A3B3I3M0; -.
DR Proteomes; UP000001038; Chromosome 16.
DR Bgee; ENSORLG00000011418; Expressed in muscle tissue and 9 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0030414; F:peptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00033; CCP; 3.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 4.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR015104; Sushi_2.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR008197; WAP_dom.
DR PANTHER; PTHR19325:SF502; BETA-2-GLYCOPROTEIN 1; 1.
DR PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1.
DR Pfam; PF00084; Sushi; 3.
DR Pfam; PF09014; Sushi_2; 1.
DR Pfam; PF00095; WAP; 1.
DR SMART; SM00032; CCP; 3.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 4.
DR PROSITE; PS50923; SUSHI; 3.
DR PROSITE; PS51390; WAP; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00302}; Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..373
FT /note="Beta-2-glycoprotein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017249283"
FT DOMAIN 31..83
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 84..147
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 157..214
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 215..275
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DISULFID 185..212
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 217..260
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 246..273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 373 AA; 40974 MW; 151B5DE1E456F19E CRC64;
MCLSLSYTKS GLTASMYSGL LLLSMWALAG TASLWDSESC PERLVGAEGR RTCPRSCKSD
RDCGGKRQCL CDSECGLSCV VPGRTCPWPL PLNENSRASL LSPTPSFSSL LEVLCKPGFT
LADGSDATVR RCQGDRQWSG DKPICTEAKS PELPGVRTCP LPQQVINTFS IHGDASVGTS
IRYSCLSGAD IVGRQENYCQ FNQTWLYPHP NCKEMLCQPP EEVEQGYVVA VQKTEYEVGF
DIHYLCKKNF LLDGPQKITC LSNGSWSAAP PHCRGEEPFV FQLLTFVRLG IRAEDLSISA
ARCIIPAERS RVVIGGVKRW PFDVTDGLVP HGENVTFFCK HPQKQCSFTA AQTCFDGKLE
TPLCYLGKTR TPI
//