ID A0A3B3TI89_9TELE Unreviewed; 328 AA.
AC A0A3B3TI89;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=APOH {ECO:0000313|Ensembl:ENSPLAP00000016358.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000000377.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000000377.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR Ensembl; ENSPLAT00000016533.1; ENSPLAP00000000377.1; ENSPLAG00000001200.1.
DR Ensembl; ENSPLAT00000025534.1; ENSPLAP00000016358.1; ENSPLAG00000020524.1.
DR GeneTree; ENSGT00940000157228; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 2.
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; 3.
DR Pfam; PF09014; Sushi_2; 1.
DR SMART; SM00032; CCP; 3.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 5.
DR PROSITE; PS50923; SUSHI; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00302}; Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..328
FT /note="Beta-2-glycoprotein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040590372"
FT DOMAIN 22..83
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 187..246
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DISULFID 189..232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 328 AA; 36249 MW; F79EB965FCCB3271 CRC64;
FVPWLKLNFF CLTSPSSLFL PPVCGRPRVS DGVDVSSMKR VFEIGEDVTL SCEQGYSPST
ATPPRITCTA TGEWTPANLA CSRESRPQLL NTYLSLFRYV MVGANESRCL HDGTWSHPPP
LCKGVNCPLP KPPREGRIVH DKAVTGTSTI YGQGWTYECN PPKAPSYERG SCMADGSATE
PPVCRDVSCS IPPRIANGVI TFAVMRQHSY KEKVKYSCLE PYTLEGEAEI QCQNTGNWSS
KPVCRAPCEV GIKRGRIFYN GRKIWIEDLR PNRVLHGEHV AFYCKNKAEK CGYPVASTCN
DGNLPIPDCY ERESMPAGQA LLKTGPVD
//
