ID   HEP2_RABIT              Reviewed;         480 AA.
AC   P47776;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Heparin cofactor 2;
DE   AltName: Full=Heparin cofactor II;
DE            Short=HC-II;
DE   AltName: Full=Protease inhibitor leuserpin-2;
DE   AltName: Full=Serpin D1;
DE   Flags: Precursor;
GN   Name=SERPIND1; Synonyms=HCF2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7974347;
RA   Sheffield W.P., Schuyler P.D., Blajchman M.A.;
RT   "Molecular cloning and expression of rabbit heparin cofactor II: a plasma
RT   thrombin inhibitor highly conserved between species.";
RL   Thromb. Haemost. 71:778-782(1994).
CC   -!- FUNCTION: Thrombin inhibitor activated by the glycosaminoglycans,
CC       heparin or dermatan sulfate. In the presence of the latter, HC-II
CC       becomes the predominant thrombin inhibitor in place of antithrombin III
CC       (AT).
CC   -!- DOMAIN: The N-terminal acidic repeat region mediates, in part, the
CC       glycosaminoglycan-accelerated thrombin inhibition. {ECO:0000250}.
CC   -!- PTM: N-glycosylated; different glycan composition appears to lead to
CC       two forms of this protein (56 and 60 kDa).
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; S73493; AAB32401.1; -; mRNA.
DR   PIR; I46990; I46990.
DR   RefSeq; NP_001075798.1; NM_001082329.1.
DR   AlphaFoldDB; P47776; -.
DR   SMR; P47776; -.
DR   STRING; 9986.ENSOCUP00000007813; -.
DR   MEROPS; I04.019; -.
DR   PRIDE; P47776; -.
DR   GeneID; 100009170; -.
DR   KEGG; ocu:100009170; -.
DR   CTD; 3053; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; P47776; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   CDD; cd02047; serpinD1_HCF2; 1.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR033831; HCII_serpin_dom.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   PANTHER; PTHR11461; PTHR11461; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Glycoprotein; Hemostasis; Heparin-binding;
KW   Protease inhibitor; Reference proteome; Repeat; Serine protease inhibitor;
KW   Signal; Sulfation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..480
FT                   /note="Heparin cofactor 2"
FT                   /id="PRO_0000032496"
FT   REPEAT          56..66
FT                   /note="1"
FT   REPEAT          70..80
FT                   /note="2"
FT   REGION          56..80
FT                   /note="2 X 11 AA approximate repeats, Asp/Glu-rich (acidic)
FT                   (hirudin-like)"
FT   REGION          173..193
FT                   /note="Glycosaminoglycan-binding site"
FT                   /evidence="ECO:0000250"
FT   SITE            444..445
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         62
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         75
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   480 AA;  54532 MW;  803BCF25203CA4FA CRC64;
     MQHRPHLLLI SLTIMSVCGG SNGLTDQLNN KNLTMPLLPI EFHKENTVTN DWIPEGEEDD
     DYLDLEKLLS EDDDYIDIID AVSPTDSEAS AGNILQLFQG KSRIQRLNIL NAKFAFSLYR
     ALKDQANAFD NIFIAPVGIS TAMGMISLGL KGETHEQVHS VLHFRDFVNA SSKYEILTIH
     NLFRKLTHRL FRRNFGYTLR SVNDLYVQKQ FPIREDFKAK VREYYFAEAQ AADFSDPAFI
     SKANNHILKV TKGLIKEALE NVDPATQMMI LNCIYFKGTW VNKFPVEMTH NHNFRLNERE
     VVKVSMMQTK GNFLAANDQE LACDVLQLEY VGGISMLIVV PHKLSGMKTL EAQLTPQVVE
     RWQKSMTNRT REVLLPKFKL EKNYNLVEAL KSMGVTELFD KNGNMSGISD QGITMDLFKH
     QGTITVNEEG TQAAAVTTVG FMPLSTQVRF TVDRPFLFLV YEHRTSCLLF MGKVANPVRS