HEP2_RAT
ID HEP2_RAT Reviewed; 479 AA.
AC Q64268; Q5BKA6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8286422; DOI=10.1016/0167-4781(94)90129-5;
RA Westrup D., Ragg H.;
RT "Secondary thrombin-binding site, glycosaminoglycan binding domain and
RT reactive center region of leuserpin-2 are strongly conserved in mammalian
RT species.";
RL Biochim. Biophys. Acta 1217:93-96(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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) (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The N-terminal acidic repeat region mediates, in part, the
CC glycosaminoglycan-accelerated thrombin inhibition. {ECO:0000250}.
CC -!- PTM: Different composition of the N-linked oligosaccharides appears to
CC yield a 68-kDa and a 72-kDa form. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; X74550; CAA52644.1; -; mRNA.
DR EMBL; X74549; CAA52643.1; -; mRNA.
DR EMBL; BC091145; AAH91145.1; -; mRNA.
DR PIR; S41066; S41066.
DR RefSeq; NP_077358.1; NM_024382.1.
DR RefSeq; XP_006248771.1; XM_006248709.2.
DR AlphaFoldDB; Q64268; -.
DR SMR; Q64268; -.
DR STRING; 10116.ENSRNOP00000031829; -.
DR MEROPS; I04.019; -.
DR GlyGen; Q64268; 4 sites.
DR iPTMnet; Q64268; -.
DR PhosphoSitePlus; Q64268; -.
DR PaxDb; Q64268; -.
DR PRIDE; Q64268; -.
DR Ensembl; ENSRNOT00000031819; ENSRNOP00000031829; ENSRNOG00000001865.
DR GeneID; 79224; -.
DR KEGG; rno:79224; -.
DR CTD; 3053; -.
DR RGD; 619854; Serpind1.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000158664; -.
DR HOGENOM; CLU_023330_8_0_1; -.
DR InParanoid; Q64268; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q64268; -.
DR TreeFam; TF343094; -.
DR Reactome; R-RNO-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q64268; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001865; Expressed in liver and 6 other tissues.
DR ExpressionAtlas; Q64268; baseline and differential.
DR Genevisible; Q64268; RN.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW Blood coagulation; Glycoprotein; Hemostasis; Heparin-binding;
KW Protease inhibitor; Reference proteome; Repeat; Serine protease inhibitor;
KW Signal; Sulfation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..479
FT /note="Heparin cofactor 2"
FT /id="PRO_0000032497"
FT REPEAT 55..65
FT /note="1"
FT REPEAT 69..79
FT /note="2"
FT REGION 55..79
FT /note="2 X 11 AA approximate repeats, Asp/Glu-rich (acidic)
FT (hirudin-like)"
FT REGION 172..192
FT /note="Glycosaminoglycan-binding site"
FT /evidence="ECO:0000250"
FT SITE 443..444
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 74
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 479 AA; 54552 MW; 4F736C2F8459E514 CRC64;
MKHPAYTLLL SLIMSMCAGS KGLAEQLTKE NLTVSLLPPN FHKENTVTND WIPEGEEDDD
YLDLEKLLSE DDDYIYVVDA VSPTDSESSA GNILQLFQGK SRIQRLNILN AKFAFNLYRV
LKDQATSSDN IFIAPVGIST AMGMISLGLR GETHEEVHSV LHFKDFVNAS SKYEVTTIHN
LFRKLTHRLF RRNFGYTLQS VNDLYIQKQF PIREDFKAAM REFYFAEAQE ADFSDPAFIS
KANSHILKLT KGLIKEALEN TDSATQMMIL NCIYFKGAWM NKFPVEMTHN HNFRLNEREV
VKVSMMQTKG NFLAANDQEL DCDILQLEYV GGISMLIVIP RKLSGMKTLE AQLTPQVVER
WQKSMTNRTR EVLLPKFKLE KNYNLVEVLK SMGITKLFNK NGNMSGISDQ RIIIDLFKHQ
STITVNEEGT QAAAVTTVGF MPLSTQVRFT VDRPFLFLVY EHRTSCLLFM GRVANPAKS
