HEP2_MOUSE
ID HEP2_MOUSE Reviewed; 478 AA.
AC P49182;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
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, Hcii;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-44.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7908224; DOI=10.1021/bi00178a021;
RA Zhang G.S., Mehringer J.H., van Deerlin V.M.D., Kozak C.A., Tollefsen D.M.;
RT "Murine heparin cofactor II: purification, cDNA sequence, expression, and
RT gene structure.";
RL Biochemistry 33:3632-3642(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-30 AND ASN-167.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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). Also inhibits chymotrypsin, but in a glycosaminoglycan-
CC independent manner.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in liver.
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 (68 and 72 kDa).
CC {ECO:0000269|PubMed:16944957}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; U07425; AAA18452.1; -; mRNA.
DR EMBL; BC034543; AAH34543.1; -; mRNA.
DR CCDS; CCDS28000.1; -.
DR PIR; A54248; A54248.
DR RefSeq; NP_001317976.1; NM_001331047.1.
DR RefSeq; NP_032249.3; NM_008223.4.
DR AlphaFoldDB; P49182; -.
DR SMR; P49182; -.
DR STRING; 10090.ENSMUSP00000023450; -.
DR MEROPS; I04.019; -.
DR GlyGen; P49182; 4 sites.
DR iPTMnet; P49182; -.
DR PhosphoSitePlus; P49182; -.
DR CPTAC; non-CPTAC-5601; -.
DR CPTAC; non-CPTAC-5602; -.
DR MaxQB; P49182; -.
DR PaxDb; P49182; -.
DR PeptideAtlas; P49182; -.
DR PRIDE; P49182; -.
DR ProteomicsDB; 269697; -.
DR Antibodypedia; 3265; 337 antibodies from 32 providers.
DR DNASU; 15160; -.
DR Ensembl; ENSMUST00000023450; ENSMUSP00000023450; ENSMUSG00000022766.
DR Ensembl; ENSMUST00000231884; ENSMUSP00000156303; ENSMUSG00000022766.
DR GeneID; 15160; -.
DR KEGG; mmu:15160; -.
DR UCSC; uc007yks.2; mouse.
DR CTD; 3053; -.
DR MGI; MGI:96051; Serpind1.
DR VEuPathDB; HostDB:ENSMUSG00000022766; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000158664; -.
DR HOGENOM; CLU_023330_8_0_1; -.
DR InParanoid; P49182; -.
DR OMA; QRLNMVN; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P49182; -.
DR TreeFam; TF343094; -.
DR Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 15160; 0 hits in 71 CRISPR screens.
DR PRO; PR:P49182; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P49182; protein.
DR Bgee; ENSMUSG00000022766; Expressed in liver and 86 other tissues.
DR Genevisible; P49182; MM.
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; Direct protein sequencing; Glycoprotein; Hemostasis;
KW Heparin-binding; Protease inhibitor; Reference proteome; Repeat;
KW Serine protease inhibitor; Signal; Sulfation.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:7908224"
FT CHAIN 24..478
FT /note="Heparin cofactor 2"
FT /id="PRO_0000032495"
FT REPEAT 54..64
FT /note="1"
FT REPEAT 68..78
FT /note="2"
FT REGION 54..78
FT /note="2 X 11 AA approximate repeats, Asp/Glu-rich (acidic)
FT (hirudin-like)"
FT REGION 171..191
FT /note="Glycosaminoglycan-binding site"
FT /evidence="ECO:0000250"
FT SITE 442..443
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT MOD_RES 60
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 478 AA; 54497 MW; 7234711F0083865D CRC64;
MKHPLCTLLS LITFMCIGSK GLAEQLTNEN LTTSFLPANF HKENTVTNDW IPEGEEDEDY
LDLEKLLGED DDYIYIIDAV SPTDSESSAG NILQLFQGKS RIQRLNILNA KFAFNLYRVL
KDQATTSDNL FIAPVGISTA MGMISLGLRG ETHEEVHSVL HFRDFVNASS KYEVTTIHNL
FRKLTHRLFR RNFGYTLRSV NGLYIQKQFP IREDFKAAMR EFYFAEAQEA NFPDPAFISK
ANNHILKLTK GLIKEALENI DPATQMLILN CIYFKGTWVN KFPVEMTHNH NFRLNEREVV
KVSMMQTKGN FLAANDQELD CDILQLEYVG GISMLIVVPR KLSGMKTLEA QLTPQVVERW
QKSMTNRTRE VLLPKFKLEK NYNLVEVLKS MGITKLFNKN GNMSGISDQR IAIDLFKHQS
TITVNEEGTQ AAAVTTVGFM PLSTQVRFTV DRPFLFLVYE HRTSCLLFMG KVTNPAKS
