GenomeNet

Database: UniProt
Entry: Q6L711
LinkDB: Q6L711
Original site: Q6L711 
ID   HABP2_RAT               Reviewed;         558 AA.
AC   Q6L711;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 96.
DE   RecName: Full=Hyaluronan-binding protein 2;
DE            EC=3.4.21.-;
DE   AltName: Full=Plasma hyaluronan-binding protein;
DE   Contains:
DE     RecName: Full=Hyaluronan-binding protein 2 50 kDa heavy chain;
DE   Contains:
DE     RecName: Full=Hyaluronan-binding protein 2 50 kDa heavy chain alternate form;
DE   Contains:
DE     RecName: Full=Hyaluronan-binding protein 2 27 kDa light chain;
DE   Contains:
DE     RecName: Full=Hyaluronan-binding protein 2 27 kDa light chain alternate form;
DE   Flags: Precursor;
GN   Name=Habp2; Synonyms=Phbp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Shimizu S., Satou K.;
RT   "Molecular cloning and expression of rat PHBP.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves the alpha-chain at multiple sites and the beta-
CC       chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of
CC       fibrinogen and therefore does not initiate the formation of the
CC       fibrin clot and does not cause the fibrinolysis directly. It does
CC       not cleave (activate) prothrombin and plasminogen but converts the
CC       inactive single chain urinary plasminogen activator (pro-
CC       urokinase) to the active two chain form. Activates coagulation
CC       factor VII (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer; disulfide-linked. Heterodimer of a 50 kDa
CC       heavy and a 27 kDa light chain linked by a disulfide bond (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted as an
CC       inactive single-chain precursor and is then activated to a
CC       heterodimeric form. {ECO:0000250}.
CC   -!- PTM: Proteolytic cleavage at Gly-23 or Met-27 can give rise to the
CC       50 kDa heavy chain and cleavage at Arg-311 or Lys-317 can give
CC       rise to the 27 kDa light chain. The heavy chain can undergo
CC       further proteolytic cleavage at Arg-168 or Arg-169 to give rise to
CC       two inactive 26 kDa fragments and the light chain can undergo
CC       further proteolytic cleavage at Arg-478 to give rise to inactive
CC       17 kDa and 8 kDa fragments (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; AB177406; BAD19044.1; -; mRNA.
DR   RefSeq; NP_001001505.1; NM_001001505.1.
DR   UniGene; Rn.161908; -.
DR   ProteinModelPortal; Q6L711; -.
DR   STRING; 10116.ENSRNOP00000045891; -.
DR   MEROPS; S01.033; -.
DR   PaxDb; Q6L711; -.
DR   PRIDE; Q6L711; -.
DR   GeneID; 292126; -.
DR   KEGG; rno:292126; -.
DR   UCSC; RGD:1302979; rat.
DR   CTD; 3026; -.
DR   RGD; 1302979; Habp2.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000237314; -.
DR   HOVERGEN; HBG106385; -.
DR   InParanoid; Q6L711; -.
DR   KO; K08648; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q6L711; -.
DR   PRO; PR:Q6L711; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:1904975; P:response to bleomycin; IEP:RGD.
DR   CDD; cd00108; KR; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.20.10; -; 1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000001; Kringle.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR018056; Kringle_CS.
DR   InterPro; IPR038178; Kringle_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57440; SSF57440; 1.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS00021; KRINGLE_1; 1.
DR   PROSITE; PS50070; KRINGLE_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
KW   EGF-like domain; Hydrolase; Kringle; Protease; Reference proteome;
KW   Repeat; Secreted; Serine protease; Signal.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    311       Hyaluronan-binding protein 2 50 kDa heavy
FT                                chain.
FT                                /FTId=PRO_0000027907.
FT   CHAIN        27    311       Hyaluronan-binding protein 2 50 kDa heavy
FT                                chain alternate form. {ECO:0000250}.
FT                                /FTId=PRO_0000027908.
FT   CHAIN       312    558       Hyaluronan-binding protein 2 27 kDa light
FT                                chain. {ECO:0000250}.
FT                                /FTId=PRO_0000027909.
FT   CHAIN       318    558       Hyaluronan-binding protein 2 27 kDa light
FT                                chain alternate form. {ECO:0000250}.
FT                                /FTId=PRO_0000027910.
FT   DOMAIN       71    107       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      109    146       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      148    186       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      191    274       Kringle. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      312    553       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    360    360       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    409    409       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    507    507       Charge relay system. {ECO:0000250}.
FT   SITE        167    168       Cleavage. {ECO:0000250}.
FT   SITE        168    169       Cleavage. {ECO:0000250}.
FT   SITE        478    479       Cleavage. {ECO:0000250}.
FT   DISULFID     75     86       {ECO:0000250}.
FT   DISULFID     80     95       {ECO:0000250}.
FT   DISULFID     97    106       {ECO:0000250}.
FT   DISULFID    113    123       {ECO:0000250}.
FT   DISULFID    118    134       {ECO:0000250}.
FT   DISULFID    136    145       {ECO:0000250}.
FT   DISULFID    152    163       {ECO:0000250}.
FT   DISULFID    157    174       {ECO:0000250}.
FT   DISULFID    176    185       {ECO:0000250}.
FT   DISULFID    192    274       {ECO:0000250}.
FT   DISULFID    213    255       {ECO:0000250}.
FT   DISULFID    244    269       {ECO:0000250}.
FT   DISULFID    299    433       Interchain (between heavy and light
FT                                chains). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000255|PROSITE-
FT                                ProRule:PRU00121, ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   DISULFID    345    361       {ECO:0000250}.
FT   DISULFID    445    513       {ECO:0000250}.
FT   DISULFID    475    491       {ECO:0000250}.
FT   DISULFID    503    531       {ECO:0000250}.
SQ   SEQUENCE   558 AA;  62093 MW;  D7CA0BB1E276D475 CRC64;
     MSVVMLVFRV LLLIALVGNS AIGLSLMPFI APPDPDWTPD DYYYSYEQSS PDKDASVTQT
     SPENPDWYYE DDDPCQSNPC EHGGDCIIRG NTFSCSCPAP FSGSRCQTVQ NKCKDNPCVQ
     GDCLITQTPP YYRCACKYPY TGPDCSKVLP VCRPNPCQNG GVCSRHRRRS RFSCACPDQY
     KGRFCEIGPD DCYVGDGYSY RGKVSRTVNQ NPCLYWNSHL LLQENYNMFM EDAETHGIAD
     HNFCRNPDGD HKPWCFVKVN SEKVKWEYCN VEVCPESDAA NPVGSLQEPV MELPGFDSCG
     KTEMTEHAVK RIYGGFKSTA GKHPWQVSLQ TSLPLTTSMP QGHFCGGSLI HPCWVLTAAH
     CTDMSTKHLK VVLGDQDLKK TESHEQTFRV EKILKYSQYN ERDEIPHNDI ALLKLKPVGG
     HCALESKYVK TVCLPSDPFP SGTECHISGW GVTETGEGSR QLLDAKVKLI ANALCNSRQL
     YDHTIDDSMI CAGNLQKPGS DTCQGDSGGP LTCEKDGTYY VYGIVSWGQE CGKKPGVYTQ
     VTKFLNWIKT TMHKEAGL
//
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