HABP2_RAT
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 03-AUG-2022, entry version 108.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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-chain
CC between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and
CC therefore does not initiate the formation of the fibrin clot and does
CC not cause the fibrinolysis directly. It does not cleave (activate)
CC prothrombin and plasminogen but converts the inactive single chain
CC urinary plasminogen activator (pro-urokinase) to the active two chain
CC form. Activates coagulation factor VII (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; disulfide-linked. Heterodimer of a 50 kDa heavy
CC and a 27 kDa light chain linked by a disulfide bond (By similarity).
CC {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 50
CC kDa heavy chain and cleavage at Arg-311 or Lys-317 can give rise to the
CC 27 kDa light chain. The heavy chain can undergo further proteolytic
CC cleavage at Arg-168 or Arg-169 to give rise to two inactive 26 kDa
CC fragments and the light chain can undergo further proteolytic cleavage
CC at Arg-478 to give rise to inactive 17 kDa and 8 kDa fragments (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AB177406; BAD19044.1; -; mRNA.
DR RefSeq; NP_001001505.1; NM_001001505.1.
DR AlphaFoldDB; Q6L711; -.
DR SMR; 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 InParanoid; Q6L711; -.
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:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:1904975; P:response to bleomycin; IEP:RGD.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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; IPR043504; Peptidase_S1_PA_chymotrypsin.
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; Disulfide bond; EGF-like domain;
KW Hydrolase; Kringle; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..311
FT /note="Hyaluronan-binding protein 2 50 kDa heavy chain"
FT /id="PRO_0000027907"
FT CHAIN 27..311
FT /note="Hyaluronan-binding protein 2 50 kDa heavy chain
FT alternate form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027908"
FT CHAIN 312..558
FT /note="Hyaluronan-binding protein 2 27 kDa light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027909"
FT CHAIN 318..558
FT /note="Hyaluronan-binding protein 2 27 kDa light chain
FT alternate form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027910"
FT DOMAIN 71..107
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 109..146
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 148..186
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 191..274
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 312..553
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 360
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 409
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 507
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 167..168
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 168..169
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 478..479
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT DISULFID 75..86
FT /evidence="ECO:0000250"
FT DISULFID 80..95
FT /evidence="ECO:0000250"
FT DISULFID 97..106
FT /evidence="ECO:0000250"
FT DISULFID 113..123
FT /evidence="ECO:0000250"
FT DISULFID 118..134
FT /evidence="ECO:0000250"
FT DISULFID 136..145
FT /evidence="ECO:0000250"
FT DISULFID 152..163
FT /evidence="ECO:0000250"
FT DISULFID 157..174
FT /evidence="ECO:0000250"
FT DISULFID 176..185
FT /evidence="ECO:0000250"
FT DISULFID 192..274
FT /evidence="ECO:0000250"
FT DISULFID 213..255
FT /evidence="ECO:0000250"
FT DISULFID 244..269
FT /evidence="ECO:0000250"
FT DISULFID 299..433
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000255|PROSITE-ProRule:PRU00121, ECO:0000255|PROSITE-
FT ProRule:PRU00274"
FT DISULFID 345..361
FT /evidence="ECO:0000250"
FT DISULFID 445..513
FT /evidence="ECO:0000250"
FT DISULFID 475..491
FT /evidence="ECO:0000250"
FT DISULFID 503..531
FT /evidence="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
