ID HABP2_MOUSE Reviewed; 558 AA.
AC Q8K0D2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 08-NOV-2023, entry version 139.
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 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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9401717; DOI=10.1248/bpb.20.1127;
RA Hashimoto K., Tobe T., Sumiya J., Saguchi K., Sano Y., Nakano Y.,
RA Choi-Miura N.-H., Tomita M.;
RT "Cloning of the cDNA for a mouse homologue of human PHBP: a novel
RT hyaluronan-binding protein.";
RL Biol. Pharm. Bull. 20:1127-1130(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-558 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 PROTEIN SEQUENCE OF N-TERMINUS, AND POST-TRANSLATIONAL MODIFICATIONS.
RX PubMed=11379758; DOI=10.1248/bpb.24.448;
RA Choi-Miura N.H., Takahashi K., Yoda M., Saito K., Mazda T., Tomita M.;
RT "Proteolytic activation and inactivation of the serine protease activity of
RT plasma hyaluronan binding protein.";
RL Biol. Pharm. Bull. 24:448-452(2001).
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.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted as an inactive single-
CC chain precursor and is then activated to a heterodimeric form.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K0D2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K0D2-2; Sequence=VSP_015395;
CC -!- TISSUE SPECIFICITY: Liver and kidney. {ECO:0000269|PubMed:9401717}.
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 2 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.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31775.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC031775; AAH31775.1; ALT_INIT; mRNA.
DR PIR; JC5878; JC5878.
DR RefSeq; NP_666213.1; NM_146101.2.
DR AlphaFoldDB; Q8K0D2; -.
DR SMR; Q8K0D2; -.
DR BioGRID; 230489; 6.
DR STRING; 10090.ENSMUSP00000093641; -.
DR MEROPS; S01.033; -.
DR PhosphoSitePlus; Q8K0D2; -.
DR CPTAC; non-CPTAC-3295; -.
DR MaxQB; Q8K0D2; -.
DR PaxDb; 10090-ENSMUSP00000093641; -.
DR ProteomicsDB; 270928; -. [Q8K0D2-1]
DR ProteomicsDB; 270929; -. [Q8K0D2-2]
DR DNASU; 226243; -.
DR GeneID; 226243; -.
DR KEGG; mmu:226243; -.
DR UCSC; uc008hyt.1; mouse. [Q8K0D2-1]
DR AGR; MGI:1196378; -.
DR CTD; 3026; -.
DR MGI; MGI:1196378; Habp2.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q8K0D2; -.
DR OrthoDB; 4629979at2759; -.
DR PhylomeDB; Q8K0D2; -.
DR BioGRID-ORCS; 226243; 0 hits in 64 CRISPR screens.
DR ChiTaRS; Habp2; mouse.
DR PRO; PR:Q8K0D2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K0D2; Protein.
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:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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 PANTHER; PTHR24264:SF40; HYALURONAN-BINDING PROTEIN 2; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Hydrolase;
KW Kringle; Protease; Reference proteome; Repeat; Secreted; Serine protease;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:11379758"
FT CHAIN 24..311
FT /note="Hyaluronan-binding protein 2 50 kDa heavy chain"
FT /id="PRO_0000027903"
FT CHAIN 27..311
FT /note="Hyaluronan-binding protein 2 50 kDa heavy chain
FT alternate form"
FT /id="PRO_0000027904"
FT CHAIN 312..558
FT /note="Hyaluronan-binding protein 2 27 kDa light chain"
FT /id="PRO_0000027905"
FT CHAIN 318..558
FT /note="Hyaluronan-binding protein 2 27 kDa light chain
FT alternate form"
FT /id="PRO_0000027906"
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 SITE 168..169
FT /note="Cleavage"
FT SITE 478..479
FT /note="Cleavage"
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"
FT VAR_SEQ 36..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015395"
SQ SEQUENCE 558 AA; 62357 MW; 0580CB38F6708E41 CRC64;
MFVRMLVFRV LLLIALVGKS VIGLSLMSFI APPDPDWTPD DYYYSYEQSS PDEDPSVTQT
TPENPDWYYE DDDPCQSNPC EHGGDCIIRG DTFSCSCPAP FSGSRCQTAQ NKCKDNPCVH
GDCLITQKHP YYRCACKYPY TGPDCSKVLP ACRPNPCQNG GVCSRHRRRS RFTCACPDQY
KGKFCEIGPD DCYVGDGYSY RGKVSKTVNQ NPCLYWNSHL LLQETYNMFM EDAETHGIAE
HNFCRNPDGD HKPWCFVKVN SEKVKWEYCD VTVCPVPDTP NPVESLLEPV MELPGFESCG
KTEVAEHAVK RIYGGFKSTA GKHPWQVSLQ TSLPLTTSMP QGHFCGGALI HPCWVLTAAH
CTDINTKHLK VVLGDQDLKK TESHEQTFRV EKILKYSQYN ERDEIPHNDI ALLKLKPVGG
HCALESRYVK TVCLPSDPFP SGTECHISGW GVTETGEGSR QLLDAKVKLI ANPLCNSRQL
YDHTIDDSMI CAGNLQKPGS DTCQGDSGGP LTCEKDGTYY VYGIVSWGQE CGKKPGVYTQ
VTKFLNWIKT TMHREAGL
//
