HABP2_BOVIN
ID HABP2_BOVIN Reviewed; 558 AA.
AC Q5E9Z2; Q3MHK6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Hyaluronan-binding protein 2;
DE EC=3.4.21.-;
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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 Leu-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 (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; BT020777; AAX08794.1; -; mRNA.
DR EMBL; BC105202; AAI05203.1; -; mRNA.
DR RefSeq; NP_001014868.1; NM_001014868.1.
DR AlphaFoldDB; Q5E9Z2; -.
DR SMR; Q5E9Z2; -.
DR STRING; 9913.ENSBTAP00000025732; -.
DR MEROPS; S01.033; -.
DR PaxDb; Q5E9Z2; -.
DR Ensembl; ENSBTAT00000025732; ENSBTAP00000025732; ENSBTAG00000019322.
DR GeneID; 507993; -.
DR KEGG; bta:507993; -.
DR CTD; 3026; -.
DR VEuPathDB; HostDB:ENSBTAG00000019322; -.
DR VGNC; VGNC:55955; HABP2.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000157814; -.
DR HOGENOM; CLU_006842_18_2_1; -.
DR InParanoid; Q5E9Z2; -.
DR OMA; GKTACGF; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF329901; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000019322; Expressed in laryngeal cartilage and 40 other tissues.
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; IEA:InterPro.
DR GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Glycoprotein; Hydrolase; Kringle; Protease; Reference proteome; Repeat;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..311
FT /note="Hyaluronan-binding protein 2 50 kDa heavy chain"
FT /id="PRO_0000027895"
FT CHAIN 27..311
FT /note="Hyaluronan-binding protein 2 50 kDa heavy chain
FT alternate form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027896"
FT CHAIN 312..558
FT /note="Hyaluronan-binding protein 2 27 kDa light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027897"
FT CHAIN 318..558
FT /note="Hyaluronan-binding protein 2 27 kDa light chain
FT alternate form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027898"
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 CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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; 62441 MW; EB9C40217B9C94A0 CRC64;
MFARMSDLHV LLLMVLAGKT AFGLSLLSFL TEPDPDWTPD QYEYSQEYNN QEENASSTTA
YSDNPDWYYE EDDPCLSNPC THGGDCLVSG ATFTCRCPDP FSGNRCQNVQ NKCKNNPCGR
GDCLITQSPP YHRCACKHPY RGSDCSRVVP VCRPNPCQNG GTCSRQRRRS KFTCACPDQF
KGKLCEIGPD DCYVDDGYSY RGRVSKTIHQ HTCLYWNSHL LLQEKYNMFM EDAEAHGIGE
HNFCRNPDGD KKPWCFIKVN NVKVKWEYCD VPACSALDVA NPEGRPTEPL TKFPEFGSCG
RTEIAEKKVK RIFGGFKSTA GKHPWQASLQ TSLRLTVSTP QGHYCGGALI HPCWVLTAAH
CTEIKTKYLK VVLGDQDLTK TEFHEQSFGV QKIFKYSHYI EIDDIPYNDI ALLKLKPVDG
HCALESKYVK TVCLPDGPFL SGTECYISGW GVTETGEGSR HLLDAKVKLI SNTICNSRQL
YDHSIDDNMI CAGNLQKPGQ DSCQGDSGGP LTCEKDGTSY IYGIVSWGLE CGKRPGVYTQ
VTKFLTWIKA TMEKEASF
