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Protein

Hyaluronan-binding protein 2

Gene

Habp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Cleaves the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro-urokinase) to the active two chain form. Activates coagulation factor VII (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei360 – 3601Charge relay systemBy similarity
Active sitei409 – 4091Charge relay systemBy similarity
Active sitei507 – 5071Charge relay systemBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.033.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:Habp2
Synonyms:Phbp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1302979. Habp2.

Subcellular locationi

  • Secreted By similarity

  • Note: Secreted as an inactive single-chain precursor and is then activated to a heterodimeric form.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 311288Hyaluronan-binding protein 2 50 kDa heavy chainPRO_0000027907Add
BLAST
Chaini27 – 311285Hyaluronan-binding protein 2 50 kDa heavy chain alternate formBy similarityPRO_0000027908Add
BLAST
Chaini312 – 558247Hyaluronan-binding protein 2 27 kDa light chainBy similarityPRO_0000027909Add
BLAST
Chaini318 – 558241Hyaluronan-binding protein 2 27 kDa light chain alternate formBy similarityPRO_0000027910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi75 ↔ 86By similarity
Disulfide bondi80 ↔ 95By similarity
Disulfide bondi97 ↔ 106By similarity
Disulfide bondi113 ↔ 123By similarity
Disulfide bondi118 ↔ 134By similarity
Disulfide bondi136 ↔ 145By similarity
Disulfide bondi152 ↔ 163By similarity
Disulfide bondi157 ↔ 174By similarity
Disulfide bondi176 ↔ 185By similarity
Disulfide bondi192 ↔ 274By similarity
Disulfide bondi213 ↔ 255By similarity
Disulfide bondi244 ↔ 269By similarity
Disulfide bondi299 ↔ 433Interchain (between heavy and light chains)PROSITE-ProRule annotation
Disulfide bondi345 ↔ 361By similarity
Disulfide bondi445 ↔ 513By similarity
Disulfide bondi475 ↔ 491By similarity
Disulfide bondi503 ↔ 531By similarity

Post-translational modificationi

Proteolytic cleavage at Gly-23 or Met-27 can give rise to the 50 kDa heavy chain and cleavage at Arg-311 or Lys-317 can give rise to the 27 kDa light chain. The heavy chain can undergo further proteolytic cleavage at Arg-168 or Arg-169 to give rise to two inactive 26 kDa fragments and the light chain can undergo further proteolytic cleavage at Arg-478 to give rise to inactive 17 kDa and 8 kDa fragments (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei167 – 1682CleavageBy similarity
Sitei168 – 1692CleavageBy similarity
Sitei478 – 4792CleavageBy similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiQ6L711.
PRIDEiQ6L711.

Interactioni

Subunit structurei

Heterodimer; disulfide-linked. Heterodimer of a 50 kDa heavy and a 27 kDa light chain linked by a disulfide bond (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000045891.

Structurei

3D structure databases

ProteinModelPortaliQ6L711.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini71 – 10737EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini109 – 14638EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini148 – 18639EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini191 – 27484KringlePROSITE-ProRule annotationAdd
BLAST
Domaini312 – 553242Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 3 EGF-like domains.PROSITE-ProRule annotation
Contains 1 kringle domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
KOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000237314.
HOVERGENiHBG106385.
InParanoidiQ6L711.
KOiK08648.
PhylomeDBiQ6L711.

Family and domain databases

InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 2 hits.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 2 hits.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00022. EGF_1. 3 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 3 hits.
PS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6L711-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVVMLVFRV LLLIALVGNS AIGLSLMPFI APPDPDWTPD DYYYSYEQSS
60 70 80 90 100
PDKDASVTQT SPENPDWYYE DDDPCQSNPC EHGGDCIIRG NTFSCSCPAP
110 120 130 140 150
FSGSRCQTVQ NKCKDNPCVQ GDCLITQTPP YYRCACKYPY TGPDCSKVLP
160 170 180 190 200
VCRPNPCQNG GVCSRHRRRS RFSCACPDQY KGRFCEIGPD DCYVGDGYSY
210 220 230 240 250
RGKVSRTVNQ NPCLYWNSHL LLQENYNMFM EDAETHGIAD HNFCRNPDGD
260 270 280 290 300
HKPWCFVKVN SEKVKWEYCN VEVCPESDAA NPVGSLQEPV MELPGFDSCG
310 320 330 340 350
KTEMTEHAVK RIYGGFKSTA GKHPWQVSLQ TSLPLTTSMP QGHFCGGSLI
360 370 380 390 400
HPCWVLTAAH CTDMSTKHLK VVLGDQDLKK TESHEQTFRV EKILKYSQYN
410 420 430 440 450
ERDEIPHNDI ALLKLKPVGG HCALESKYVK TVCLPSDPFP SGTECHISGW
460 470 480 490 500
GVTETGEGSR QLLDAKVKLI ANALCNSRQL YDHTIDDSMI CAGNLQKPGS
510 520 530 540 550
DTCQGDSGGP LTCEKDGTYY VYGIVSWGQE CGKKPGVYTQ VTKFLNWIKT

TMHKEAGL
Length:558
Mass (Da):62,093
Last modified:July 5, 2004 - v1
Checksum:iD7CA0BB1E276D475
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB177406 mRNA. Translation: BAD19044.1.
RefSeqiNP_001001505.1. NM_001001505.1.
UniGeneiRn.161908.

Genome annotation databases

GeneIDi292126.
KEGGirno:292126.
UCSCiRGD:1302979. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB177406 mRNA. Translation: BAD19044.1.
RefSeqiNP_001001505.1. NM_001001505.1.
UniGeneiRn.161908.

3D structure databases

ProteinModelPortaliQ6L711.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000045891.

Protein family/group databases

MEROPSiS01.033.

Proteomic databases

PaxDbiQ6L711.
PRIDEiQ6L711.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi292126.
KEGGirno:292126.
UCSCiRGD:1302979. rat.

Organism-specific databases

CTDi3026.
RGDi1302979. Habp2.

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
KOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000237314.
HOVERGENiHBG106385.
InParanoidiQ6L711.
KOiK08648.
PhylomeDBiQ6L711.

Miscellaneous databases

PROiQ6L711.

Family and domain databases

InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 2 hits.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 2 hits.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00022. EGF_1. 3 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 3 hits.
PS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and expression of rat PHBP."
    Shimizu S., Satou K.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiHABP2_RAT
AccessioniPrimary (citable) accession number: Q6L711
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.