Gene
hpn
- ID
- ZDB-GENE-141212-373
- Name
- hepsin
- Symbol
- hpn Nomenclature History
- Previous Names
-
- si:ch73-124g13.3 (1)
- Type
- protein_coding_gene
- Location
- Chr: 16 Mapping Details/Browsers
- Description
- Predicted to enable serine-type endopeptidase activity and serine-type exopeptidase activity. Acts upstream of or within blood coagulation, fibrin clot formation and regulation of serine-type endopeptidase activity. Predicted to be located in membrane. Human ortholog(s) of this gene implicated in intellectual disability. Orthologous to human HPN (hepsin).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- No data available
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
- No data available
Wild Type Expression Summary
- All Phenotype Data
- 3 figures from Khandekar et al., 2014
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
No data available
Human Disease
Domain, Family, and Site Summary
Type | InterPro ID | Name |
---|---|---|
Active_site | IPR018114 | Serine proteases, trypsin family, histidine active site |
Active_site | IPR033116 | Serine proteases, trypsin family, serine active site |
Domain | IPR001190 | SRCR domain |
Domain | IPR001254 | Serine proteases, trypsin domain |
Domain | IPR015352 | Hepsin, SRCR domain |
Family | IPR001314 | Peptidase S1A, chymotrypsin family |
Homologous_superfamily | IPR009003 | Peptidase S1, PA clan |
Homologous_superfamily | IPR036772 | SRCR-like domain superfamily |
Homologous_superfamily | IPR043504 | Peptidase S1, PA clan, chymotrypsin-like fold |
Domain Details Per Protein
Protein | Additional Resources | Length | Hepsin, SRCR domain | Peptidase S1A, chymotrypsin family | Peptidase S1, PA clan | Peptidase S1, PA clan, chymotrypsin-like fold | Serine proteases, trypsin domain | Serine proteases, trypsin family, histidine active site | Serine proteases, trypsin family, serine active site | SRCR domain | SRCR-like domain superfamily |
---|---|---|---|---|---|---|---|---|---|---|---|
UniProtKB:A8DZG9 | InterPro | 425 | |||||||||
UniProtKB:A5D6S2 | InterPro | 423 | |||||||||
UniProtKB:A0A8M9PJK7 | InterPro | 413 |
Interactions and Pathways
No data available
Plasmids
No data available
No data available
Relationship | Marker Type | Marker | Accession Numbers | Citations |
---|---|---|---|---|
Contained in | BAC | CH73-124G13 | ZFIN Curated Data | |
Contained in | BAC | DKEY-33I11 | ZFIN Curated Data | |
Encodes | cDNA | MGC:162190 | ZFIN Curated Data |
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Type | Accession # | Sequence | Length (nt/aa) | Analysis |
---|---|---|---|---|
RNA | RefSeq:NM_001098187 (1) | 5798 nt | ||
Genomic | GenBank:AL953842 (2) | 225654 nt | ||
Polypeptide | UniProtKB:A8DZG9 (2) | 425 aa |
- Khandekar, G., and Jagadeeswaran, P. (2014) Role of hepsin in factor VII activation in zebrafish. Blood cells, molecules & diseases. 52(1):76-81
- Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G., Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D., Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K., Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F., Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L., Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L., Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S., Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J., Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J., McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S., Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W., Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A., Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y., Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M., Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E., Schnerch,A., Schein,J.E., Jones,S.J., and Marra,M.A. (2002) Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America. 99(26):16899-903
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