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O35453 (HEPS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine protease hepsin

EC=3.4.21.106
Gene names
Name:Hpn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May mediate the activating cleavage of HGF and MST1/HGFL By similarity. Plays an essential role in cell growth and maintenance of cell morphology.

Catalytic activity

Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys.

Subcellular location

Membrane; Single-pass type II membrane protein.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Contains 1 SRCR domain.

Sequence caution

The sequence BAB22289.2 differs from that shown. Reason: Frameshift at positions 155, 191 and 233.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbasement membrane disassembly

Inferred from sequence or structural similarity. Source: UniProtKB

cholesterol homeostasis

Inferred from mutant phenotype PubMed 22912808. Source: MGI

cochlea morphogenesis

Inferred from mutant phenotype PubMed 20683358. Source: UniProtKB

detection of mechanical stimulus involved in sensory perception of sound

Inferred from mutant phenotype PubMed 17620368PubMed 17918732PubMed 20683358. Source: UniProtKB

epithelium development

Inferred from expression pattern PubMed 8346233. Source: UniProtKB

negative regulation of alkaline phosphatase activity

Inferred from mutant phenotype PubMed 22912808. Source: MGI

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of epithelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: UniProtKB

pilomotor reflex

Inferred from mutant phenotype PubMed 17620368. Source: UniProtKB

positive regulation by host of viral transcription

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from mutant phenotype PubMed 17620368. Source: UniProtKB

positive regulation of hepatocyte proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of plasminogen activation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of thyroid hormone generation

Inferred from mutant phenotype PubMed 17620368. Source: UniProtKB

potassium ion transmembrane transport

Inferred from mutant phenotype PubMed 17620368. Source: UniProtKB

proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell shape

Inferred from sequence or structural similarity. Source: UniProtKB

response to thyroid hormone

Inferred from mutant phenotype PubMed 20683358. Source: UniProtKB

sensory perception of sound

Inferred from mutant phenotype PubMed 22912808. Source: MGI

   Cellular_componentcell surface

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell junction

Inferred from mutant phenotype PubMed 17620368. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from direct assay PubMed 17918732. Source: UniProtKB

nuclear membrane

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 12744720. Source: MGI

   Molecular_functioncalcium-activated potassium channel activity

Inferred from mutant phenotype PubMed 17620368. Source: UniProtKB

scavenger receptor activity

Inferred from electronic annotation. Source: InterPro

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

serine-type exopeptidase activity

Inferred from electronic annotation. Source: InterPro

serine-type peptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O35453-1)

Also known as: 1a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Minor isoform.
Isoform 2 (identifier: O35453-2)

Also known as: 2a;

The sequence of this isoform differs from the canonical sequence as follows:
     25-44: Missing.
Note: Major isoform.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 181181Serine protease hepsin non-catalytic chain Potential
PRO_0000027843
Chain182 – 436255Serine protease hepsin catalytic chain Potential
PRO_0000027844

Regions

Topological domain1 – 3838Cytoplasmic Potential
Transmembrane39 – 5921Helical; Signal-anchor for type II membrane protein; Potential
Topological domain60 – 436377Extracellular Potential
Domain73 – 17098SRCR
Domain182 – 424243Peptidase S1

Sites

Active site2221Charge relay system By similarity
Active site2761Charge relay system By similarity
Active site3721Charge relay system By similarity

Amino acid modifications

Glycosylation1311N-linked (GlcNAc...) Potential
Disulfide bond96 ↔ 159 By similarity
Disulfide bond109 ↔ 169 By similarity
Disulfide bond138 ↔ 157 By similarity
Disulfide bond172 ↔ 296Interchain (between non-catalytic and catalytic chains) By similarity
Disulfide bond207 ↔ 223 By similarity
Disulfide bond310 ↔ 378 By similarity
Disulfide bond341 ↔ 357 By similarity
Disulfide bond368 ↔ 400 By similarity

Natural variations

Alternative sequence25 – 4420Missing in isoform 2.
VSP_007232

Experimental info

Sequence conflict851F → L in AAB84221. Ref.1
Sequence conflict2041T → Y in BAB22289. Ref.3
Sequence conflict2141G → R in BAB22289. Ref.3
Sequence conflict228 – 2292NR → ET in BAB22289. Ref.3
Sequence conflict2641P → L in BAB22289. Ref.3
Sequence conflict2811H → N in BAB22289. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (1a) [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: C0C71FFFF4D016F0

FASTA43646,821
        10         20         30         40         50         60 
MAKEDEEPGA HRGGSTCSRP QPGKGGRTAA CCSRPKVAAL IVGTLLFLTG IGAASWAIVT 

        70         80         90        100        110        120 
ILLQSDQEPL YQVQLSPGDS RLAVFDKTEG TWRLLCSSRS NARVAGLGCE EMGFLRALAH 

       130        140        150        160        170        180 
SELDVRTAGA NGTSGFFCVD EGGLPLAQRL LDVISVCDCP RGRFLTATCQ DCGRRKLPVD 

       190        200        210        220        230        240 
RIVGGQDSSL GRWPWQVSLR YDGTHLCGGS LLSGDWVLTA AHCFPERNRV LSRWRVFAGA 

       250        260        270        280        290        300 
VARTSPHAVQ LGVQAVIYHG GYLPFRDPTI DENSNDIALV HLSSSLPLTE YIQPVCLPAA 

       310        320        330        340        350        360 
GQALVDGKVC TVTGWGNTQF YGQQAMVLQE ARVPIISNEV CNSPDFYGNQ IKPKMFCAGY 

       370        380        390        400        410        420 
PEGGIDACQG DSGGPFVCED SISGTSRWRL CGIVSWGTGC ALARKPGVYT KVTDFREWIF 

       430 
KAIKTHSEAS GMVTQP 

« Hide

Isoform 2 (2a) [UniParc].

Checksum: 3689A7277E186CF6
Show »

FASTA41644,908

References

« Hide 'large scale' references
[1]"Identification and cloning of the membrane-associated serine protease, hepsin, from mouse preimplantation embryos."
Vu T.-K.H., Liu R.W., Haaksma C., Tomasek J.J., Howard E.W.
J. Biol. Chem. 272:31315-31320(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Liver.
[2]"Complete nucleotide sequence, origin of isoform and functional characterization of the mouse hepsin gene."
Kawamura S., Kurachi S., Deyashiki Y., Kurachi K.
Eur. J. Biochem. 262:755-764(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Kidney.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF030065 mRNA. Translation: AAB84221.1.
AK002694 mRNA. Translation: BAB22289.2. Frameshift.
CH466593 Genomic DNA. Translation: EDL23952.1.
BC138809 mRNA. Translation: AAI38810.1.
BC145413 mRNA. Translation: AAI45414.1.
RefSeqNP_001103722.1. NM_001110252.2.
NP_001263198.1. NM_001276269.1.
NP_032307.2. NM_008281.4.
XP_006539624.1. XM_006539561.1.
UniGeneMm.19182.

3D structure databases

ProteinModelPortalO35453.
SMRO35453. Positions 68-435.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.224.

PTM databases

PhosphoSiteO35453.

Proteomic databases

PaxDbO35453.
PRIDEO35453.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000108102; ENSMUSP00000103737; ENSMUSG00000001249. [O35453-1]
GeneID15451.
KEGGmmu:15451.
UCSCuc009gid.2. mouse. [O35453-1]

Organism-specific databases

CTD3249.
MGIMGI:1196620. Hpn.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00730000110471.
HOGENOMHOG000251822.
HOVERGENHBG013304.
KOK08665.
TreeFamTF351678.

Gene expression databases

ArrayExpressO35453.
BgeeO35453.
CleanExMM_HPN.
GenevestigatorO35453.

Family and domain databases

Gene3D3.10.250.10. 1 hit.
InterProIPR015352. Hepsin-SRCR_dom.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR017448. SRCR-like_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF09272. Hepsin-SRCR. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
ProDomPD021735. Hepsin-SRCR. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio288256.
PROO35453.
SOURCESearch...

Entry information

Entry nameHEPS_MOUSE
AccessionPrimary (citable) accession number: O35453
Secondary accession number(s): B2RSC4, Q9CW97
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot