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Protein

Retroviral-like aspartic protease 1

Gene

Asprv1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei210 – 2101PROSITE-ProRule annotation

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  • protein processing Source: UniProtKB
  • skin development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA28.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Retroviral-like aspartic protease 1 (EC:3.4.23.-)
Alternative name(s):
Skin-specific retroviral-like aspartic protease
Short name:
SASPase
Short name:
Skin aspartic protease
TPA-inducible aspartic proteinase-like protein
Gene namesi
Name:Asprv1Imported
Synonyms:Sasp1 Publication, Taps
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1915105. Asprv1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei55 – 7521HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Mice display fine wrinkles on the lateral trunk which start to form 5 weeks after birth. There are no apparent epidermal differentiation defects.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi210 – 2101D → A: Abolishes production of active form of enzyme. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1881881 PublicationPRO_0000271173Add
BLAST
Chaini189 – 324136Retroviral-like aspartic protease 11 PublicationPRO_0000271174Add
BLAST
Propeptidei325 – 339151 PublicationPRO_0000271175Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...)Sequence analysis
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Undergoes autocleavage which is necessary for activation of the protein.1 Publication

Keywords - PTMi

Autocatalytic cleavage, Glycoprotein

Proteomic databases

MaxQBiQ09PK2.
PaxDbiQ09PK2.
PRIDEiQ09PK2.

PTM databases

PhosphoSiteiQ09PK2.

Expressioni

Tissue specificityi

Highly expressed in stratified epithelia in skin, tongue, esophagus, forestomach and vagina. Also expressed in trachea, urinary bladder and thymus. Undetectable in simple epithelia. Within the epidermis, expressed exclusively in the granular layer (at protein level). Levels are elevated in benign skin tumors but are down-regulated in squamous cell carcinomas.2 Publications

Developmental stagei

Expression is first detected at embryonic day 15.5.1 Publication

Inductioni

By 12-O-tetradecanoylphorbol-13-acetate (TPA). No TPA-induced expression is seen in mice lacking Fos.1 Publication

Gene expression databases

BgeeiQ09PK2.
CleanExiMM_ASPRV1.
GenevisibleiQ09PK2. MM.

Interactioni

Subunit structurei

Homodimer.Curated1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000046121.

Structurei

3D structure databases

ProteinModelPortaliQ09PK2.
SMRiQ09PK2. Positions 194-314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini205 – 28682Peptidase A2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 peptidase A2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFHF. Eukaryota.
ENOG410ZM0E. LUCA.
GeneTreeiENSGT00390000017260.
HOGENOMiHOG000034019.
HOVERGENiHBG080861.
InParanoidiQ09PK2.
OMAiMGKGYYL.
OrthoDBiEOG7SR4N6.
PhylomeDBiQ09PK2.
TreeFamiTF337956.

Family and domain databases

InterProiIPR001969. Aspartic_peptidase_AS.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q09PK2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNPGGPGWA SKRPLQKKQN TACLCAQQPA RHFVPAPFNS SRQGKNTAQP
60 70 80 90 100
TEPSLSSVIA PTLFCAFLYL ACVTAELPEV SRRMATSGVR SKEGRREHAF
110 120 130 140 150
VPEPFTGTNL APSLWLHRFE VIDDLNHWDH ATKLRFLKES LKGDALDVYN
160 170 180 190 200
GLSSQAQGDF SFVKQALLRA FGAPGEAFSE PEEILFANSM GKGYYLKGKV
210 220 230 240 250
GHVPVRFLVD SGAQVSVVHP ALWEEVTDGD LDTLRPFNNV VKVANGAEMK
260 270 280 290 300
ILGVWDTEIS LGKTKLKAEF LVANASAEEA IIGTDVLQDH NAVLDFEHRT
310 320 330
CTLKGKKFRL LPVGSSLEDE FDLELIEEEE GSSAPEGSH
Length:339
Mass (Da):37,174
Last modified:October 17, 2006 - v1
Checksum:i3284E246B7706D40
GO

Sequence cautioni

The sequence AAH57938.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti331 – 3311G → E in AAI08358 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ841260 mRNA. Translation: ABI23689.1.
BC057938 mRNA. Translation: AAH57938.1. Different initiation.
BC108357 mRNA. Translation: AAI08358.1.
BC119099 mRNA. Translation: AAI19100.1.
BC119101 mRNA. Translation: AAI19102.1.
AK004007 mRNA. Translation: BAB23121.2.
CCDSiCCDS39542.1.
RefSeqiNP_080690.2. NM_026414.2.
UniGeneiMm.183043.

Genome annotation databases

EnsembliENSMUST00000043400; ENSMUSP00000046121; ENSMUSG00000033508.
GeneIDi67855.
KEGGimmu:67855.
UCSCiuc009csf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ841260 mRNA. Translation: ABI23689.1.
BC057938 mRNA. Translation: AAH57938.1. Different initiation.
BC108357 mRNA. Translation: AAI08358.1.
BC119099 mRNA. Translation: AAI19100.1.
BC119101 mRNA. Translation: AAI19102.1.
AK004007 mRNA. Translation: BAB23121.2.
CCDSiCCDS39542.1.
RefSeqiNP_080690.2. NM_026414.2.
UniGeneiMm.183043.

3D structure databases

ProteinModelPortaliQ09PK2.
SMRiQ09PK2. Positions 194-314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000046121.

Protein family/group databases

MEROPSiA28.004.

PTM databases

PhosphoSiteiQ09PK2.

Proteomic databases

MaxQBiQ09PK2.
PaxDbiQ09PK2.
PRIDEiQ09PK2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043400; ENSMUSP00000046121; ENSMUSG00000033508.
GeneIDi67855.
KEGGimmu:67855.
UCSCiuc009csf.1. mouse.

Organism-specific databases

CTDi151516.
MGIiMGI:1915105. Asprv1.

Phylogenomic databases

eggNOGiENOG410IFHF. Eukaryota.
ENOG410ZM0E. LUCA.
GeneTreeiENSGT00390000017260.
HOGENOMiHOG000034019.
HOVERGENiHBG080861.
InParanoidiQ09PK2.
OMAiMGKGYYL.
OrthoDBiEOG7SR4N6.
PhylomeDBiQ09PK2.
TreeFamiTF337956.

Miscellaneous databases

ChiTaRSiAsprv1. mouse.
NextBioi325725.
PROiQ09PK2.
SOURCEiSearch...

Gene expression databases

BgeeiQ09PK2.
CleanExiMM_ASPRV1.
GenevisibleiQ09PK2. MM.

Family and domain databases

InterProiIPR001969. Aspartic_peptidase_AS.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel aspartic proteinase-like gene expressed in stratified epithelia and squamous cell carcinoma of the skin."
    Rhiemeier V., Breitenbach U., Richter K.H., Gebhardt C., Vogt I., Hartenstein B., Fuerstenberger G., Mauch C., Hess J., Angel P.
    Am. J. Pathol. 168:1354-1364(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Tissue: Skin1 Publication.
  2. "Mouse homologue of skin-specific retroviral-like aspartic protease involved in wrinkle formation."
    Matsui T., Kinoshita-Ida Y., Hayashi-Kisumi F., Hata M., Matsubara K., Chiba M., Katahira-Tayama S., Morita K., Miyachi Y., Tsukita S.
    J. Biol. Chem. 281:27512-27525(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AUTOCATALYTIC CLEAVAGE, MUTAGENESIS OF ASP-210, DISRUPTION PHENOTYPE.
    Strain: BALB/cJImported.
  3. "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] OF 3-339.
    Strain: Czech IIImported and NMRIImported.
    Tissue: Mammary glandImported.
  4. "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.
    , 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] OF 186-339.
    Strain: C57BL/6JImported.
    Tissue: EmbryoImported.

Entry informationi

Entry nameiAPRV1_MOUSE
AccessioniPrimary (citable) accession number: Q09PK2
Secondary accession number(s): Q0VEV3
, Q32P05, Q6PEP7, Q9D135
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 17, 2006
Last modified: November 11, 2015
This is version 68 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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.