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Q53RT3

- APRV1_HUMAN

UniProt

Q53RT3 - APRV1_HUMAN

Protein

Retroviral-like aspartic protease 1

Gene

ASPRV1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    Functioni

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei212 – 2121PROSITE-ProRule annotation

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. protein processing Source: UniProtKB
    2. skin development Source: UniProtKB

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Protein family/group databases

    MEROPSiA33.001.

    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
    Short name:
    TAPS
    Gene namesi
    Name:ASPRV1By similarity
    Synonyms:SASP1 Publication
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:26321. ASPRV1.

    Subcellular locationi

    Membrane Sequence Analysis; Single-pass membrane protein Sequence Analysis

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi212 – 2121D → A or E: Abolishes production of active form of enzyme. 1 Publication

    Organism-specific databases

    PharmGKBiPA162376919.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 1901901 PublicationPRO_0000271170Add
    BLAST
    Chaini191 – 326136Retroviral-like aspartic protease 11 PublicationPRO_0000271171Add
    BLAST
    Propeptidei327 – 343171 PublicationPRO_0000271172Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi276 – 2761N-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

    PaxDbiQ53RT3.
    PRIDEiQ53RT3.

    PTM databases

    PhosphoSiteiQ53RT3.

    Expressioni

    Tissue specificityi

    Expressed primarily in the granular layer of the epidermis and inner root sheath of hair follicles. In psoriatic skin, expressed throughout the stratum corneum. In ulcerated skin, expressed in the stratum granulosum of intact epidermis but almost absent from ulcerated regions. Expressed in differentiated areas of squamous cell carcinomas but not in undifferentiated tumors.2 Publications

    Gene expression databases

    BgeeiQ53RT3.
    CleanExiHS_ASPRV1.
    GenevestigatoriQ53RT3.

    Organism-specific databases

    HPAiHPA034809.
    HPA034810.

    Interactioni

    Subunit structurei

    Homodimer.By similarityCurated

    Protein-protein interaction databases

    BioGridi127385. 2 interactions.
    IntActiQ53RT3. 1 interaction.
    STRINGi9606.ENSP00000315383.

    Structurei

    3D structure databases

    ProteinModelPortaliQ53RT3.
    SMRiQ53RT3. Positions 197-305.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5555CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini77 – 343267ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei56 – 7621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini207 – 28882Peptidase A2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 peptidase A2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG45468.
    HOGENOMiHOG000034019.
    HOVERGENiHBG080861.
    InParanoidiQ53RT3.
    OMAiMGKGYYL.
    OrthoDBiEOG7SR4N6.
    PhylomeDBiQ53RT3.
    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.

    Q53RT3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSPGASLGI KKALQSEQAT ALPASAPAVS QPTAPAPSCL PKAGQVIPTL    50
    LREAPFSSVI APTLLCGFLF LAWVAAEVPE ESSRMAGSGA RSEEGRRQHA 100
    FVPEPFDGAN VVPNLWLHSF EVINDLNHWD HITKLRFLKE SLRGEALGVY 150
    NRLSPQDQGD YGTVKEALLK AFGVPGAAPS HLPKEIVFAN SMGKGYYLKG 200
    KIGKVPVRFL VDSGAQVSVV HPNLWEEVTD GDLDTLQPFE NVVKVANGAE 250
    MKILGVWDTA VSLGKLKLKA QFLVANASAE EAIIGTDVLQ DHNAILDFEH 300
    RTCTLKGKKF RLLPVGGSLE DEFDLELIEE DPSSEEGRQE LSH 343
    Length:343
    Mass (Da):36,991
    Last modified:May 24, 2005 - v1
    Checksum:i439BAC407F5EBCCB
    GO

    Sequence cautioni

    The sequence BAB71587.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311Q → R in BAB71587. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti49 – 491T → A.2 Publications
    Corresponds to variant rs3796097 [ dbSNP | Ensembl ].
    VAR_051508

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK055994 mRNA. Translation: BAB71067.1.
    AK057813 mRNA. Translation: BAB71587.1. Different initiation.
    AC079811 Genomic DNA. Translation: AAY24017.1.
    BC031997 mRNA. Translation: AAH31997.2.
    BC094002 mRNA. Translation: AAH94002.1.
    BC094000 mRNA. Translation: AAH94000.1.
    CCDSiCCDS1897.1.
    RefSeqiNP_690005.2. NM_152792.2.
    UniGeneiHs.516253.

    Genome annotation databases

    EnsembliENST00000320256; ENSP00000315383; ENSG00000244617.
    GeneIDi151516.
    KEGGihsa:151516.
    UCSCiuc002sfz.4. human.

    Polymorphism databases

    DMDMi74726595.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK055994 mRNA. Translation: BAB71067.1 .
    AK057813 mRNA. Translation: BAB71587.1 . Different initiation.
    AC079811 Genomic DNA. Translation: AAY24017.1 .
    BC031997 mRNA. Translation: AAH31997.2 .
    BC094002 mRNA. Translation: AAH94002.1 .
    BC094000 mRNA. Translation: AAH94000.1 .
    CCDSi CCDS1897.1.
    RefSeqi NP_690005.2. NM_152792.2.
    UniGenei Hs.516253.

    3D structure databases

    ProteinModelPortali Q53RT3.
    SMRi Q53RT3. Positions 197-305.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127385. 2 interactions.
    IntActi Q53RT3. 1 interaction.
    STRINGi 9606.ENSP00000315383.

    Protein family/group databases

    MEROPSi A33.001.

    PTM databases

    PhosphoSitei Q53RT3.

    Polymorphism databases

    DMDMi 74726595.

    Proteomic databases

    PaxDbi Q53RT3.
    PRIDEi Q53RT3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000320256 ; ENSP00000315383 ; ENSG00000244617 .
    GeneIDi 151516.
    KEGGi hsa:151516.
    UCSCi uc002sfz.4. human.

    Organism-specific databases

    CTDi 151516.
    GeneCardsi GC02M070187.
    H-InvDB HIX0002133.
    HGNCi HGNC:26321. ASPRV1.
    HPAi HPA034809.
    HPA034810.
    MIMi 611765. gene.
    neXtProti NX_Q53RT3.
    PharmGKBi PA162376919.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45468.
    HOGENOMi HOG000034019.
    HOVERGENi HBG080861.
    InParanoidi Q53RT3.
    OMAi MGKGYYL.
    OrthoDBi EOG7SR4N6.
    PhylomeDBi Q53RT3.
    TreeFami TF337956.

    Miscellaneous databases

    GenomeRNAii 151516.
    NextBioi 86714.
    PROi Q53RT3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q53RT3.
    CleanExi HS_ASPRV1.
    Genevestigatori Q53RT3.

    Family and domain databases

    InterProi IPR001969. Aspartic_peptidase_AS.
    IPR001995. Peptidase_A2_cat.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view ]
    SUPFAMi SSF50630. SSF50630. 1 hit.
    PROSITEi PS50175. ASP_PROT_RETROV. 1 hit.
    PS00141. ASP_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a novel retroviral-like aspartic protease specifically expressed in human epidermis."
      Bernard D., Mehul B., Thomas-Collignon A., Delattre C., Donovan M., Schmidt R.
      J. Invest. Dermatol. 125:278-287(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, AUTOCATALYTIC CLEAVAGE, MUTAGENESIS OF ASP-212.
      Tissue: Epidermis1 Publication.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-49.
      Tissue: CerebellumImported and TeratocarcinomaImported.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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], VARIANT ALA-49.
      Tissue: Skin.
    5. "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: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiAPRV1_HUMAN
    AccessioniPrimary (citable) accession number: Q53RT3
    Secondary accession number(s): Q8N5P2, Q96LT3, Q96N43
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3