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Protein

Retroviral-like aspartic protease 1

Gene

ASPRV1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5555CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei56 – 7621HelicalSequence AnalysisAdd
BLAST
Topological domaini77 – 343267ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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. 7 interactions.
IntActiQ53RT3. 1 interaction.
STRINGi9606.ENSP00000315383.

Structurei

3D structure databases

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

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.
GeneTreeiENSGT00390000017260.
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

        10         20         30         40         50
MGSPGASLGI KKALQSEQAT ALPASAPAVS QPTAPAPSCL PKAGQVIPTL
60 70 80 90 100
LREAPFSSVI APTLLCGFLF LAWVAAEVPE ESSRMAGSGA RSEEGRRQHA
110 120 130 140 150
FVPEPFDGAN VVPNLWLHSF EVINDLNHWD HITKLRFLKE SLRGEALGVY
160 170 180 190 200
NRLSPQDQGD YGTVKEALLK AFGVPGAAPS HLPKEIVFAN SMGKGYYLKG
210 220 230 240 250
KIGKVPVRFL VDSGAQVSVV HPNLWEEVTD GDLDTLQPFE NVVKVANGAE
260 270 280 290 300
MKILGVWDTA VSLGKLKLKA QFLVANASAE EAIIGTDVLQ DHNAILDFEH
310 320 330 340
RTCTLKGKKF RLLPVGGSLE DEFDLELIEE DPSSEEGRQE LSH
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi127385. 7 interactions.
IntActiQ53RT3. 1 interaction.
STRINGi9606.ENSP00000315383.

Protein family/group databases

MEROPSiA33.001.

PTM databases

PhosphoSiteiQ53RT3.

Polymorphism databases

DMDMi74726595.

Proteomic databases

PaxDbiQ53RT3.
PRIDEiQ53RT3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi151516.
GeneCardsiGC02M070187.
H-InvDBHIX0002133.
HGNCiHGNC:26321. ASPRV1.
HPAiHPA034809.
HPA034810.
MIMi611765. gene.
neXtProtiNX_Q53RT3.
PharmGKBiPA162376919.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG45468.
GeneTreeiENSGT00390000017260.
HOGENOMiHOG000034019.
HOVERGENiHBG080861.
InParanoidiQ53RT3.
OMAiMGKGYYL.
OrthoDBiEOG7SR4N6.
PhylomeDBiQ53RT3.
TreeFamiTF337956.

Miscellaneous databases

GenomeRNAii151516.
NextBioi86714.
PROiQ53RT3.
SOURCEiSearch...

Gene expression databases

BgeeiQ53RT3.
CleanExiHS_ASPRV1.
GenevestigatoriQ53RT3.

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. "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: January 7, 2015
This is version 80 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

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 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.