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Retroviral-like aspartic protease 1 (EC 3.4.23.-) (Skin-specific retroviral-like aspartic protease) (SASPase) (Skin aspartic protease) (TPA-inducible aspartic proteinase-like protein)

 APRV1_MOUSE             Reviewed;         339 AA.
Q09PK2; Q0VEV3; Q32P05; Q6PEP7; Q9D135;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 1.
12-SEP-2018, entry version 81.
RecName: Full=Retroviral-like aspartic protease 1;
EC=3.4.23.-;
AltName: Full=Skin-specific retroviral-like aspartic protease;
Short=SASPase;
Short=Skin aspartic protease;
AltName: Full=TPA-inducible aspartic proteinase-like protein;
Flags: Precursor;
Name=Asprv1 {ECO:0000312|MGI:MGI:1915105};
Synonyms=Sasp {ECO:0000303|PubMed:16837463}, Taps;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
TISSUE=Skin {ECO:0000269|PubMed:16565508};
PubMed=16565508; DOI=10.2353/ajpath.2006.050871;
Rhiemeier V., Breitenbach U., Richter K.H., Gebhardt C., Vogt I.,
Hartenstein B., Fuerstenberger G., Mauch C., Hess J., Angel P.;
"A novel aspartic proteinase-like gene expressed in stratified
epithelia and squamous cell carcinoma of the skin.";
Am. J. Pathol. 168:1354-1364(2006).
[2] {ECO:0000305, ECO:0000312|EMBL:ABI23689.1}
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AUTOCATALYTIC CLEAVAGE, MUTAGENESIS
OF ASP-210, AND DISRUPTION PHENOTYPE.
STRAIN=BALB/cJ {ECO:0000312|EMBL:ABI23689.1};
PubMed=16837463; DOI=10.1074/jbc.M603559200;
Matsui T., Kinoshita-Ida Y., Hayashi-Kisumi F., Hata M., Matsubara K.,
Chiba M., Katahira-Tayama S., Morita K., Miyachi Y., Tsukita S.;
"Mouse homologue of skin-specific retroviral-like aspartic protease
involved in wrinkle formation.";
J. Biol. Chem. 281:27512-27525(2006).
[3] {ECO:0000305, ECO:0000312|EMBL:AAH57938.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-339.
STRAIN=Czech II {ECO:0000312|EMBL:AAI08358.1}, and
NMRI {ECO:0000312|EMBL:AAH57938.1};
TISSUE=Mammary gland {ECO:0000312|EMBL:AAH57938.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4] {ECO:0000305, ECO:0000312|EMBL:BAB23121.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 186-339.
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB23121.2};
TISSUE=Embryo {ECO:0000312|EMBL:BAB23121.2};
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16837463, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: 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.
{ECO:0000269|PubMed:16565508, ECO:0000269|PubMed:16837463}.
-!- DEVELOPMENTAL STAGE: Expression is first detected at embryonic day
15.5. {ECO:0000269|PubMed:16837463}.
-!- INDUCTION: By 12-O-tetradecanoylphorbol-13-acetate (TPA). No TPA-
induced expression is seen in mice lacking Fos.
{ECO:0000269|PubMed:16565508}.
-!- PTM: Undergoes autocleavage which is necessary for activation of
the protein. {ECO:0000269|PubMed:16837463}.
-!- DISRUPTION PHENOTYPE: Mice display fine wrinkles on the lateral
trunk which start to form 5 weeks after birth. There are no
apparent epidermal differentiation defects.
{ECO:0000269|PubMed:16837463}.
-!- SEQUENCE CAUTION:
Sequence=AAH57938.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; DQ841260; ABI23689.1; -; mRNA.
EMBL; BC057938; AAH57938.1; ALT_INIT; mRNA.
EMBL; BC108357; AAI08358.1; -; mRNA.
EMBL; BC119099; AAI19100.1; -; mRNA.
EMBL; BC119101; AAI19102.1; -; mRNA.
EMBL; AK004007; BAB23121.2; -; mRNA.
CCDS; CCDS39542.1; -.
RefSeq; NP_080690.2; NM_026414.2.
UniGene; Mm.183043; -.
ProteinModelPortal; Q09PK2; -.
SMR; Q09PK2; -.
STRING; 10090.ENSMUSP00000046121; -.
MEROPS; A28.004; -.
PhosphoSitePlus; Q09PK2; -.
MaxQB; Q09PK2; -.
PaxDb; Q09PK2; -.
PeptideAtlas; Q09PK2; -.
PRIDE; Q09PK2; -.
Ensembl; ENSMUST00000043400; ENSMUSP00000046121; ENSMUSG00000033508.
GeneID; 67855; -.
KEGG; mmu:67855; -.
UCSC; uc009csf.1; mouse.
CTD; 151516; -.
MGI; MGI:1915105; Asprv1.
eggNOG; ENOG410IFHF; Eukaryota.
eggNOG; ENOG410ZM0E; LUCA.
GeneTree; ENSGT00390000017260; -.
HOGENOM; HOG000034019; -.
HOVERGEN; HBG080861; -.
InParanoid; Q09PK2; -.
OMA; MGKGYYL; -.
OrthoDB; EOG091G0NU5; -.
PhylomeDB; Q09PK2; -.
TreeFam; TF337956; -.
ChiTaRS; Asprv1; mouse.
PRO; PR:Q09PK2; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000033508; Expressed in 71 organ(s), highest expression level in skin epidermis.
CleanEx; MM_ASPRV1; -.
Genevisible; Q09PK2; MM.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0016485; P:protein processing; IDA:UniProtKB.
GO; GO:0043588; P:skin development; IMP:UniProtKB.
Gene3D; 2.40.70.10; -; 1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR033539; Asprv1.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
PANTHER; PTHR37006; PTHR37006; 1.
SUPFAM; SSF50630; SSF50630; 1.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
1: Evidence at protein level;
Aspartyl protease; Autocatalytic cleavage; Complete proteome;
Direct protein sequencing; Glycoprotein; Hydrolase; Membrane;
Protease; Reference proteome; Transmembrane; Transmembrane helix.
PROPEP 1 188 {ECO:0000269|PubMed:16837463}.
/FTId=PRO_0000271173.
CHAIN 189 324 Retroviral-like aspartic protease 1.
{ECO:0000269|PubMed:16837463}.
/FTId=PRO_0000271174.
PROPEP 325 339 {ECO:0000269|PubMed:16837463}.
/FTId=PRO_0000271175.
TRANSMEM 55 75 Helical. {ECO:0000255}.
DOMAIN 205 286 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
ACT_SITE 210 210 {ECO:0000255|PROSITE-ProRule:PRU10094}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 274 274 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 210 210 D->A: Abolishes production of active form
of enzyme. {ECO:0000269|PubMed:16837463}.
CONFLICT 331 331 G -> E (in Ref. 3; AAI08358).
{ECO:0000305}.
SEQUENCE 339 AA; 37174 MW; 3284E246B7706D40 CRC64;
MRNPGGPGWA SKRPLQKKQN TACLCAQQPA RHFVPAPFNS SRQGKNTAQP TEPSLSSVIA
PTLFCAFLYL ACVTAELPEV SRRMATSGVR SKEGRREHAF VPEPFTGTNL APSLWLHRFE
VIDDLNHWDH ATKLRFLKES LKGDALDVYN GLSSQAQGDF SFVKQALLRA FGAPGEAFSE
PEEILFANSM GKGYYLKGKV GHVPVRFLVD SGAQVSVVHP ALWEEVTDGD LDTLRPFNNV
VKVANGAEMK ILGVWDTEIS LGKTKLKAEF LVANASAEEA IIGTDVLQDH NAVLDFEHRT
CTLKGKKFRL LPVGSSLEDE FDLELIEEEE GSSAPEGSH


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