APRV1_MOUSE
ID APRV1_MOUSE Reviewed; 339 AA.
AC Q09PK2; Q0VEV3; Q32P05; Q6PEP7; Q9D135;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Retroviral-like aspartic protease 1;
DE EC=3.4.23.-;
DE AltName: Full=Skin-specific retroviral-like aspartic protease;
DE Short=SASPase;
DE Short=Skin aspartic protease;
DE AltName: Full=TPA-inducible aspartic proteinase-like protein;
DE Flags: Precursor;
GN Name=Asprv1 {ECO:0000312|MGI:MGI:1915105};
GN Synonyms=Sasp {ECO:0000303|PubMed:16837463}, Taps;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Skin {ECO:0000269|PubMed:16565508};
RX PubMed=16565508; DOI=10.2353/ajpath.2006.050871;
RA Rhiemeier V., Breitenbach U., Richter K.H., Gebhardt C., Vogt I.,
RA Hartenstein B., Fuerstenberger G., Mauch C., Hess J., Angel P.;
RT "A novel aspartic proteinase-like gene expressed in stratified epithelia
RT and squamous cell carcinoma of the skin.";
RL Am. J. Pathol. 168:1354-1364(2006).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABI23689.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AUTOCATALYTIC CLEAVAGE, MUTAGENESIS OF ASP-210, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:ABI23689.1};
RX PubMed=16837463; DOI=10.1074/jbc.m603559200;
RA Matsui T., Kinoshita-Ida Y., Hayashi-Kisumi F., Hata M., Matsubara K.,
RA Chiba M., Katahira-Tayama S., Morita K., Miyachi Y., Tsukita S.;
RT "Mouse homologue of skin-specific retroviral-like aspartic protease
RT involved in wrinkle formation.";
RL J. Biol. Chem. 281:27512-27525(2006).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH57938.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-339.
RC STRAIN=Czech II {ECO:0000312|EMBL:AAI08358.1}, and
RC NMRI {ECO:0000312|EMBL:AAH57938.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH57938.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAB23121.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 186-339.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB23121.2};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB23121.2};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Protease responsible for filaggrin processing, essential for
CC the maintenance of a proper epidermis organization.
CC {ECO:0000250|UniProtKB:Q53RT3}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16837463, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in stratified epithelia in skin,
CC tongue, esophagus, forestomach and vagina. Also expressed in trachea,
CC urinary bladder and thymus. Undetectable in simple epithelia. Within
CC the epidermis, expressed exclusively in the granular layer (at protein
CC level). Levels are elevated in benign skin tumors but are down-
CC regulated in squamous cell carcinomas. {ECO:0000269|PubMed:16565508,
CC ECO:0000269|PubMed:16837463}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected at embryonic day
CC 15.5. {ECO:0000269|PubMed:16837463}.
CC -!- INDUCTION: By 12-O-tetradecanoylphorbol-13-acetate (TPA). No TPA-
CC induced expression is seen in mice lacking Fos.
CC {ECO:0000269|PubMed:16565508}.
CC -!- PTM: Undergoes autocleavage which is necessary for activation of the
CC protein. {ECO:0000269|PubMed:16837463}.
CC -!- DISRUPTION PHENOTYPE: Mice display fine wrinkles on the lateral trunk
CC which start to form 5 weeks after birth. There are no apparent
CC epidermal differentiation defects. {ECO:0000269|PubMed:16837463}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57938.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ841260; ABI23689.1; -; mRNA.
DR EMBL; BC057938; AAH57938.1; ALT_INIT; mRNA.
DR EMBL; BC108357; AAI08358.1; -; mRNA.
DR EMBL; BC119099; AAI19100.1; -; mRNA.
DR EMBL; BC119101; AAI19102.1; -; mRNA.
DR EMBL; AK004007; BAB23121.2; -; mRNA.
DR RefSeq; NP_080690.2; NM_026414.2.
DR AlphaFoldDB; Q09PK2; -.
DR SMR; Q09PK2; -.
DR BioGRID; 212483; 4.
DR STRING; 10090.ENSMUSP00000046121; -.
DR MEROPS; A28.004; -.
DR GlyGen; Q09PK2; 2 sites.
DR PhosphoSitePlus; Q09PK2; -.
DR MaxQB; Q09PK2; -.
DR PaxDb; Q09PK2; -.
DR PeptideAtlas; Q09PK2; -.
DR PRIDE; Q09PK2; -.
DR ProteomicsDB; 296272; -.
DR Antibodypedia; 31062; 79 antibodies from 23 providers.
DR DNASU; 67855; -.
DR GeneID; 67855; -.
DR KEGG; mmu:67855; -.
DR UCSC; uc009csf.1; mouse.
DR CTD; 151516; -.
DR MGI; MGI:1915105; Asprv1.
DR VEuPathDB; HostDB:ENSMUSG00000033508; -.
DR eggNOG; ENOG502SQVT; Eukaryota.
DR HOGENOM; CLU_846072_0_0_1; -.
DR InParanoid; Q09PK2; -.
DR OrthoDB; 1105506at2759; -.
DR PhylomeDB; Q09PK2; -.
DR TreeFam; TF337956; -.
DR BioGRID-ORCS; 67855; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Asprv1; mouse.
DR PRO; PR:Q09PK2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q09PK2; protein.
DR Genevisible; Q09PK2; MM.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0016485; P:protein processing; IDA:UniProtKB.
DR GO; GO:0043588; P:skin development; IMP:UniProtKB.
DR Gene3D; 2.40.70.10; -; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033539; Asprv1.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR37006; PTHR37006; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Autocatalytic cleavage; Direct protein sequencing;
KW Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT PROPEP 1..188
FT /evidence="ECO:0000269|PubMed:16837463"
FT /id="PRO_0000271173"
FT CHAIN 189..324
FT /note="Retroviral-like aspartic protease 1"
FT /evidence="ECO:0000269|PubMed:16837463"
FT /id="PRO_0000271174"
FT PROPEP 325..339
FT /evidence="ECO:0000269|PubMed:16837463"
FT /id="PRO_0000271175"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 205..286
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT REGION 34..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 210
FT /note="D->A: Abolishes production of active form of
FT enzyme."
FT /evidence="ECO:0000269|PubMed:16837463"
FT CONFLICT 331
FT /note="G -> E (in Ref. 3; AAI08358)"
FT /evidence="ECO:0000305"
SQ 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
