ID F7E1Z0_ORNAN Unreviewed; 408 AA.
AC F7E1Z0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=Napsin A aspartic peptidase {ECO:0000313|Ensembl:ENSOANP00000019807.4};
GN Name=NAPSA {ECO:0000313|Ensembl:ENSOANP00000019807.4};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000019807.4, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000019807.4, ECO:0000313|Proteomes:UP000002279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000019807.4,
RC ECO:0000313|Proteomes:UP000002279};
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2] {ECO:0000313|Ensembl:ENSOANP00000019807.4}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000019807.4};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR AlphaFoldDB; F7E1Z0; -.
DR STRING; 9258.ENSOANP00000019807; -.
DR MEROPS; A01.046; -.
DR Ensembl; ENSOANT00000019810.4; ENSOANP00000019807.4; ENSOANG00000012522.4.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000160179; -.
DR HOGENOM; CLU_013253_3_3_1; -.
DR InParanoid; F7E1Z0; -.
DR OMA; DYVIQIS; -.
DR OrthoDB; 1120702at2759; -.
DR TreeFam; TF314990; -.
DR Proteomes; UP000002279; Chromosome 10.
DR Bgee; ENSOANG00000012522; Expressed in adult mammalian kidney and 6 other cell types or tissues.
DR GO; GO:0097208; C:alveolar lamellar body; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0033619; P:membrane protein proteolysis; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0043129; P:surfactant homeostasis; IEA:Ensembl.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..408
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028212272"
FT DOMAIN 80..397
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 285
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 111..118
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 276..280
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 408 AA; 44108 MW; 7871BAE029FD9F62 CRC64;
MLRLRLLLLL LSAPLAGPAL LRIPLRRGRS VHRTLDALGD VSREWTALEA PDPPGPTSGN
PQPHNEPVLE PLTNYLDAQY FGEIGLGTPP QHFSVVFDTG SSNLWVPSRH CSFFNLACWL
HRRYDSSASS SFHPNGSHFA IRYGTGRLDG FLSQETLTIG KLQGKAVPFG EAVHQPGLVF
ILAHFDGILG LGYPALAAAG AQPVFDALLE QGLLDAPIFS FYFNRDPTGE EGGELVLGGT
DPAHYTGELH FLNVTRKAYW QIQMDEVAVG PQLTLCKGGC QAIVDTGTSL ITGPSPEIRA
LQRAIGALPV FGGEYMVPCE TLPSLPVVSF QLGGVWFNLT AEQYVLKITR LGTGVCLSGF
LGLDIPPPAG PLWILGDVFL GPHYTVFDRQ RDRVGLARAQ ARSRRGGP
//