NAPSA_MOUSE
ID NAPSA_MOUSE Reviewed; 419 AA.
AC O09043;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Napsin-A;
DE EC=3.4.23.-;
DE AltName: Full=KDAP-1;
DE AltName: Full=Kidney-derived aspartic protease-like protein;
DE Short=KAP;
DE Flags: Precursor;
GN Name=Napsa; Synonyms=Kdap, Nap;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RX PubMed=9013890; DOI=10.1016/s0014-5793(96)01473-1;
RA Mori K., Ogawa Y., Tamura N., Ebihara K., Aoki T., Muro S., Ozaki S.,
RA Tanaka I., Tashiro K., Nakao K.;
RT "Molecular cloning of a novel mouse aspartic protease-like protein that is
RT expressed abundantly in the kidney.";
RL FEBS Lett. 401:218-222(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=11082205; DOI=10.1046/j.1432-1033.2000.01795.x;
RA Tatnell P.J., Cook M., Peters C., Kay J.;
RT "Molecular organization, expression and chromosomal localization of the
RT mouse pronapsin gene.";
RL Eur. J. Biochem. 267:6921-6930(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be involved in processing of pneumocyte surfactant
CC precursors. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at the highest levels in the kidney, at a
CC moderate level in the lung, and at low levels in the spleen and adipose
CC tissue. {ECO:0000269|PubMed:9013890}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; D88899; BAA19004.1; -; mRNA.
DR EMBL; AJ250718; CAB82907.1; -; Genomic_DNA.
DR EMBL; AJ250719; CAB82907.1; JOINED; Genomic_DNA.
DR EMBL; AJ250720; CAB82907.1; JOINED; Genomic_DNA.
DR EMBL; BC014813; AAH14813.1; -; mRNA.
DR CCDS; CCDS21212.1; -.
DR RefSeq; NP_032463.1; NM_008437.1.
DR AlphaFoldDB; O09043; -.
DR SMR; O09043; -.
DR STRING; 10090.ENSMUSP00000002274; -.
DR MEROPS; A01.046; -.
DR GlyGen; O09043; 4 sites.
DR iPTMnet; O09043; -.
DR PhosphoSitePlus; O09043; -.
DR EPD; O09043; -.
DR jPOST; O09043; -.
DR PaxDb; O09043; -.
DR PeptideAtlas; O09043; -.
DR PRIDE; O09043; -.
DR ProteomicsDB; 287436; -.
DR Antibodypedia; 3755; 834 antibodies from 40 providers.
DR DNASU; 16541; -.
DR Ensembl; ENSMUST00000002274; ENSMUSP00000002274; ENSMUSG00000002204.
DR GeneID; 16541; -.
DR KEGG; mmu:16541; -.
DR UCSC; uc009gqe.1; mouse.
DR CTD; 9476; -.
DR MGI; MGI:109365; Napsa.
DR VEuPathDB; HostDB:ENSMUSG00000002204; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000160179; -.
DR HOGENOM; CLU_013253_3_3_1; -.
DR InParanoid; O09043; -.
DR OMA; PSIRCHF; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; O09043; -.
DR TreeFam; TF314990; -.
DR BRENDA; 3.4.23.B1; 3474.
DR Reactome; R-MMU-5683826; Surfactant metabolism.
DR BioGRID-ORCS; 16541; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Napsa; mouse.
DR PRO; PR:O09043; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O09043; protein.
DR Bgee; ENSMUSG00000002204; Expressed in right kidney and 115 other tissues.
DR ExpressionAtlas; O09043; baseline and differential.
DR Genevisible; O09043; MM.
DR GO; GO:0097208; C:alveolar lamellar body; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0033619; P:membrane protein proteolysis; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0043129; P:surfactant homeostasis; ISO:MGI.
DR Gene3D; 2.40.70.10; -; 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; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..?
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000025998"
FT CHAIN ?..419
FT /note="Napsin-A"
FT /id="PRO_0000025999"
FT DOMAIN 73..394
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 391..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..111
FT /evidence="ECO:0000250"
FT DISULFID 269..273
FT /evidence="ECO:0000250"
FT DISULFID 312..349
FT /evidence="ECO:0000250"
SQ SEQUENCE 419 AA; 45544 MW; 715ED4532791143E CRC64;
MSPLLLLLLC LLLGNLEPEE AKLIRVPLQR IHLGHRILNP LNGWEQLAEL SRTSTSGGNP
SFVPLSKFMN TQYFGTIGLG TPPQNFTVVF DTGSSNLWVP STRCHFFSLA CWFHHRFNPK
ASSSFRPNGT KFAIQYGTGR LSGILSQDNL TIGGIHDAFV TFGEALWEPS LIFALAHFDG
ILGLGFPTLA VGGVQPPLDA MVEQGLLEKP VFSFYLNRDS EGSDGGELVL GGSDPAHYVP
PLTFIPVTIP AYWQVHMESV KVGTGLSLCA QGCSAILDTG TSLITGPSEE IRALNKAIGG
YPFLNGQYFI QCSKTPTLPP VSFHLGGVWF NLTGQDYVIK ILQSDVGLCL LGFQALDIPK
PAGPLWILGD VFLGPYVAVF DRGDKNVGPR VGLARAQSRS TDRAERRTTQ AQFFKRRPG
