NAPSA_HUMAN
ID NAPSA_HUMAN Reviewed; 420 AA.
AC O96009; Q8WWD9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Napsin-A;
DE EC=3.4.23.-;
DE AltName: Full=Aspartyl protease 4;
DE Short=ASP4;
DE Short=Asp 4;
DE AltName: Full=Napsin-1;
DE AltName: Full=TA01/TA02;
DE Flags: Precursor;
GN Name=NAPSA; Synonyms=NAP1, NAPA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney, and Lung;
RX PubMed=9877162; DOI=10.1016/s0014-5793(98)01522-1;
RA Tatnell P.J., Powell D.J., Hill J., Smith T.S., Tew D.G., Kay J.;
RT "Napsins: new human aspartic proteinases. Distinction between two closely
RT related genes.";
RL FEBS Lett. 441:43-48(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Fetal lung;
RX PubMed=10580105; DOI=10.1016/s0014-5793(99)01493-3;
RA Chuman Y., Bergman A.-C., Ueno T., Saito S., Sakaguchi K., Alaiya A.A.,
RA Franzen B., Bergman T., Arnott D., Auer G., Appella E., Joernvall H.,
RA Linder S.;
RT "Napsin A, a member of the aspartic protease family, is abundantly
RT expressed in normal lung and kidney tissue and is expressed in lung
RT adenocarcinomas.";
RL FEBS Lett. 462:129-134(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10591213; DOI=10.1038/990107;
RA Yan R., Bienkowski M.J., Shuck M.E., Miao H., Tory M.C., Pauley A.M.,
RA Brashier J.R., Stratman N.C., Mathews W.R., Buhl A.E., Carter D.B.,
RA Tomasselli A.G., Parodi L.A., Heinrikson R.L., Gurney M.E.;
RT "Membrane-anchored aspartyl protease with Alzheimer's disease beta-
RT secretase activity.";
RL Nature 402:533-537(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Koelsch G., Wu S., Henthorn J., Tang J., Lin X.;
RT "New human aspartic proteases napsin 1 and napsin 2: molecular cloning and
RT intracellular localization of napsin 1.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-40.
RC TISSUE=Lung;
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).
CC -!- FUNCTION: May be involved in processing of pneumocyte surfactant
CC precursors.
CC -!- INTERACTION:
CC O96009; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-7196415, EBI-10245913;
CC O96009; Q5TA76: LCE3A; NbExp=3; IntAct=EBI-7196415, EBI-9394625;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in adult lung (type II
CC pneumocytes) and kidney and in fetal lung. Low levels in adult spleen
CC and very low levels in peripheral blood leukocytes.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AF090386; AAD04917.1; -; mRNA.
DR EMBL; AF200345; AAF17081.1; -; mRNA.
DR EMBL; AF098484; AAD13215.1; -; mRNA.
DR EMBL; BC017842; AAH17842.1; -; mRNA.
DR CCDS; CCDS12794.1; -.
DR RefSeq; NP_004842.1; NM_004851.2.
DR RefSeq; XP_011525842.1; XM_011527540.1.
DR AlphaFoldDB; O96009; -.
DR SMR; O96009; -.
DR BioGRID; 114861; 10.
DR IntAct; O96009; 8.
DR MINT; O96009; -.
DR STRING; 9606.ENSP00000253719; -.
DR MEROPS; A01.046; -.
DR GlyGen; O96009; 3 sites.
DR iPTMnet; O96009; -.
DR PhosphoSitePlus; O96009; -.
DR SwissPalm; O96009; -.
DR BioMuta; NAPSA; -.
DR EPD; O96009; -.
DR jPOST; O96009; -.
DR MassIVE; O96009; -.
DR PaxDb; O96009; -.
DR PeptideAtlas; O96009; -.
DR PRIDE; O96009; -.
DR ProteomicsDB; 51189; -.
DR Antibodypedia; 3755; 834 antibodies from 40 providers.
DR DNASU; 9476; -.
DR Ensembl; ENST00000253719.7; ENSP00000253719.1; ENSG00000131400.8.
DR GeneID; 9476; -.
DR KEGG; hsa:9476; -.
DR MANE-Select; ENST00000253719.7; ENSP00000253719.1; NM_004851.3; NP_004842.1.
DR UCSC; uc002prx.4; human.
DR CTD; 9476; -.
DR DisGeNET; 9476; -.
DR GeneCards; NAPSA; -.
DR HGNC; HGNC:13395; NAPSA.
DR HPA; ENSG00000131400; Tissue enriched (lung).
DR MIM; 605631; gene.
DR neXtProt; NX_O96009; -.
DR OpenTargets; ENSG00000131400; -.
DR PharmGKB; PA134891814; -.
DR VEuPathDB; HostDB:ENSG00000131400; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000160179; -.
DR InParanoid; O96009; -.
DR OMA; PSIRCHF; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; O96009; -.
DR TreeFam; TF314990; -.
DR BRENDA; 3.4.23.B1; 2681.
DR PathwayCommons; O96009; -.
DR Reactome; R-HSA-5683826; Surfactant metabolism.
DR SignaLink; O96009; -.
DR BioGRID-ORCS; 9476; 9 hits in 1078 CRISPR screens.
DR GeneWiki; NAPSA; -.
DR GenomeRNAi; 9476; -.
DR Pharos; O96009; Tbio.
DR PRO; PR:O96009; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O96009; protein.
DR Bgee; ENSG00000131400; Expressed in lower lobe of lung and 110 other tissues.
DR ExpressionAtlas; O96009; baseline and differential.
DR Genevisible; O96009; HS.
DR GO; GO:0097208; C:alveolar lamellar body; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0097486; C:multivesicular body lumen; TAS:Reactome.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0043129; P:surfactant homeostasis; IDA:UniProtKB.
DR Gene3D; 2.40.70.10; -; 3.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..63
FT /note="Activation peptide"
FT /id="PRO_0000025996"
FT CHAIN 64..420
FT /note="Napsin-A"
FT /id="PRO_0000025997"
FT DOMAIN 78..399
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..116
FT /evidence="ECO:0000250"
FT DISULFID 274..278
FT /evidence="ECO:0000250"
FT DISULFID 317..354
FT /evidence="ECO:0000250"
FT VARIANT 40
FT /note="I -> T (in dbSNP:rs676314)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_051510"
FT VARIANT 310
FT /note="A -> T (in dbSNP:rs11670727)"
FT /id="VAR_024586"
SQ SEQUENCE 420 AA; 45387 MW; 018B86AE5BD0C865 CRC64;
MSPPPLLQPL LLLLPLLNVE PSGATLIRIP LHRVQPGRRI LNLLRGWREP AELPKLGAPS
PGDKPIFVPL SNYRDVQYFG EIGLGTPPQN FTVAFDTGSS NLWVPSRRCH FFSVPCWLHH
RFDPKASSSF QANGTKFAIQ YGTGRVDGIL SEDKLTIGGI KGASVIFGEA LWEPSLVFAF
AHFDGILGLG FPILSVEGVR PPMDVLVEQG LLDKPVFSFY LNRDPEEPDG GELVLGGSDP
AHYIPPLTFV PVTVPAYWQI HMERVKVGPG LTLCAKGCAA ILDTGTSLIT GPTEEIRALH
AAIGGIPLLA GEYIILCSEI PKLPAVSFLL GGVWFNLTAH DYVIQTTRNG VRLCLSGFQA
LDVPPPAGPF WILGDVFLGT YVAVFDRGDM KSSARVGLAR ARTRGADLGW GETAQAQFPG
