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 13-FEB-2019, entry version 150. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT closely related genes."; RL FEBS Lett. 441:43-48(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND RP IDENTIFICATION BY 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., RA Alaiya A.A., Franzen B., Bergman T., Arnott D., Auer G., Appella E., RA Joernvall H., 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 RT and 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 RT project: 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 -!- 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 CC spleen and very low levels in peripheral blood leukocytes. CC -!- SIMILARITY: Belongs to the peptidase A1 family. {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; 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 UniGene; Hs.512843; -. DR ProteinModelPortal; O96009; -. DR SMR; O96009; -. DR BioGrid; 114861; 7. DR IntAct; O96009; 2. DR MINT; O96009; -. DR STRING; 9606.ENSP00000253719; -. DR MEROPS; A01.046; -. DR iPTMnet; O96009; -. DR PhosphoSitePlus; O96009; -. DR SwissPalm; O96009; -. DR BioMuta; NAPSA; -. DR EPD; O96009; -. DR PaxDb; O96009; -. DR PeptideAtlas; O96009; -. DR PRIDE; O96009; -. DR ProteomicsDB; 51189; -. DR DNASU; 9476; -. DR Ensembl; ENST00000253719; ENSP00000253719; ENSG00000131400. DR GeneID; 9476; -. DR KEGG; hsa:9476; -. DR UCSC; uc002prx.4; human. DR CTD; 9476; -. DR DisGeNET; 9476; -. DR EuPathDB; HostDB:ENSG00000131400.7; -. DR GeneCards; NAPSA; -. DR H-InvDB; HIX0039966; -. DR HGNC; HGNC:13395; NAPSA. DR HPA; CAB009591; -. DR HPA; HPA045280; -. DR HPA; HPA047236; -. DR HPA; HPA047744; -. DR MIM; 605631; gene. DR neXtProt; NX_O96009; -. DR OpenTargets; ENSG00000131400; -. DR PharmGKB; PA134891814; -. DR eggNOG; KOG1339; Eukaryota. DR eggNOG; ENOG410XNV7; LUCA. DR GeneTree; ENSGT00940000160179; -. DR HOGENOM; HOG000197681; -. DR HOVERGEN; HBG000482; -. DR InParanoid; O96009; -. DR KO; K08565; -. DR OMA; IILCSEI; -. DR OrthoDB; 1619495at2759; -. DR PhylomeDB; O96009; -. DR TreeFam; TF314990; -. DR BRENDA; 3.4.23.B1; 2681. DR Reactome; R-HSA-5683826; Surfactant metabolism. DR GeneWiki; NAPSA; -. DR GenomeRNAi; 9476; -. DR PRO; PR:O96009; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000131400; Expressed in 98 organ(s), highest expression level in upper lobe of lung. 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:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB. DR GO; GO:0030163; P:protein catabolic process; IBA:GO_Central. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR GO; GO:0043129; P:surfactant homeostasis; IDA:UniProtKB. 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; PTHR13683; PTHR13683; 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; Complete proteome; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Hydrolase; Polymorphism; Protease; KW Reference proteome; Secreted; Signal; Zymogen. FT SIGNAL 1 25 {ECO:0000255}. FT PROPEP 26 63 Activation peptide. FT /FTId=PRO_0000025996. FT CHAIN 64 420 Napsin-A. FT /FTId=PRO_0000025997. FT DOMAIN 78 399 Peptidase A1. {ECO:0000255|PROSITE- FT ProRule:PRU01103}. FT ACT_SITE 96 96 {ECO:0000255|PROSITE-ProRule:PRU10094}. FT ACT_SITE 283 283 {ECO:0000255|PROSITE-ProRule:PRU10094}. FT CARBOHYD 90 90 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 133 133 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 336 336 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 109 116 {ECO:0000250}. FT DISULFID 274 278 {ECO:0000250}. FT DISULFID 317 354 {ECO:0000250}. FT VARIANT 40 40 I -> T (in dbSNP:rs676314). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_051510. FT VARIANT 310 310 A -> T (in dbSNP:rs11670727). FT /FTId=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 //