ID PRS38_HUMAN Reviewed; 326 AA. AC A1L453; Q7RTY6; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 2. DT 16-JAN-2019, entry version 84. DE RecName: Full=Serine protease 38; DE EC=3.4.21.-; DE AltName: Full=Marapsin-2; DE Flags: Precursor; GN Name=PRSS38; Synonyms=MPN2; 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 [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-204. RC TISSUE=Testis; 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). RN [3] RP IDENTIFICATION. RX PubMed=12838346; DOI=10.1038/nrg1111; RA Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.; RT "Human and mouse proteases: a comparative genomic approach."; RL Nat. Rev. Genet. 4:544-558(2003). CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. 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; AL356323; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL731702; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC130400; AAI30401.1; -; mRNA. DR EMBL; BN000131; CAD67593.1; -; mRNA. DR CCDS; CCDS1563.1; -. DR RefSeq; NP_898885.1; NM_183062.2. DR UniGene; Hs.97604; -. DR ProteinModelPortal; A1L453; -. DR SMR; A1L453; -. DR BioGrid; 130896; 1. DR IntAct; A1L453; 1. DR STRING; 9606.ENSP00000355719; -. DR MEROPS; S01.318; -. DR iPTMnet; A1L453; -. DR PhosphoSitePlus; A1L453; -. DR BioMuta; PRSS38; -. DR jPOST; A1L453; -. DR PaxDb; A1L453; -. DR PRIDE; A1L453; -. DR ProteomicsDB; 147; -. DR Ensembl; ENST00000366757; ENSP00000355719; ENSG00000185888. DR GeneID; 339501; -. DR KEGG; hsa:339501; -. DR UCSC; uc001hrh.4; human. DR CTD; 339501; -. DR DisGeNET; 339501; -. DR EuPathDB; HostDB:ENSG00000185888.5; -. DR GeneCards; PRSS38; -. DR H-InvDB; HIX0028897; -. DR HGNC; HGNC:29625; PRSS38. DR HPA; HPA028003; -. DR HPA; HPA055809; -. DR neXtProt; NX_A1L453; -. DR OpenTargets; ENSG00000185888; -. DR PharmGKB; PA165752268; -. DR eggNOG; KOG3627; Eukaryota. DR eggNOG; COG5640; LUCA. DR GeneTree; ENSGT00940000154494; -. DR HOGENOM; HOG000251820; -. DR HOVERGEN; HBG013304; -. DR InParanoid; A1L453; -. DR OMA; WQVSVHY; -. DR OrthoDB; 1314811at2759; -. DR PhylomeDB; A1L453; -. DR TreeFam; TF351676; -. DR GenomeRNAi; 339501; -. DR PRO; PR:A1L453; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000185888; Expressed in 12 organ(s), highest expression level in right testis. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR CDD; cd00190; Tryp_SPc; 1. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; KW Polymorphism; Protease; Reference proteome; Secreted; Serine protease; KW Signal. FT SIGNAL 1 32 {ECO:0000255}. FT PROPEP 33 59 Activation peptide. {ECO:0000255}. FT /FTId=PRO_0000328820. FT CHAIN 60 326 Serine protease 38. FT /FTId=PRO_0000328821. FT DOMAIN 60 293 Peptidase S1. {ECO:0000255|PROSITE- FT ProRule:PRU00274}. FT ACT_SITE 100 100 Charge relay system. {ECO:0000250}. FT ACT_SITE 150 150 Charge relay system. {ECO:0000250}. FT ACT_SITE 245 245 Charge relay system. {ECO:0000250}. FT CARBOHYD 125 125 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 85 101 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 183 251 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 214 230 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 241 269 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT VARIANT 204 204 M -> V (in dbSNP:rs9426581). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_042531. FT CONFLICT 123 123 A -> D (in Ref. 2; AAI30401). FT {ECO:0000305}. SQ SEQUENCE 326 AA; 35356 MW; 9F3A8EE36B082777 CRC64; MAAPASVMGP LGPSALGLLL LLLVVAPPRV AALVHRQPEN QGISLTGSVA CGRPSMEGKI LGGVPAPERK WPWQVSVHYA GLHVCGGSIL NEYWVLSAAH CFHRDKNIKI YDMYVGLVNL RVAGNHTQWY EVNRVILHPT YEMYHPIGGD VALVQLKTRI VFSESVLPVC LATPEVNLTS ANCWATGWGL VSKQGETSDE LQEMQLPLIL EPWCHLLYGH MSYIMPDMLC AGDILNAKTV CEGDSGGPLV CEFNRSWLQI GIVSWGRGCS NPLYPGVYAS VSYFSKWICD NIEITPTPAQ PAPALSPALG PTLSVLMAML AGWSVL //