ID PRS29_HUMAN Reviewed; 313 AA. AC A6NIE9; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 3. DT 16-JAN-2019, entry version 65. DE RecName: Full=Putative serine protease 29; DE EC=3.4.21.-; DE AltName: Full=Implantation serine proteinase 2-like protein; DE Short=ISP2-like protein; DE Flags: Precursor; GN Name=PRSS29P; Synonyms=ISP2; 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=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- CAUTION: Could be the product of a pseudogene. {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; AC120498; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR UniGene; Hs.738703; -. DR ProteinModelPortal; A6NIE9; -. DR SMR; A6NIE9; -. DR BioMuta; HGNC:17542; -. DR jPOST; A6NIE9; -. DR PRIDE; A6NIE9; -. DR ProteomicsDB; 1266; -. DR TopDownProteomics; A6NIE9; -. DR GeneCards; PRSS29P; -. DR HGNC; HGNC:17542; PRSS29P. DR neXtProt; NX_A6NIE9; -. DR HOGENOM; HOG000251820; -. DR HOVERGEN; HBG013304; -. DR InParanoid; A6NIE9; -. DR PhylomeDB; A6NIE9; -. DR Proteomes; UP000005640; Unplaced. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. 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 5: Uncertain; KW Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Protease; KW Reference proteome; Secreted; Serine protease; Signal. FT SIGNAL 1 ? {ECO:0000255}. FT CHAIN ? 313 Putative serine protease 29. FT /FTId=PRO_0000349227. FT DOMAIN 68 310 Peptidase S1. {ECO:0000255|PROSITE- FT ProRule:PRU00274}. FT COMPBIAS 2 29 Pro-rich. FT ACT_SITE 114 114 Charge relay system. {ECO:0000250}. FT ACT_SITE 161 161 Charge relay system. {ECO:0000250}. FT ACT_SITE 262 262 Charge relay system. {ECO:0000250}. FT CARBOHYD 143 143 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 99 115 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 193 268 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 226 249 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 258 286 {ECO:0000255|PROSITE-ProRule:PRU00274}. SQ SEQUENCE 313 AA; 34063 MW; 4DE6123C63C5F67C CRC64; MPTTPDPGSE PPARTPRPPP LTPGLSPQPA LHALSPQLLL LLFLAVSSLG SCSTGSPVPV PENDLVGIVG GHNAPPGKWP WQVSLRVYSY HWASWAHICG GSLIHPQWVL TAAHCIFWKD TDPSIYRIHA GDVYLYGGRG LLNVSRIIVH PNYVTAGLGA DVALLQLEPH DLSNVRTVKL SPVSLELTPK DQCWVTGWGA IIRKESLPPP YRLQQASVQV LENAVCEQPY RNASGHTGDR QLILDDMLCA GSEGRDSCYG DSGGPLVCRL RGSWRLVGVV SWGYGCTLRD FPGVYTHVQI YVPWILQQVG ELP //