PRS29_HUMAN
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 25-MAY-2022, entry version 73.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., 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., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., 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. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AC120498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A6NIE9; -.
DR SMR; A6NIE9; -.
DR GlyGen; A6NIE9; 1 site.
DR BioMuta; HGNC:17542; -.
DR MassIVE; A6NIE9; -.
DR PeptideAtlas; A6NIE9; -.
DR PRIDE; A6NIE9; -.
DR ProteomicsDB; 1266; -.
DR TopDownProteomics; A6NIE9; -.
DR GeneCards; PRSS29P; -.
DR HGNC; HGNC:17542; PRSS29P.
DR neXtProt; NX_A6NIE9; -.
DR InParanoid; A6NIE9; -.
DR PhylomeDB; A6NIE9; -.
DR Pharos; A6NIE9; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; A6NIE9; protein.
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 Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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 Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..313
FT /note="Putative serine protease 29"
FT /id="PRO_0000349227"
FT DOMAIN 68..310
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 262
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 193..268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 226..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 258..286
FT /evidence="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
