PRS41_HUMAN
ID PRS41_HUMAN Reviewed; 318 AA.
AC Q7RTY9;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Serine protease 41;
DE EC=3.4.21.-;
DE AltName: Full=Testis serine protease 1;
DE Short=TESSP-1;
DE Flags: Precursor;
GN Name=PRSS41 {ECO:0000312|HGNC:HGNC:30715}; Synonyms=TESSP1;
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).
RN [2]
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).
RN [3]
RP VARIANT GLY-286.
RX PubMed=20797691; DOI=10.1016/j.ajhg.2010.08.001;
RA Corbett M.A., Bahlo M., Jolly L., Afawi Z., Gardner A.E., Oliver K.L.,
RA Tan S., Coffey A., Mulley J.C., Dibbens L.M., Simri W., Shalata A.,
RA Kivity S., Jackson G.D., Berkovic S.F., Gecz J.;
RT "A focal epilepsy and intellectual disability syndrome is due to a mutation
RT in TBC1D24.";
RL Am. J. Hum. Genet. 87:371-375(2010).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC Note=Localized in the plasma membrane of spermatogonia. Localized in
CC intracellular compartment in spermatocytes, probably in the Golgi
CC apparatus (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AC092117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000124; CAD67575.1; -; mRNA.
DR RefSeq; NP_001128558.1; NM_001135086.1.
DR AlphaFoldDB; Q7RTY9; -.
DR SMR; Q7RTY9; -.
DR BioGRID; 131864; 1.
DR IntAct; Q7RTY9; 1.
DR MEROPS; S01.327; -.
DR GlyGen; Q7RTY9; 3 sites, 2 O-linked glycans (1 site).
DR iPTMnet; Q7RTY9; -.
DR PhosphoSitePlus; Q7RTY9; -.
DR BioMuta; PRSS41; -.
DR DMDM; 74759056; -.
DR jPOST; Q7RTY9; -.
DR MassIVE; Q7RTY9; -.
DR PeptideAtlas; Q7RTY9; -.
DR PRIDE; Q7RTY9; -.
DR Antibodypedia; 78183; 12 antibodies from 5 providers.
DR GeneCards; PRSS41; -.
DR HGNC; HGNC:30715; PRSS41.
DR HPA; ENSG00000215148; Tissue enhanced (testis).
DR neXtProt; NX_Q7RTY9; -.
DR PharmGKB; PA165450634; -.
DR VEuPathDB; HostDB:ENSG00000215148; -.
DR InParanoid; Q7RTY9; -.
DR PhylomeDB; Q7RTY9; -.
DR PathwayCommons; Q7RTY9; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; Q7RTY9; -.
DR BioGRID-ORCS; 360226; 1 hit in 129 CRISPR screens.
DR GenomeRNAi; 360226; -.
DR Pharos; Q7RTY9; Tdark.
DR PRO; PR:Q7RTY9; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q7RTY9; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0043229; C:intracellular organelle; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0017080; F:sodium channel regulator activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Protease; Reference proteome; Serine protease;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..54
FT /evidence="ECO:0000255"
FT /id="PRO_0000345420"
FT CHAIN 55..299
FT /note="Serine protease 41"
FT /id="PRO_5000095968"
FT PROPEP 300..318
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000345421"
FT DOMAIN 55..297
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 95
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 249
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT LIPID 299
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 181..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 215..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 245..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VARIANT 286
FT /note="S -> G (in dbSNP:rs746540699)"
FT /evidence="ECO:0000269|PubMed:20797691"
FT /id="VAR_064369"
SQ SEQUENCE 318 AA; 35078 MW; D792213630CF15C3 CRC64;
MGARGALLLA LLLARAGLGK PGELGALQAG PGAARRPGGG GREEACGHRE IHALVAGGVE
SARGRWPWQA SLRLRRRHRC GGSLLSRRWV LSAAHCFQKH YYPSEWTVQL GELTSRPTPW
NLRAYSSRYK VQDIIVNPDA LGVLRNDIAL LRLASSVTYN AYIQPICIES STFNFVHRPD
CWVTGWGLIS PSGTPLPPPY NLREAQVTIL NNTRCNYLFE QPSSRSMIWD SMFCAGAEDG
SVDTCKGDSG GPLVCDKDGL WYQVGIVSWG MDCGQPNRPG VYTNISVYFH WIRRVMSHST
PRPNPSQLLL LLALLWAP
