PRS38_HUMAN
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 03-AUG-2022, entry version 101.
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; 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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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 project:
RT 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. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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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 AlphaFoldDB; A1L453; -.
DR SMR; A1L453; -.
DR BioGRID; 130896; 1.
DR IntAct; A1L453; 1.
DR STRING; 9606.ENSP00000355719; -.
DR MEROPS; S01.318; -.
DR GlyGen; A1L453; 1 site.
DR iPTMnet; A1L453; -.
DR PhosphoSitePlus; A1L453; -.
DR BioMuta; PRSS38; -.
DR MassIVE; A1L453; -.
DR PaxDb; A1L453; -.
DR PeptideAtlas; A1L453; -.
DR PRIDE; A1L453; -.
DR Antibodypedia; 20773; 30 antibodies from 11 providers.
DR DNASU; 339501; -.
DR Ensembl; ENST00000366757.3; ENSP00000355719.3; ENSG00000185888.5.
DR GeneID; 339501; -.
DR KEGG; hsa:339501; -.
DR MANE-Select; ENST00000366757.4; ENSP00000355719.3; NM_183062.3; NP_898885.1.
DR UCSC; uc001hrh.4; human.
DR CTD; 339501; -.
DR GeneCards; PRSS38; -.
DR HGNC; HGNC:29625; PRSS38.
DR HPA; ENSG00000185888; Tissue enriched (testis).
DR neXtProt; NX_A1L453; -.
DR OpenTargets; ENSG00000185888; -.
DR PharmGKB; PA165752268; -.
DR VEuPathDB; HostDB:ENSG00000185888; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000154494; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; A1L453; -.
DR OMA; TACEGDS; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; A1L453; -.
DR TreeFam; TF351676; -.
DR PathwayCommons; A1L453; -.
DR SignaLink; A1L453; -.
DR BioGRID-ORCS; 339501; 6 hits in 1061 CRISPR screens.
DR GenomeRNAi; 339501; -.
DR Pharos; A1L453; Tdark.
DR PRO; PR:A1L453; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; A1L453; protein.
DR Bgee; ENSG00000185888; Expressed in right testis and 4 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 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 Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT PROPEP 33..59
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000328820"
FT CHAIN 60..326
FT /note="Serine protease 38"
FT /id="PRO_0000328821"
FT DOMAIN 60..293
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 100
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 245
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 183..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 214..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 241..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VARIANT 204
FT /note="M -> V (in dbSNP:rs9426581)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_042531"
FT CONFLICT 123
FT /note="A -> D (in Ref. 2; AAI30401)"
FT /evidence="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
