PRS37_HUMAN
ID PRS37_HUMAN Reviewed; 235 AA.
AC A4D1T9; B2RPB5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable inactive serine protease 37 {ECO:0000305};
DE AltName: Full=Probable inactive trypsin-X2;
DE Flags: Precursor;
GN Name=PRSS37 {ECO:0000312|HGNC:HGNC:29211}; Synonyms=TRYX2;
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=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INVOLVEMENT IN
RP UNEXPLAINED MALE INFERTILITY.
RX PubMed=27649891; DOI=10.1093/abbs/gmw096;
RA Liu J., Shen C., Fan W., Chen Y., Zhang A., Feng Y., Li Z., Kuang Y.,
RA Wang Z.;
RT "Low levels of PRSS37 protein in sperm are associated with many cases of
RT unexplained male infertility.";
RL Acta Biochim. Biophys. Sin. 48:1058-1065(2016).
CC -!- FUNCTION: Plays a role in male fertility (By similarity). May have a
CC role in sperm migration or binding to zona-intact eggs (By similarity).
CC Involved in the activation of the proacrosin/acrosin system
CC (PubMed:27649891). {ECO:0000250|UniProtKB:Q9DAA4,
CC ECO:0000269|PubMed:27649891}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000269|PubMed:27649891}. Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Testis-specific (PubMed:27649891). Expressed in
CC spermatids (at protein level) (PubMed:27649891).
CC {ECO:0000269|PubMed:27649891}.
CC -!- DISEASE: Note=Patients with unexplained male infertility (UMI) show a
CC decrease in the number of sperm cells compared to fertile men
CC (PubMed:27649891). Sperm exhibit also abnormal activation of the
CC proacrosin/acrosin system and premature proteolysis of ADAM2
CC (PubMed:27649891). {ECO:0000269|PubMed:27649891}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Although related to peptidase S1 family, lacks the conserved
CC active Ser residue in position 192 which is replaced by an Ala,
CC suggesting that it has no protease activity. Lacks also metal binding
CC sites Glu in position 67 which is replaced by Asn and Asn in position
CC 69 which is replaced by Lys. {ECO:0000305}.
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DR EMBL; CH236950; EAL24014.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83986.1; -; Genomic_DNA.
DR EMBL; BC137353; AAI37354.1; -; mRNA.
DR EMBL; BC137354; AAI37355.1; -; mRNA.
DR CCDS; CCDS34764.1; -.
DR RefSeq; NP_001008271.2; NM_001008270.2.
DR AlphaFoldDB; A4D1T9; -.
DR SMR; A4D1T9; -.
DR BioGRID; 126449; 42.
DR IntAct; A4D1T9; 13.
DR STRING; 9606.ENSP00000297767; -.
DR MEROPS; S01.989; -.
DR BioMuta; PRSS37; -.
DR MassIVE; A4D1T9; -.
DR PaxDb; A4D1T9; -.
DR PeptideAtlas; A4D1T9; -.
DR PRIDE; A4D1T9; -.
DR ProteomicsDB; 631; -.
DR Antibodypedia; 18320; 27 antibodies from 11 providers.
DR DNASU; 136242; -.
DR Ensembl; ENST00000350549.8; ENSP00000297767.3; ENSG00000165076.14.
DR Ensembl; ENST00000438520.1; ENSP00000414461.1; ENSG00000165076.14.
DR GeneID; 136242; -.
DR KEGG; hsa:136242; -.
DR MANE-Select; ENST00000350549.8; ENSP00000297767.3; NM_001008270.3; NP_001008271.2.
DR UCSC; uc003vws.3; human.
DR CTD; 136242; -.
DR DisGeNET; 136242; -.
DR GeneCards; PRSS37; -.
DR HGNC; HGNC:29211; PRSS37.
DR HPA; ENSG00000165076; Tissue enriched (testis).
DR neXtProt; NX_A4D1T9; -.
DR OpenTargets; ENSG00000165076; -.
DR PharmGKB; PA165618277; -.
DR VEuPathDB; HostDB:ENSG00000165076; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000161483; -.
DR HOGENOM; CLU_006842_1_6_1; -.
DR InParanoid; A4D1T9; -.
DR OMA; DKDCQKT; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; A4D1T9; -.
DR TreeFam; TF331065; -.
DR PathwayCommons; A4D1T9; -.
DR SignaLink; A4D1T9; -.
DR BioGRID-ORCS; 136242; 8 hits in 1062 CRISPR screens.
DR GenomeRNAi; 136242; -.
DR Pharos; A4D1T9; Tdark.
DR PRO; PR:A4D1T9; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; A4D1T9; protein.
DR Bgee; ENSG00000165076; Expressed in right testis and 79 other tissues.
DR ExpressionAtlas; A4D1T9; baseline and differential.
DR Genevisible; A4D1T9; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0008354; P:germ cell migration; IEA:Ensembl.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IMP:UniProtKB.
DR GO; GO:1905516; P:positive regulation of fertilization; ISS:UniProtKB.
DR GO; GO:0051604; P:protein maturation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0070613; P:regulation of protein processing; IMP:UniProtKB.
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 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.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Disulfide bond; Fertilization; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..235
FT /note="Probable inactive serine protease 37"
FT /id="PRO_0000326070"
FT DOMAIN 20..233
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 40..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 131..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 163..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VARIANT 119
FT /note="T -> P (in dbSNP:rs12669721)"
FT /id="VAR_039985"
SQ SEQUENCE 235 AA; 26445 MW; ECEED5C51E94E3B5 CRC64;
MKYVFYLGVL AGTFFFADSS VQKEDPAPYL VYLKSHFNPC VGVLIKPSWV LAPAHCYLPN
LKVMLGNFKS RVRDGTEQTI NPIQIVRYWN YSHSAPQDDL MLIKLAKPAM LNPKVQPLTL
ATTNVRPGTV CLLSGLDWSQ ENSGRHPDLR QNLEAPVMSD RECQKTEQGK SHRNSLCVKF
VKVFSRIFGE VAVATVICKD KLQGIEVGHF MGGDVGIYTN VYKYVSWIEN TAKDK
