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 16-JAN-2019, entry version 88. 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; 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=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., RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., RA 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., RA Mural R.J., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT of unexplained male infertility."; RL Acta Biochim. Biophys. Sin. 48:1058-1065(2016). CC -!- FUNCTION: Plays a role in male fertility (By similarity). May have CC a role in sperm migration or binding to zona-intact eggs (By CC similarity). Involved in the activation of the proacrosin/acrosin CC system (PubMed:27649891). {ECO:0000250|UniProtKB:Q9DAA4, CC ECO:0000269|PubMed:27649891}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, CC acrosome {ECO:0000269|PubMed:27649891}. Secreted {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Testis-specific (PubMed:27649891). Expressed CC in spermatids (at protein level) (PubMed:27649891). CC {ECO:0000269|PubMed:27649891}. CC -!- DISEASE: Note=Patients with unexplained male infertility (UMI) CC show a decrease in the number of sperm cells compared to fertile CC men (PubMed:27649891). Sperm exhibit also abnormal activation of CC the proacrosin/acrosin system and premature proteolysis of ADAM2 CC (PubMed:27649891). {ECO:0000269|PubMed:27649891}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- CAUTION: Although related to peptidase S1 family, lacks the CC conserved active Ser residue in position 192 which is replaced by CC an Ala, suggesting that it has no protease activity. Lacks also CC metal binding sites Glu in position 67 which is replaced by Asn CC and Asn in position 69 which is replaced by Lys. {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; 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 UniGene; Hs.98947; -. DR ProteinModelPortal; A4D1T9; -. DR BioGrid; 126449; 11. DR STRING; 9606.ENSP00000297767; -. DR MEROPS; S01.989; -. DR BioMuta; PRSS37; -. DR PaxDb; A4D1T9; -. DR PRIDE; A4D1T9; -. DR ProteomicsDB; 631; -. DR Ensembl; ENST00000350549; ENSP00000297767; ENSG00000165076. DR Ensembl; ENST00000438520; ENSP00000414461; ENSG00000165076. DR GeneID; 136242; -. DR KEGG; hsa:136242; -. DR UCSC; uc003vws.3; human. DR CTD; 136242; -. DR EuPathDB; HostDB:ENSG00000165076.13; -. DR GeneCards; PRSS37; -. DR HGNC; HGNC:29211; PRSS37. DR HPA; HPA020541; -. DR neXtProt; NX_A4D1T9; -. DR OpenTargets; ENSG00000165076; -. DR PharmGKB; PA165618277; -. DR eggNOG; KOG3627; Eukaryota. DR eggNOG; COG5640; LUCA. DR GeneTree; ENSGT00940000161483; -. DR HOGENOM; HOG000251820; -. DR InParanoid; A4D1T9; -. DR OMA; RYWNYSH; -. DR OrthoDB; 1314811at2759; -. DR PhylomeDB; A4D1T9; -. DR TreeFam; TF331065; -. DR GenomeRNAi; 136242; -. DR PRO; PR:A4D1T9; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000165076; Expressed in 63 organ(s), highest expression level in left testis. DR ExpressionAtlas; A4D1T9; baseline and differential. DR Genevisible; A4D1T9; HS. DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0030141; C:secretory granule; IBA:GO_Central. 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: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:0070613; P:regulation of protein processing; IMP:UniProtKB. DR InterPro; IPR009003; Peptidase_S1_PA. 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 Complete proteome; Cytoplasmic vesicle; Disulfide bond; Fertilization; KW Polymorphism; Reference proteome; Secreted; Signal. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 235 Probable inactive serine protease 37. FT /FTId=PRO_0000326070. FT DOMAIN 20 233 Peptidase S1. {ECO:0000255|PROSITE- FT ProRule:PRU00274}. FT DISULFID 40 56 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 131 198 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT DISULFID 163 177 {ECO:0000255|PROSITE-ProRule:PRU00274}. FT VARIANT 119 119 T -> P (in dbSNP:rs12669721). FT /FTId=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 //