PRS55_HUMAN
ID PRS55_HUMAN Reviewed; 352 AA.
AC Q6UWB4; E5RJX5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Serine protease 55;
DE EC=3.4.21.-;
DE AltName: Full=Testis serine protease 1 {ECO:0000303|PubMed:18844450};
DE Short=T-SP1 {ECO:0000303|PubMed:18844450};
DE Flags: Precursor;
GN Name=PRSS55; Synonyms=TSP1 {ECO:0000303|PubMed:18844450};
GN ORFNames=UNQ9391/PRO34284;
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 MRNA] (ISOFORM 1), AND VARIANTS ARG-44 AND
RP VAL-212.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=18844450; DOI=10.1515/bc.2008.170;
RA Neth P., Profanter B., Geissler C., Naegler D.K., Nerlich A.,
RA Sommerhoff C.P., Jochum M.;
RT "T-SP1: a novel serine protease-like protein predominantly expressed in
RT testis.";
RL Biol. Chem. 389:1495-1504(2008).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=23436708; DOI=10.1002/pmic.201200489;
RA Liu M., Hu Z., Qi L., Wang J., Zhou T., Guo Y., Zeng Y., Zheng B., Wu Y.,
RA Zhang P., Chen X., Tu W., Zhang T., Zhou Q., Jiang M., Guo X., Zhou Z.,
RA Sha J.;
RT "Scanning of novel cancer/testis proteins by human testis proteomic
RT analysis.";
RL Proteomics 13:1200-1210(2013).
CC -!- FUNCTION: Probable serine protease, which plays a crucial role in the
CC fertility of male mice including sperm migration and sperm-egg
CC interaction. {ECO:0000250|UniProtKB:Q14BX2}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:18844450}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:Q14BX2}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:18844450}. Note=Mainly found in the membrane part
CC of the cells and only in small amounts in the cytosol.
CC {ECO:0000269|PubMed:18844450}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:18844450}. Note=Present primarily in the cytosol
CC and only in minor amounts in the membrane fraction.
CC {ECO:0000269|PubMed:18844450}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q6UWB4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UWB4-2; Sequence=VSP_044557;
CC -!- TISSUE SPECIFICITY: Only detected in testis. Expressed in
CC spermatogonia, spermatocytes, spermatids, Leydig and Sertoli cells.
CC Expressed in prostate cancer and ovarian cancer (at protein level).
CC {ECO:0000269|PubMed:18844450, ECO:0000269|PubMed:23436708}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Controversial data exist concerning the topology of PRSS55.
CC One study in mouse shows that PRS55 is a GPI-anchored protein (By
CC similarity). An other study does not confirm the GPI-anchor status of
CC PRSS55 (PubMed:18844450). However as a GPI-anchor motif is detected,
CC the possibility of a GPI-anchor instead of a single-pass type I
CC membrane protein is probable. {ECO:0000250|UniProtKB:Q14BX2,
CC ECO:0000269|PubMed:18844450, ECO:0000305}.
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DR EMBL; AY358867; AAQ89226.1; -; mRNA.
DR EMBL; AC104964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033497; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS56523.1; -. [Q6UWB4-2]
DR CCDS; CCDS5976.1; -. [Q6UWB4-1]
DR RefSeq; NP_001183949.1; NM_001197020.1. [Q6UWB4-2]
DR RefSeq; NP_940866.2; NM_198464.3. [Q6UWB4-1]
DR AlphaFoldDB; Q6UWB4; -.
DR SMR; Q6UWB4; -.
DR STRING; 9606.ENSP00000333003; -.
DR MEROPS; S01.299; -.
DR GlyGen; Q6UWB4; 1 site.
DR BioMuta; PRSS55; -.
DR DMDM; 296453030; -.
DR jPOST; Q6UWB4; -.
DR MassIVE; Q6UWB4; -.
DR PaxDb; Q6UWB4; -.
DR PeptideAtlas; Q6UWB4; -.
DR PRIDE; Q6UWB4; -.
DR ProteomicsDB; 16739; -.
DR ProteomicsDB; 67463; -. [Q6UWB4-1]
DR Antibodypedia; 8438; 83 antibodies from 13 providers.
DR DNASU; 203074; -.
DR Ensembl; ENST00000328655.8; ENSP00000333003.3; ENSG00000184647.11. [Q6UWB4-1]
DR Ensembl; ENST00000522210.1; ENSP00000430459.1; ENSG00000184647.11. [Q6UWB4-2]
DR GeneID; 203074; -.
DR KEGG; hsa:203074; -.
DR MANE-Select; ENST00000328655.8; ENSP00000333003.3; NM_198464.4; NP_940866.2.
DR UCSC; uc003wta.4; human. [Q6UWB4-1]
DR CTD; 203074; -.
DR DisGeNET; 203074; -.
DR GeneCards; PRSS55; -.
DR HGNC; HGNC:30824; PRSS55.
DR HPA; ENSG00000184647; Tissue enriched (testis).
DR MIM; 615144; gene.
DR neXtProt; NX_Q6UWB4; -.
DR OpenTargets; ENSG00000184647; -.
DR PharmGKB; PA165585933; -.
DR VEuPathDB; HostDB:ENSG00000184647; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000156020; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q6UWB4; -.
DR OMA; HEEFNRT; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q6UWB4; -.
DR TreeFam; TF338267; -.
DR PathwayCommons; Q6UWB4; -.
DR BioGRID-ORCS; 203074; 10 hits in 1062 CRISPR screens.
DR GenomeRNAi; 203074; -.
DR Pharos; Q6UWB4; Tbio.
DR PRO; PR:Q6UWB4; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q6UWB4; protein.
DR Bgee; ENSG00000184647; Expressed in right testis and 38 other tissues.
DR ExpressionAtlas; Q6UWB4; baseline and differential.
DR Genevisible; Q6UWB4; HS.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0030317; P:flagellated sperm motility; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Disulfide bond;
KW Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Protease;
KW Reference proteome; Serine protease; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..352
FT /note="Serine protease 55"
FT /id="PRO_0000328815"
FT PROPEP 326..352
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000449398"
FT DOMAIN 68..300
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 308..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 250
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT LIPID 325
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 93..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 189..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 222..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 246..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 248..352
FT /note="GDSGGPLVCTPEPGEKWYQVGIISWGKSCGEKNTPGIYTSLVNYNLWIEKVT
FT QLEGRPFNAEKRRTSVKQKPMGSPVSGVPEPGSPRSWLLLCPLSHVLFRAILY -> QS
FT YFPTLQRMNTGSSQTKPPGSHTFHLQN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:18844450"
FT /id="VSP_044557"
FT VARIANT 44
FT /note="P -> R (in dbSNP:rs4521726)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_042525"
FT VARIANT 212
FT /note="A -> V (in dbSNP:rs4406360)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_042526"
FT CONFLICT 15
FT /note="G -> R (in Ref. 3; BC033497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 38856 MW; 0DBDFC385D5413A4 CRC64;
MLLFSVLLLL SLVTGTQLGP RTPLPEAGVA ILGRARGAHR PQPPHPPSPV SECGDRSIFE
GRTRYSRITG GMEAEVGEFP WQVSIQARSE PFCGGSILNK WWILTAAHCL YSEELFPEEL
SVVLGTNDLT SPSMEIKEVA SIILHKDFKR ANMDNDIALL LLASPIKLDD LKVPICLPTQ
PGPATWRECW VAGWGQTNAA DKNSVKTDLM KAPMVIMDWE ECSKMFPKLT KNMLCAGYKN
ESYDACKGDS GGPLVCTPEP GEKWYQVGII SWGKSCGEKN TPGIYTSLVN YNLWIEKVTQ
LEGRPFNAEK RRTSVKQKPM GSPVSGVPEP GSPRSWLLLC PLSHVLFRAI LY
