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   27-MAR-2024, entry version 136.
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   GlyCosmos; Q6UWB4; 1 site, No reported glycans.
DR   GlyGen; Q6UWB4; 1 site.
DR   BioMuta; PRSS55; -.
DR   DMDM; 296453030; -.
DR   jPOST; Q6UWB4; -.
DR   MassIVE; Q6UWB4; -.
DR   PaxDb; 9606-ENSP00000333003; -.
DR   PeptideAtlas; Q6UWB4; -.
DR   ProteomicsDB; 16739; -.
DR   ProteomicsDB; 67463; -. [Q6UWB4-1]
DR   Antibodypedia; 8438; 108 antibodies from 14 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   AGR; HGNC:30824; -.
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; GVGEFPW; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; Q6UWB4; -.
DR   TreeFam; TF338267; -.
DR   PathwayCommons; Q6UWB4; -.
DR   BioGRID-ORCS; 203074; 10 hits in 1140 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 primordial germ cell in gonad and 39 other cell types or tissues.
DR   ExpressionAtlas; Q6UWB4; baseline and differential.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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; Trypsin-like serine proteases; 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   PANTHER; PTHR24253:SF90; SERINE PROTEASE 55; 1.
DR   PANTHER; PTHR24253; TRANSMEMBRANE PROTEASE SERINE; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   Genevisible; Q6UWB4; HS.
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
//