ID   PI15_HUMAN              Reviewed;         258 AA.
AC   O43692; Q68CY1;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   24-JAN-2024, entry version 152.
DE   RecName: Full=Peptidase inhibitor 15;
DE            Short=PI-15;
DE   AltName: Full=25 kDa trypsin inhibitor;
DE            Short=p25TI;
DE   AltName: Full=Cysteine-rich secretory protein 8;
DE            Short=CRISP-8;
DE   AltName: Full=SugarCrisp;
DE   Flags: Precursor;
GN   Name=PI15; Synonyms=CRISP8, P25TI;
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 [MRNA], TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX   PubMed=9473672; DOI=10.1016/s0167-4781(97)00149-8;
RA   Yamakawa T., Miyata S., Ogawa N., Koshikawa N., Yasumitsu H., Kanamori T.,
RA   Miyazaki K.;
RT   "cDNA cloning of a novel trypsin inhibitor with similarity to pathogenesis-
RT   related proteins, and its frequent expression in human brain cancer
RT   cells.";
RL   Biochim. Biophys. Acta 1395:202-208(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Endometrial adenocarcinoma;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   PROTEIN SEQUENCE OF 61-85, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=8882727; DOI=10.1093/oxfordjournals.jbchem.a021244;
RA   Koshikawa N., Nakamura T., Tsuchiya N., Isaji M., Yasumitsu H., Umeda M.,
RA   Miyazaki K.;
RT   "Purification and identification of a novel and four known serine
RT   proteinase inhibitors secreted by human glioblastoma cells.";
RL   J. Biochem. 119:334-339(1996).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=11287197; DOI=10.1016/s0925-4773(01)00293-3;
RA   Smith D.M., Collins-Racie L.A., Marigo V.A., Roberts D.J., Davis N.M.,
RA   Hartmann C., Schweitzer R., LaVallie E.R., Gamer L., McCoy J., Tabin C.J.;
RT   "Cloning and expression of a novel cysteine-rich secreted protein family
RT   member expressed in thyroid and pancreatic mesoderm within the chicken
RT   embryo.";
RL   Mech. Dev. 102:223-226(2001).
CC   -!- FUNCTION: Serine protease inhibitor which displays weak inhibitory
CC       activity against trypsin (PubMed:8882727). May play a role in facial
CC       patterning during embryonic development (By similarity).
CC       {ECO:0000250|UniProtKB:Q98ST6, ECO:0000269|PubMed:8882727}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8882727}.
CC   -!- TISSUE SPECIFICITY: Weakly expressed. Expressed at low level in
CC       prostate, mammary gland, salivary gland and thyroid gland.
CC       {ECO:0000269|PubMed:11287197, ECO:0000269|PubMed:9473672}.
CC   -!- PTM: N-glycosylated. {ECO:0000305|PubMed:9473672}.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; D45027; BAA25066.1; -; mRNA.
DR   EMBL; CR749657; CAH18451.2; -; mRNA.
DR   EMBL; BC074931; AAH74931.1; -; mRNA.
DR   EMBL; BC074932; AAH74932.1; -; mRNA.
DR   EMBL; BC126290; AAI26291.1; -; mRNA.
DR   EMBL; BC126292; AAI26293.1; -; mRNA.
DR   CCDS; CCDS6218.1; -.
DR   RefSeq; NP_001311332.1; NM_001324403.1.
DR   RefSeq; NP_056970.1; NM_015886.4.
DR   AlphaFoldDB; O43692; -.
DR   SMR; O43692; -.
DR   BioGRID; 119244; 92.
DR   STRING; 9606.ENSP00000260113; -.
DR   GlyCosmos; O43692; 3 sites, No reported glycans.
DR   GlyGen; O43692; 3 sites.
DR   iPTMnet; O43692; -.
DR   PhosphoSitePlus; O43692; -.
DR   BioMuta; PI15; -.
DR   jPOST; O43692; -.
DR   MassIVE; O43692; -.
DR   MaxQB; O43692; -.
DR   PaxDb; 9606-ENSP00000260113; -.
DR   PeptideAtlas; O43692; -.
DR   ProteomicsDB; 49119; -.
DR   Antibodypedia; 1731; 195 antibodies from 28 providers.
DR   DNASU; 51050; -.
DR   Ensembl; ENST00000260113.7; ENSP00000260113.2; ENSG00000137558.9.
DR   Ensembl; ENST00000523773.1; ENSP00000428567.1; ENSG00000137558.9.
DR   Ensembl; ENST00000649643.1; ENSP00000497041.1; ENSG00000137558.9.
DR   GeneID; 51050; -.
DR   KEGG; hsa:51050; -.
DR   MANE-Select; ENST00000260113.7; ENSP00000260113.2; NM_015886.5; NP_056970.1.
DR   UCSC; uc003yal.3; human.
DR   AGR; HGNC:8946; -.
DR   CTD; 51050; -.
DR   DisGeNET; 51050; -.
DR   GeneCards; PI15; -.
DR   HGNC; HGNC:8946; PI15.
DR   HPA; ENSG00000137558; Tissue enhanced (lymphoid tissue, prostate, smooth muscle).
DR   MIM; 607076; gene.
DR   neXtProt; NX_O43692; -.
DR   OpenTargets; ENSG00000137558; -.
DR   PharmGKB; PA33282; -.
DR   VEuPathDB; HostDB:ENSG00000137558; -.
DR   eggNOG; KOG3017; Eukaryota.
DR   GeneTree; ENSGT00940000158635; -.
DR   HOGENOM; CLU_035730_2_2_1; -.
DR   InParanoid; O43692; -.
DR   OMA; CSPNEVY; -.
DR   OrthoDB; 5470953at2759; -.
DR   PhylomeDB; O43692; -.
DR   TreeFam; TF316148; -.
DR   PathwayCommons; O43692; -.
DR   BioGRID-ORCS; 51050; 9 hits in 1146 CRISPR screens.
DR   ChiTaRS; PI15; human.
DR   GenomeRNAi; 51050; -.
DR   Pharos; O43692; Tbio.
DR   PRO; PR:O43692; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; O43692; Protein.
DR   Bgee; ENSG00000137558; Expressed in cauda epididymis and 130 other cell types or tissues.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd18814; CAP_PI15; 1.
DR   Gene3D; 3.40.33.10; CAP; 1.
DR   InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR001283; CRISP-related.
DR   InterPro; IPR047832; PI15_CAP.
DR   PANTHER; PTHR10334; CYSTEINE-RICH SECRETORY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10334:SF63; PEPTIDASE INHIBITOR 15; 1.
DR   Pfam; PF00188; CAP; 1.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; PR-1-like; 1.
DR   PROSITE; PS01010; CRISP_2; 1.
DR   Genevisible; O43692; HS.
PE   1: Evidence at protein level;
KW   Developmental protein; Direct protein sequencing; Glycoprotein;
KW   Protease inhibitor; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..60
FT                   /evidence="ECO:0000305|PubMed:8882727"
FT                   /id="PRO_0000287622"
FT   CHAIN           61..258
FT                   /note="Peptidase inhibitor 15"
FT                   /id="PRO_0000287623"
FT   DOMAIN          71..211
FT                   /note="SCP"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   258 AA;  29065 MW;  1915A5831637795F CRC64;
     MIAISAVSSA LLFSLLCEAS TVVLLNSTDS SPPTNNFTDI EAALKAQLDS ADIPKARRKR
     YISQNDMIAI LDYHNQVRGK VFPPAANMEY MVWDENLAKS AEAWAATCIW DHGPSYLLRF
     LGQNLSVRTG RYRSILQLVK PWYDEVKDYA FPYPQDCNPR CPMRCFGPMC THYTQMVWAT
     SNRIGCAIHT CQNMNVWGSV WRRAVYLVCN YAPKGNWIGE APYKVGVPCS SCPPSYGGSC
     TDNLCFPGVT SNYLYWFK
//