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   13-FEB-2019, entry version 129.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Kanamori T., Miyazaki K.;
RT   "cDNA cloning of a novel trypsin inhibitor with similarity to
RT   pathogenesis-related proteins, and its frequent expression in human
RT   brain cancer 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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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
RT   project: 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.,
RA   Umeda M., 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.,
RA   Tabin C.J.;
RT   "Cloning and expression of a novel cysteine-rich secreted protein
RT   family member expressed in thyroid and pancreatic mesoderm within the
RT   chicken 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
CC       facial 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   UniGene; Hs.98558; -.
DR   ProteinModelPortal; O43692; -.
DR   BioGrid; 119244; 13.
DR   STRING; 9606.ENSP00000260113; -.
DR   iPTMnet; O43692; -.
DR   PhosphoSitePlus; O43692; -.
DR   BioMuta; PI15; -.
DR   jPOST; O43692; -.
DR   MaxQB; O43692; -.
DR   PaxDb; O43692; -.
DR   PeptideAtlas; O43692; -.
DR   PRIDE; O43692; -.
DR   ProteomicsDB; 49119; -.
DR   DNASU; 51050; -.
DR   Ensembl; ENST00000260113; ENSP00000260113; ENSG00000137558.
DR   Ensembl; ENST00000523773; ENSP00000428567; ENSG00000137558.
DR   Ensembl; ENST00000649643; ENSP00000497041; ENSG00000137558.
DR   GeneID; 51050; -.
DR   KEGG; hsa:51050; -.
DR   UCSC; uc003yal.3; human.
DR   CTD; 51050; -.
DR   DisGeNET; 51050; -.
DR   EuPathDB; HostDB:ENSG00000137558.7; -.
DR   GeneCards; PI15; -.
DR   HGNC; HGNC:8946; PI15.
DR   HPA; HPA006593; -.
DR   HPA; HPA030057; -.
DR   MIM; 607076; gene.
DR   neXtProt; NX_O43692; -.
DR   OpenTargets; ENSG00000137558; -.
DR   PharmGKB; PA33282; -.
DR   eggNOG; KOG3017; Eukaryota.
DR   eggNOG; COG2340; LUCA.
DR   GeneTree; ENSGT00940000158635; -.
DR   HOGENOM; HOG000111978; -.
DR   HOVERGEN; HBG079090; -.
DR   InParanoid; O43692; -.
DR   OMA; NMNVWGA; -.
DR   OrthoDB; 1528782at2759; -.
DR   PhylomeDB; O43692; -.
DR   TreeFam; TF316148; -.
DR   GenomeRNAi; 51050; -.
DR   PRO; PR:O43692; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   Bgee; ENSG00000137558; Expressed in 149 organ(s), highest expression level in uterine cervix.
DR   Genevisible; O43692; HS.
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   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.33.10; -; 1.
DR   InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR001283; CRISP-related.
DR   PANTHER; PTHR10334; PTHR10334; 1.
DR   Pfam; PF00188; CAP; 1.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; SSF55797; 1.
DR   PROSITE; PS01010; CRISP_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Developmental protein; Direct protein sequencing;
KW   Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   PROPEP       20     60       {ECO:0000305|PubMed:8882727}.
FT                                /FTId=PRO_0000287622.
FT   CHAIN        61    258       Peptidase inhibitor 15.
FT                                /FTId=PRO_0000287623.
FT   DOMAIN       71    211       SCP.
FT   CARBOHYD     26     26       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     36     36       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    124    124       N-linked (GlcNAc...) asparagine.
FT                                {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
//