PI15_MOUSE
ID PI15_MOUSE Reviewed; 258 AA.
AC Q8BS03; Q3TN14; Q99MM7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Peptidase inhibitor 15;
DE Short=PI-15;
DE AltName: Full=SugarCrisp;
DE Flags: Precursor;
GN Name=Pi15;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, Colon, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Serine protease inhibitor which displays weak inhibitory
CC activity against trypsin (By similarity). May play a role in facial
CC patterning during embryonic development (By similarity).
CC {ECO:0000250|UniProtKB:O43692, ECO:0000250|UniProtKB:Q98ST6}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O43692}.
CC -!- TISSUE SPECIFICITY: Weakly expressed. Expressed at low level in
CC prostate, mammary gland, salivary gland and thyroid gland.
CC {ECO:0000269|PubMed:11287197}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O43692}.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30762.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF329196; AAK16494.1; -; mRNA.
DR EMBL; AK040961; BAC30762.1; ALT_INIT; mRNA.
DR EMBL; AK165584; BAE38275.1; -; mRNA.
DR EMBL; BC116705; AAI16706.2; -; mRNA.
DR RefSeq; NP_444421.2; NM_053191.2.
DR AlphaFoldDB; Q8BS03; -.
DR SMR; Q8BS03; -.
DR STRING; 10090.ENSMUSP00000085826; -.
DR GlyGen; Q8BS03; 2 sites.
DR PhosphoSitePlus; Q8BS03; -.
DR MaxQB; Q8BS03; -.
DR PaxDb; Q8BS03; -.
DR PRIDE; Q8BS03; -.
DR ProteomicsDB; 289415; -.
DR DNASU; 94227; -.
DR GeneID; 94227; -.
DR KEGG; mmu:94227; -.
DR UCSC; uc007ake.2; mouse.
DR CTD; 51050; -.
DR MGI; MGI:1934659; Pi15.
DR eggNOG; KOG3017; Eukaryota.
DR InParanoid; Q8BS03; -.
DR OrthoDB; 1528782at2759; -.
DR PhylomeDB; Q8BS03; -.
DR TreeFam; TF316148; -.
DR BioGRID-ORCS; 94227; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q8BS03; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BS03; protein.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030414; F:peptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0010466; P:negative regulation of peptidase activity; 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 2: Evidence at transcript level;
KW Developmental protein; Glycoprotein; Protease inhibitor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..60
FT /evidence="ECO:0000250|UniProtKB:O43692"
FT /id="PRO_0000287624"
FT CHAIN 61..258
FT /note="Peptidase inhibitor 15"
FT /id="PRO_0000287625"
FT DOMAIN 71..211
FT /note="SCP"
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"
FT CONFLICT 50
FT /note="S -> R (in Ref. 2; BAE38275)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="D -> V (in Ref. 2; BAE38275)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 258 AA; 29151 MW; 2FA994A9A2562640 CRC64;
MIMNSAVSLV ILLSLLCEAH TVVLLNPTDS SLPANNFTDT EAALSTPLES ADIPKARRKR
YISQNDMIAI LDYHNQVRGK VFPPAANMEY MVWDENLAKS AEAWAATCIW DHGPSYLLRF
LGQNLSVRTG RYRSILQLVK PWYDEVKDYA FPYPQDCNPR CPMRCFGPMC THYTQMVWAT
SNRIGCAIHT CQNMNVWGSV WRRAVYLVCN YAPKGNWIGE APYKVGVPCS SCPPSYGGAC
TDNLCFPGVT TNYLYWFK
