PI15_CHICK
ID PI15_CHICK Reviewed; 258 AA.
AC Q98ST6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Peptidase inhibitor 15;
DE AltName: Full=SugarCrisp;
DE Flags: Precursor;
GN Name=PI15;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Limb bud;
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 FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION BY NOG AND RETINOIC ACID.
RX PubMed=26385749; DOI=10.1016/j.ydbio.2015.09.007;
RA Nimmagadda S., Buchtova M., Fu K., Geetha-Loganathan P.,
RA Hosseini-Farahabadi S., Trachtenberg A.J., Kuo W.P., Vesela I.,
RA Richman J.M.;
RT "Identification and functional analysis of novel facial patterning genes in
RT the duplicated beak chicken embryo.";
RL Dev. Biol. 407:275-288(2015).
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 (PubMed:26385749).
CC {ECO:0000250|UniProtKB:O43692, ECO:0000269|PubMed:26385749}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O43692}.
CC -!- DEVELOPMENTAL STAGE: First expressed the mesoderm of the emerging
CC dorsal pancreatic bud at stage 17-18. Also expressed in the thyroid
CC anlagen. Expression persists throughout the dorsal pancreatic mesoderm
CC through E6 as the pancreas continues to enlarge. After E6, the amount
CC of mesoderm in the pancreas declines to a minimal level and little or
CC no expression is seen. The expression in the mesoderm of the thyroid
CC persists at least through E8 in the development of this organ. Weakly
CC expressed within the emerging lung buds and developing gut. Also
CC expressed in developing carniofacial structures. At stage 17,
CC expression is restricted to the cranial paraxial mesoderm. At stage 24,
CC expressed in the corners of the frontonasal mass (globular processes)
CC where the lip will fuse. At stage 26 through 29, becomes focused in the
CC center of the frontonasal mass. At stage 30, further restricted to the
CC future egg tooth. By stage 34, found in the egg tooth and structures
CC derived from the frontonasal mass, such as the premaxillary mesenchyme
CC (PubMed:26385749). {ECO:0000269|PubMed:11287197,
CC ECO:0000269|PubMed:26385749}.
CC -!- INDUCTION: Up-regulated by Noggin/NOG and retinoic acid. May be a
CC direct retinoic acid target. {ECO:0000269|PubMed:26385749}.
CC -!- MISCELLANEOUS: Was named SugarCrisp after the breakfast cereal.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; AF329195; AAK16493.1; -; mRNA.
DR RefSeq; NP_989665.1; NM_204334.1.
DR AlphaFoldDB; Q98ST6; -.
DR SMR; Q98ST6; -.
DR STRING; 9031.ENSGALP00000035875; -.
DR PaxDb; Q98ST6; -.
DR Ensembl; ENSGALT00000065508; ENSGALP00000051751; ENSGALG00000029264.
DR GeneID; 374241; -.
DR KEGG; gga:374241; -.
DR CTD; 51050; -.
DR VEuPathDB; HostDB:geneid_374241; -.
DR eggNOG; KOG3017; Eukaryota.
DR GeneTree; ENSGT00940000158635; -.
DR HOGENOM; CLU_035730_2_2_1; -.
DR InParanoid; Q98ST6; -.
DR OMA; WQRAVYL; -.
DR OrthoDB; 1528782at2759; -.
DR PhylomeDB; Q98ST6; -.
DR TreeFam; TF316148; -.
DR PRO; PR:Q98ST6; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000029264; Expressed in colon and 1 other tissue.
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_0000287626"
FT CHAIN 61..258
FT /note="Peptidase inhibitor 15"
FT /id="PRO_0000287627"
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; 29239 MW; 3FD853945B92FF35 CRC64;
MTIIAAISCV FLFSILCETS ALVLPNSTDL LLSNNNFTDI ETALAAHLDS AKIPKARRKR
YISQNDMIAI LDYHNQVRGK VFPPASNMEY MVWDETLAKS AEAWAATCIW DHGPSYLLRF
LGQNLSVRTG RYRSILQLVK PWYDEVKDYA FPYPQDCNPR CPMRCYGPMC THYTQMVWAT
SNRIGCAIHT CQNMNVWGSV WRRAVYLVCN YAPKGNWIGE APYKVGVPCS ACPPSYGGSC
TDNLCFPGVT SNYLYWFK
