PI16_MOUSE
ID PI16_MOUSE Reviewed; 498 AA.
AC Q9ET66; Q148Q6; Q8CHU4; Q9JJ56;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Peptidase inhibitor 16;
DE Short=PI-16;
DE AltName: Full=Cysteine-rich protease inhibitor;
DE AltName: CD_antigen=CD364;
DE Flags: Precursor;
GN Name=Pi16; Synonyms=Cripi;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RA Jang J.S., Hahn Y., Chung J.H.;
RT "Genomic structure of murine cysteine-rich protease inhibitor gene.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RA Brathwaite M., Waeltz P., Schlessinger D., Nagaraja R.;
RT "Genomic sequence analysis in the mouse T-complex region.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-498 (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 53-498 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 FUNCTION, IDENTIFICATION OF ISOFORM 2, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, AND GLYCOSYLATION.
RX PubMed=17909105; DOI=10.1161/circulationaha.107.696468;
RA Frost R.J., Engelhardt S.;
RT "A secretion trap screen in yeast identifies protease inhibitor 16 as a
RT novel antihypertrophic protein secreted from the heart.";
RL Circulation 116:1768-1775(2007).
CC -!- FUNCTION: May inhibit cardiomyocyte growth.
CC {ECO:0000269|PubMed:17909105}.
CC -!- SUBUNIT: Interacts with PSP94/MSMB. {ECO:0000250|UniProtKB:Q6UXB8}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17909105}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ET66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ET66-2; Sequence=VSP_025575;
CC -!- TISSUE SPECIFICITY: Expressed strongly in aorta and skin, and weakly in
CC adipose tissue (at protein level). In heart, found in the extracellular
CC space surrounding cardiomyocytes (at protein level).
CC {ECO:0000269|PubMed:17909105}.
CC -!- INDUCTION: Up-regulated in a mouse model of heart failure.
CC {ECO:0000269|PubMed:17909105}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17909105}.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39124.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH39124.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI18027.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP45197.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB03398.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB03453.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB046537; BAB03398.1; ALT_INIT; mRNA.
DR EMBL; AB046539; BAB03453.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY301264; AAP45197.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC039124; AAH39124.1; ALT_INIT; mRNA.
DR EMBL; BC118026; AAI18027.1; ALT_INIT; mRNA.
DR CCDS; CCDS28595.2; -. [Q9ET66-1]
DR RefSeq; NP_076223.3; NM_023734.3. [Q9ET66-1]
DR RefSeq; XP_006525077.1; XM_006525014.1. [Q9ET66-2]
DR AlphaFoldDB; Q9ET66; -.
DR SMR; Q9ET66; -.
DR STRING; 10090.ENSMUSP00000110349; -.
DR GlyGen; Q9ET66; 2 sites.
DR PhosphoSitePlus; Q9ET66; -.
DR jPOST; Q9ET66; -.
DR MaxQB; Q9ET66; -.
DR PaxDb; Q9ET66; -.
DR PeptideAtlas; Q9ET66; -.
DR PRIDE; Q9ET66; -.
DR ProteomicsDB; 289557; -. [Q9ET66-1]
DR ProteomicsDB; 289558; -. [Q9ET66-2]
DR Antibodypedia; 29743; 184 antibodies from 27 providers.
DR DNASU; 74116; -.
DR Ensembl; ENSMUST00000114701; ENSMUSP00000110349; ENSMUSG00000024011. [Q9ET66-1]
DR Ensembl; ENSMUST00000155348; ENSMUSP00000116183; ENSMUSG00000024011. [Q9ET66-2]
DR GeneID; 74116; -.
DR KEGG; mmu:74116; -.
DR CTD; 221476; -.
DR MGI; MGI:1921366; Pi16.
DR VEuPathDB; HostDB:ENSMUSG00000024011; -.
DR eggNOG; KOG3017; Eukaryota.
DR GeneTree; ENSGT00940000162458; -.
DR InParanoid; Q9ET66; -.
DR OMA; AYAQQCI; -.
DR OrthoDB; 1528782at2759; -.
DR PhylomeDB; Q9ET66; -.
DR BioGRID-ORCS; 74116; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q9ET66; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9ET66; protein.
DR Bgee; ENSMUSG00000024011; Expressed in granulocyte and 134 other tissues.
DR ExpressionAtlas; Q9ET66; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0030414; F:peptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IDA:MGI.
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; PS01009; CRISP_1; 1.
DR PROSITE; PS01010; CRISP_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Protease inhibitor; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000250"
FT CHAIN 30..498
FT /note="Peptidase inhibitor 16"
FT /id="PRO_0000287634"
FT DOMAIN 39..167
FT /note="SCP"
FT REGION 204..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 200..461
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025575"
FT CONFLICT 248
FT /note="T -> I (in Ref. 1; BAB03398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 53650 MW; 14D34F12393D71AF CRC64;
MHGSCSPWVM LPPPLLLLLL LIATGPTTAL TEDEKQTMVD LHNQYRAQVS PPASDMLQMR
WDDELAAFAK AYAQKCVWGH NKERGRRGEN LFAITDEGMD VPLAVGNWHE EHEYYNFSTA
TCDPNQMCGH YTQVVWSKTE RIGCGSHFCE TLQGVEEANI HLLVCNYEPP GNVKGRKPYQ
EGTPCSQCPL GYSCENSLCE PMRNPEKAQD SPPRVTEVPS TRATEAPSSR ETGTPSLATS
ETLHFSVTKV SDSLATESSP AVETKAPSSL ATEGPSSMAT EAQAFVTEVP LVSARHMQPS
VDEGPVNFLT STHIPVPKSM DEEASKSSAT SVSPKKSLYP KMSLTESGES VPQIQEEAEP
KDELSEPEAI LPEAEAAPTE AEVELREPEA ESPKAESPEA EAESPLSSEA LVPVLPAQER
GGQKASLEHS GHPASPSLPT FPSASGNATG GRTLALQSSW TGAENPEKAD WDLKNSAHVW
GPFLGLLLPS LLLLAGMV
