ID   PI16_BOVIN              Reviewed;         464 AA.
AC   Q58D34;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Peptidase inhibitor 16;
DE            Short=PI-16;
DE   AltName: CD_antigen=CD364;
DE   Flags: Precursor;
GN   Name=PI16;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May inhibit cardiomyocyte growth.
CC       {ECO:0000250|UniProtKB:Q9ET66}.
CC   -!- SUBUNIT: Interacts with PSP94/MSMB. {ECO:0000250|UniProtKB:Q6UXB8}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9ET66}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6UXB8}.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; BT021763; AAX46610.1; -; mRNA.
DR   EMBL; BC119955; AAI19956.1; -; mRNA.
DR   RefSeq; NP_001019658.1; NM_001024487.1.
DR   RefSeq; XP_005223367.2; XM_005223310.3.
DR   RefSeq; XP_005223368.2; XM_005223311.2.
DR   AlphaFoldDB; Q58D34; -.
DR   SMR; Q58D34; -.
DR   STRING; 9913.ENSBTAP00000002703; -.
DR   PaxDb; Q58D34; -.
DR   PRIDE; Q58D34; -.
DR   Ensembl; ENSBTAT00000002703; ENSBTAP00000002703; ENSBTAG00000002092.
DR   Ensembl; ENSBTAT00000047585; ENSBTAP00000044778; ENSBTAG00000002092.
DR   GeneID; 507058; -.
DR   KEGG; bta:507058; -.
DR   CTD; 221476; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002092; -.
DR   VGNC; VGNC:32853; PI16.
DR   eggNOG; KOG3017; Eukaryota.
DR   GeneTree; ENSGT00940000162458; -.
DR   HOGENOM; CLU_049124_0_0_1; -.
DR   InParanoid; Q58D34; -.
DR   OMA; AYAQQCI; -.
DR   OrthoDB; 1528782at2759; -.
DR   TreeFam; TF316148; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000002092; Expressed in trachea and 97 other tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Glycoprotein; Protease inhibitor; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..464
FT                   /note="Peptidase inhibitor 16"
FT                   /id="PRO_0000287632"
FT   DOMAIN          37..165
FT                   /note="SCP"
FT   REGION          208..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   464 AA;  49327 MW;  740F12722A9DBBAF CRC64;
     MHGSGSLLAC LLPPLLLLGA APGPAGALSE EEKHVMVELH NLYRTQVSPP ATNMLQMRWD
     EELAAFAKAY AQQCVWGHNK ERGRRGENLF AITGEGLDVP LAMEEWHHER EHYNLSAISC
     AAGQMCGHYT QVVWAKTERI GCGSHFCEKL QGVEETNIHL LVCNYEPPGN VKGQRPYQEG
     TPCSQCPLGY HCKNSLCEPI RGPEEAQDLS SLVPEAPSSL ATEASSSRRE GIDSSLATEP
     PPFLVTEVSG SLATKVLSSV ETKAPSSLVT EDSPSMATKT PLSLATKVPS VLATHSLLSL
     DKRPATLLPK STHDPIPKSA DKEASSTRMP SRIPESSLHP KISLMGTREP LPLSQEEGEA
     EAELAHCSEI LASVFPAQEK PGELQTTLKH KGHSSSKSLS NSPSASATAN AVGGRTLALQ
     SSLPDAEGPG KHGFRSGSNA SPGHVGGLLL GLLLLLPLVL AGIF