PI15A_DANRE
ID PI15A_DANRE Reviewed; 260 AA.
AC Q7T141;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Peptidase inhibitor 15-A;
DE Flags: Precursor;
GN Name=pi15a; Synonyms=pi15; ORFNames=si:rp71-1m12.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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 -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE17614.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL627168; CAE17614.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001153449.1; NM_001159977.1.
DR AlphaFoldDB; Q7T141; -.
DR SMR; Q7T141; -.
DR STRING; 7955.ENSDARP00000117953; -.
DR PaxDb; Q7T141; -.
DR Ensembl; ENSDART00000141620; ENSDARP00000117953; ENSDARG00000045378.
DR GeneID; 561978; -.
DR KEGG; dre:561978; -.
DR CTD; 561978; -.
DR ZFIN; ZDB-GENE-040724-135; pi15a.
DR eggNOG; KOG3017; Eukaryota.
DR GeneTree; ENSGT00940000158635; -.
DR HOGENOM; CLU_035730_2_2_1; -.
DR InParanoid; Q7T141; -.
DR OMA; CSPNEVY; -.
DR OrthoDB; 1528782at2759; -.
DR PhylomeDB; Q7T141; -.
DR TreeFam; TF316148; -.
DR PRO; PR:Q7T141; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000045378; Expressed in swim bladder and 11 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: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 3: Inferred from homology;
KW Developmental protein; Glycoprotein; Protease inhibitor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..62
FT /evidence="ECO:0000250|UniProtKB:O43692"
FT /id="PRO_0000287628"
FT CHAIN 63..260
FT /note="Peptidase inhibitor 15-A"
FT /id="PRO_0000287629"
FT DOMAIN 73..213
FT /note="SCP"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 260 AA; 29345 MW; E664A54E35DA747D CRC64;
MNENRLAIDI LLLCISCGAS ALAGFSPTAS SSLPATNLTD IGFAPPKYLT EAANIPKTRR
KRYISQNDML AILDYHNKVR GKVFPPASNM EYMVWDDTLA KTAEQWASTC IWEHGPRNLL
RFLGQNLSVR TGRYRSILQL VKPWHDEVKD YSFPYPRDCN PRCPLKCYGP MCTHYTQMVW
ATSNKVGCAI NTCHNMNVWG SVWKRATYLV CNYSPKGNWI GEAPYKVGVP CSMCPPSYGG
SCSNNMCFPA VNSNYLHWFK