ID Q561U4_DANRE Unreviewed; 265 AA.
AC Q561U4; A0A8M1N583;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE SubName: Full=Chymotrypsinogen B2 precursor {ECO:0000313|RefSeq:NP_001017724.1};
DE EC=3.4.21.1 {ECO:0000313|RefSeq:NP_001017724.1};
DE SubName: Full=Zgc:112160 {ECO:0000313|EMBL:AAH93233.1, ECO:0000313|Ensembl:ENSDARP00000058066};
GN Name=ctrb.3 {ECO:0000313|ZFIN:ZDB-GENE-050417-229};
GN ORFNames=zgc:112160 {ECO:0000313|EMBL:AAH93233.1,
GN ECO:0000313|RefSeq:NP_001017724.1};
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 {ECO:0000313|EMBL:AAH93233.1};
RN [1] {ECO:0000313|EMBL:AAH93233.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Larvae {ECO:0000313|EMBL:AAH93233.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:NP_001017724.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22110365;
RA Chung A.Y., Kim S., Kim H., Bae Y.K., Park H.C.;
RT "Microarray screening for genes involved in oligodendrocyte differentiation
RT in the zebrafish CNS.";
RL Exp. Neurobiol. 20:85-91(2011).
RN [3] {ECO:0000313|Ensembl:ENSDARP00000058066}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000058066};
RG Ensembl;
RL Submitted (FEB-2012) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSDARP00000058066, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000058066};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA 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).
RN [5] {ECO:0000313|RefSeq:NP_001017724.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25576359;
RA Orosz F.;
RT "On the tubulin polymerization promoting proteins of zebrafish.";
RL Biochem. Biophys. Res. Commun. 457:267-272(2015).
RN [6] {ECO:0000313|Ensembl:ENSDARP00000156092}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000156092};
RG Ensembl;
RL Submitted (APR-2018) to UniProtKB.
RN [7] {ECO:0000313|RefSeq:NP_001017724.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; CR356247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093233; AAH93233.1; -; mRNA.
DR RefSeq; NP_001017724.1; NM_001017724.2.
DR STRING; 7955.ENSDARP00000058066; -.
DR MEROPS; S01.437; -.
DR PaxDb; 7955-ENSDARP00000058066; -.
DR Ensembl; ENSDART00000058067.5; ENSDARP00000058066.3; ENSDARG00000039730.5.
DR Ensembl; ENSDART00000188844.1; ENSDARP00000156092.1; ENSDARG00000113624.1.
DR GeneID; 550419; -.
DR KEGG; dre:550419; -.
DR AGR; ZFIN:ZDB-GENE-050417-229; -.
DR CTD; 550419; -.
DR ZFIN; ZDB-GENE-050417-229; ctrb.3.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_6_1; -.
DR OMA; RWNPRTI; -.
DR OrthoDB; 4629979at2759; -.
DR TreeFam; TF330455; -.
DR Reactome; R-DRE-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-DRE-9758881; Uptake of dietary cobalamins into enterocytes.
DR Proteomes; UP000000437; Alternate scaffold 7.
DR Proteomes; UP000000437; Chromosome 7.
DR Bgee; ENSDARG00000039730; Expressed in intestine and 13 other cell types or tissues.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24250; CHYMOTRYPSIN-RELATED; 1.
DR PANTHER; PTHR24250:SF54; ZGC:112160; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q561U4};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001017724.1}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..265
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001017724.1"
FT /id="PRO_5035034223"
FT DOMAIN 34..263
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 265 AA; 28617 MW; C669FA2D900518FB CRC64;
MAFLWLLSCV AFFSAAYGCG VPAIPPVVSG YARIVNGEEA VPHSWPWQVS LQDFTGFHFC
GGSLINEFWV VTAAHCSVRT SHRVILGEHN KGKSNTQEDI QTMKVSKVFT HPQYNSNTIE
NDIALVKLTA PASLNAHVSP VCLAEASDNF ASGMTCVTSG WGVTRYNALF TPDELQQVAL
PLLSNEDCKN HWGSNIRDTM ICAGAAGASS CMGDSGGPLV CQKDNIWTLV GIVSWGSSRC
DPTMPGVYGR VTELRDWVDQ ILASN
//
