ID Q1AMP9_DISMA Unreviewed; 242 AA.
AC Q1AMP9;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Trypsinogen {ECO:0000313|EMBL:ABA41381.1, ECO:0000313|EMBL:AEA08587.1};
DE SubName: Full=Trypsinogen H2_1e {ECO:0000313|EMBL:AEA08613.1};
GN Name=AFGP {ECO:0000313|EMBL:ABA41381.1};
OS Dissostichus mawsoni (Antarctic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Dissostichus.
OX NCBI_TaxID=36200 {ECO:0000313|EMBL:ABA41381.1};
RN [1] {ECO:0000313|EMBL:ABA41381.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pancreas {ECO:0000313|EMBL:ABA41381.1};
RX PubMed=16798878; DOI=10.1073/pnas.0603796103;
RA Cheng C.H., Cziko P.A., Evans C.W.;
RT "Nonhepatic origin of notothenioid antifreeze reveals pancreatic synthesis
RT as common mechanism in polar fish freezing avoidance.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10491-10496(2006).
RN [2] {ECO:0000313|EMBL:AEA08587.1}
RP NUCLEOTIDE SEQUENCE.
RA Nicodemus Johnson J.D., Cheng C.-H.C.;
RT "Assembly of the antifreeze glycoprotein/trypsinogen-like protease genomic
RT locus.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
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DR EMBL; DQ062459; ABA41381.1; -; mRNA.
DR EMBL; HQ447059; AEA08587.1; -; Genomic_DNA.
DR EMBL; HQ447060; AEA08613.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1AMP9; -.
DR MEROPS; S01.125; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; PTHR24264; TRYPSIN-RELATED; 1.
DR PANTHER; PTHR24264:SF6; TRYPSINOGEN 1A-RELATED; 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 2: Evidence at transcript level;
KW Digestion {ECO:0000256|ARBA:ARBA00022757};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..242
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011945875"
FT DOMAIN 21..240
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 242 AA; 26265 MW; 881CDC4B2CE8DCAD CRC64;
MRSLVFVLLI GAAFATEEDK IVGGKECTPY SMPHQVSLNS GYHFCGGSLV NADWVVSAAH
CYKTRVEVQL GEHNFRVTEG NEQYISSSRV IRHPNYNSYN IDNDIMLIKL SKPATLNQYV
QPVALPSSCA PAGTMCTVSG WGSTMSSTAD KNKLQCLNIP ILSDRDCDNS YPGMITDSMF
CAGYLEGGKD SCQGDSGGPV VCNGELQGVV SWGYGCAQKD NPGVYTKVCL FNNWLETTMA
SY
//
