ID   KNG_GADMO               Reviewed;         123 AA.
AC   P83856;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Kininogen;
DE   Contains:
DE     RecName: Full=Bradykinin;
DE   Flags: Fragments;
OS   Gadus morhua (Atlantic cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX   NCBI_TaxID=8049 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, GLYCOSYLATION, AND MASS SPECTROMETRY.
RC   TISSUE=Skin {ECO:0000269|PubMed:12047371};
RX   PubMed=12047371; DOI=10.1046/j.1432-1033.2002.02927.x;
RA   Yloenen A., Helin J., Bogwald J., Jaakola A., Rinne A., Kalkkinen N.;
RT   "Purification and characterization of novel kininogens from spotted
RT   wolffish and Atlantic cod.";
RL   Eur. J. Biochem. 269:2639-2646(2002).
CC   -!- FUNCTION: Inhibits papain and ficin (cysteine proteinases) but not
CC       trypsin (a serine proteinase). {ECO:0000269|PubMed:12047371}.
CC   -!- PTM: Bradykinin is released from kininogen by kallikrein.
CC       {ECO:0000250|UniProtKB:P01042}.
CC   -!- PTM: N-glycosylated. Contains sulfated N-acetylglucosamine and O-
CC       acetylated sialic acids as terminal elements on biantennary and
CC       triantennary N-glycans. {ECO:0000269|PubMed:12047371}.
CC   -!- MASS SPECTROMETRY: Mass=51000; Method=MALDI; Note=The measured range is
CC       1-123.; Evidence={ECO:0000269|PubMed:12047371};
CC   -!- CAUTION: The order of the last 3 peptides shown is unknown.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P83856; -.
DR   Proteomes; UP000694546; Unplaced.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Glycoprotein; Protease inhibitor; Reference proteome;
KW   Thiol protease inhibitor; Vasoactive; Vasodilator.
FT   CHAIN           <1..>123
FT                   /note="Kininogen"
FT                   /id="PRO_0000045864"
FT   PEPTIDE         85..93
FT                   /note="Bradykinin"
FT                   /evidence="ECO:0000250|UniProtKB:P01042"
FT                   /id="PRO_0000006708"
FT   NON_CONS        19..20
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        36..37
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        50..51
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        57..58
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        83..84
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        93..94
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        102..103
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        114..115
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_TER         123
FT                   /evidence="ECO:0000303|PubMed:12047371"
SQ   SEQUENCE   123 AA;  13427 MW;  442F3BDD1C02804B CRC64;
     RHEVPQANLE CDEGAMDLKI STGNMVALYQ ILSASKDSDC PAGGAVTWTD QVVAGLRICM
     GCPVELDLES EELKVPVAVS ISKRRPPGWS PLRAAVTSFN EKEFSPPAPP SRAEYSLYFD
     MRK