ID   KNG_ANAMI               Reviewed;         188 AA.
AC   P83857;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   07-OCT-2020, entry version 33.
DE   RecName: Full=Kininogen;
DE   Contains:
DE     RecName: Full=Bradykinin;
DE   Flags: Fragments;
OS   Anarhichas minor (Arctic spotted wolffish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Zoarcales; Anarhichadidae; Anarhichas.
OX   NCBI_TaxID=65739 {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 O-acetylated sialic acids as terminal
CC       elements on biantennary and triantennary N-glycans.
CC       {ECO:0000269|PubMed:12047371}.
CC   -!- MASS SPECTROMETRY: [Kininogen]: Mass=45800; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12047371};
CC   -!- CAUTION: The order of the last 2 peptides shown is unknown.
CC       {ECO:0000305}.
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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; Thiol protease inhibitor; Vasoactive;
KW   Vasodilator.
FT   CHAIN           1..>188
FT                   /note="Kininogen"
FT                   /id="PRO_0000045863"
FT   PEPTIDE         134..142
FT                   /note="Bradykinin"
FT                   /evidence="ECO:0000250|UniProtKB:P01042"
FT                   /id="PRO_0000006707"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   NON_CONS        15..16
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        33..34
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        49..50
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        71..72
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        81..82
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        113..114
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        122..123
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        142..143
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_CONS        163..164
FT                   /evidence="ECO:0000303|PubMed:12047371"
FT   NON_TER         188
FT                   /evidence="ECO:0000303|PubMed:12047371"
SQ   SEQUENCE   188 AA;  21006 MW;  593B4E3E6DC09958 CRC64;
     XLVQPGVLIF CDDPSYNSMS DSTHLFTLHF VXYSENGSDS VYSLQFTSRS DCPAGSNKPW
     TECDYLSYER RFNERLSTGH KQVYCLLDDV IIPEKAPCLG CPMEVDENSE DLKFPLSVSI
     SKAGALPTMF TRRRPPGWSP LRRKKPISCN ATVYMTETEA DTKDLNDLCV PDDQNAGYAN
     CNSTVNVA