KNT1_RAT
ID KNT1_RAT Reviewed; 430 AA.
AC P01048; P04081; Q6LDW3;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=T-kininogen 1;
DE AltName: Full=Alpha-1-MAP;
DE AltName: Full=Major acute phase protein;
DE AltName: Full=T-kininogen I;
DE AltName: Full=Thiostatin;
DE Contains:
DE RecName: Full=T-kininogen 1 heavy chain;
DE AltName: Full=T-kininogen I heavy chain;
DE Contains:
DE RecName: Full=T-kinin;
DE Contains:
DE RecName: Full=T-kininogen 1 light chain;
DE AltName: Full=T-kininogen I light chain;
DE Flags: Precursor;
GN Name=Map1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2413018; DOI=10.1016/s0021-9258(17)38984-6;
RA Furuto-Kato S., Matsumoto A., Kitamura N., Nakanishi S.;
RT "Primary structures of the mRNAs encoding the rat precursors for bradykinin
RT and T-kinin. Structural relationship of kininogens with major acute phase
RT protein and alpha 1-cysteine proteinase inhibitor.";
RL J. Biol. Chem. 260:12054-12059(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=2806908; DOI=10.1016/0378-1119(89)90342-9;
RA Anderson K.P., Croyle M.L., Lingrel J.B.;
RT "Primary structure of a gene encoding rat T-kininogen.";
RL Gene 81:119-128(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
RX PubMed=2439509; DOI=10.1016/s0021-9258(18)48080-5;
RA Fung W.-P., Schreiber G.;
RT "Structure and expression of the genes for major acute phase alpha 1-
RT protein (thiostatin) and kininogen in the rat.";
RL J. Biol. Chem. 262:9298-9308(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=3818598; DOI=10.1016/s0021-9258(18)61660-6;
RA Kageyama R., Kitamura N., Ohkubo H., Nakanishi S.;
RT "Differing utilization of homologous transcription initiation sites of rat
RT K and T kininogen genes under inflammation condition.";
RL J. Biol. Chem. 262:2345-2351(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-430.
RX PubMed=2578992; DOI=10.1016/0014-5793(85)81153-4;
RA Cole T., Inglis A.S., Roxburgh C.M., Howlett G.J., Schreiber G.;
RT "Major acute phase alpha 1-protein of the rat is homologous to bovine
RT kininogen and contains the sequence for bradykinin: its synthesis is
RT regulated at the mRNA level.";
RL FEBS Lett. 182:57-61(1985).
RN [6]
RP PROTEIN SEQUENCE OF 19-48 AND 376-430, AND PYROGLUTAMATE FORMATION AT
RP GLN-19.
RX PubMed=3121623; DOI=10.1016/s0021-9258(19)35448-1;
RA Enjyoji K., Kato H., Hayashi I., Oh-ishi S., Iwanaga S.;
RT "Purification and characterization of rat T-kininogens isolated from plasma
RT of adjuvant-treated rats. Identification of three kinds of T-kininogens.";
RL J. Biol. Chem. 263:973-979(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 330-430.
RX PubMed=2108948; DOI=10.1111/j.1349-7006.1990.tb02508.x;
RA Kanda S., Sugiyama K., Takahashi M., Shumiya S., Tomino S., Nagase S.;
RT "Identification of a protein increasing in serum of Nagase analbuminemic
RT rats bearing intestinal tumors as an isotype of T-kininogen.";
RL Jpn. J. Cancer Res. 81:63-68(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 340-430.
RX PubMed=7574705; DOI=10.1006/abbi.1995.1472;
RA Sierra F., Walter R., Vautravers P., Guigoz Y.;
RT "Identification of several isoforms of T-kininogen expressed in the liver
RT of aging rats.";
RL Arch. Biochem. Biophys. 322:333-338(1995).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 375-430.
RX PubMed=3029068; DOI=10.1016/s0021-9258(18)61638-2;
RA Kitagawa H., Kitamura N., Hayashida H., Miyata T., Nakanishi S.;
RT "Differing expression patterns and evolution of the rat kininogen gene
RT family.";
RL J. Biol. Chem. 262:2190-2198(1987).
RN [10]
RP PROTEIN SEQUENCE OF 376-430.
RX PubMed=3335530; DOI=10.1016/s0021-9258(19)35447-x;
RA Enjyoji K., Kato H., Hayashi I., Oh-ishi S., Iwanaga S.;
RT "Purification and characterization of two kinds of low molecular weight
RT kininogens from rat (non-inflamed) plasma. One resistant and the second
RT sensitive to rat glandular kallikreins.";
RL J. Biol. Chem. 263:965-972(1988).
CC -!- FUNCTION: Kininogens are plasma glycoproteins with a number of
CC functions: (1) as precursor of the active peptide bradykinin they
CC effect smooth muscle contraction, induction of hypotension and increase
CC of vascular permeability. (2) They play a role in blood coagulation by
CC helping to position optimally prekallikrein and factor XI next to
CC factor XII. (3) They are inhibitor of thiol proteases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- INDUCTION: In response to an inflammatory stimulant. T-kininogen II
CC synthesis is induced and the plasma concentration of T-kininogen I is
CC raised.
CC -!- PTM: As T-kinin is preceded by a Met instead of an Arg or Lys, it is
CC not released from its precursor by either tissue or plasma kallikrein.
CC -!- MISCELLANEOUS: Rats express four types of kininogens: the classical HMW
CC and LMW kininogens produced by alternative splicing of the same gene,
CC and two additional LMW-like kininogens: T-I and T-II.
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DR EMBL; M11883; AAA41489.1; -; mRNA.
DR EMBL; M16454; AAA41568.1; -; Genomic_DNA.
DR EMBL; M14356; AAA41492.1; -; Genomic_DNA.
DR EMBL; X02299; CAA26162.1; ALT_SEQ; mRNA.
DR PIR; A01285; KGRTM.
DR PIR; A01286; KGRTT1.
DR PIR; A23897; A23897.
DR PIR; A27115; A27115.
DR AlphaFoldDB; P01048; -.
DR SMR; P01048; -.
DR MEROPS; I25.019; -.
DR GlyConnect; 604; 6 N-Linked glycans.
DR GlyGen; P01048; 5 sites, 11 N-linked glycans (1 site).
DR jPOST; P01048; -.
DR PRIDE; P01048; -.
DR InParanoid; P01048; -.
DR PhylomeDB; P01048; -.
DR PRO; PR:P01048; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0030195; P:negative regulation of blood coagulation; IBA:GO_Central.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR CDD; cd00042; CY; 3.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR027358; Kininogen-type_cystatin_dom.
DR InterPro; IPR018073; Prot_inh_cystat_CS.
DR Pfam; PF00031; Cystatin; 3.
DR SMART; SM00043; CY; 3.
DR SUPFAM; SSF54403; SSF54403; 3.
DR PROSITE; PS00287; CYSTATIN; 2.
DR PROSITE; PS51647; CYSTATIN_KININOGEN; 3.
PE 1: Evidence at protein level;
KW Acute phase; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Protease inhibitor; Pyrrolidone carboxylic acid; Reference proteome;
KW Repeat; Secreted; Signal; Thiol protease inhibitor; Vasoactive;
KW Vasodilator.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:3121623"
FT CHAIN 19..430
FT /note="T-kininogen 1"
FT /id="PRO_0000006699"
FT CHAIN 19..375
FT /note="T-kininogen 1 heavy chain"
FT /id="PRO_0000006700"
FT PEPTIDE 376..386
FT /note="T-kinin"
FT /id="PRO_0000006701"
FT CHAIN 387..430
FT /note="T-kininogen 1 light chain"
FT /id="PRO_0000006702"
FT DOMAIN 28..131
FT /note="Cystatin kininogen-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT DOMAIN 150..253
FT /note="Cystatin kininogen-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT DOMAIN 272..375
FT /note="Cystatin kininogen-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT REGION 411..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:3121623"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..404
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT DISULFID 83..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT DISULFID 107..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT DISULFID 141..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT DISULFID 205..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT DISULFID 228..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT DISULFID 263..266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT DISULFID 327..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT DISULFID 350..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT CONFLICT 7
FT /note="L -> V (in Ref. 5; CAA26162)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="Q -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="E -> K (in Ref. 1; AAA41489)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="K -> R (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="F -> S (in Ref. 1; AAA41489)"
FT /evidence="ECO:0000305"
FT CONFLICT 179..181
FT /note="REV -> TKI (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="S -> F (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="R -> H (in Ref. 5; CAA26162)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="E -> S (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="Q -> R (in Ref. 5; CAA26162)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="R -> Q (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="R -> G (in Ref. 2; no nucleotide entry and 5;
FT CAA26162)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="D -> E (in Ref. 5; CAA26162)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="H -> R (in Ref. 5; CAA26162 and 7; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="P -> S (in Ref. 1; AAA41489, 6; AA sequence, 8, 9
FT and 10; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 47775 MW; FEBBF28FA44793C3 CRC64;
MKLITILLLC SRLLPSLAQE EGAQELNCND ETVFQAVDTA LKKYNAELES GNQFVLYRVT
EGTKKDGAET LYSFKYQIKE GNCSVQSGLT WQDCDFKDAE EAATGECTTT LGKKENKFSV
ATQICNITPG KGPKKTEEDL CVGCFQPIPM DSSDLKPVLK HAVEHFNNNT KHTHLFALRE
VKSAHSQVVA GMNYKIIYSI VQTNCSKEDF PSLREDCVPL PYGDHGECTG HTHVDIHNTI
AGFSQSCDLY PGDDLFELLP KNCRGCPREI PVDSPELKEA LGHSIAQLNA QHNHIFYFKI
DTVKKATSQV VAGVIYVIEF IARETNCSKQ SKTELTADCE TKHLGQSLNC NANVYMRPWE
NKVVPTVRCQ ALDMMISRPP GFSPFRLVRV QETKEGTTRL LNSCEYKGRL SKARAGPAPD
HQAEASTVTP
