KNT2_RAT
ID KNT2_RAT Reviewed; 430 AA.
AC P08932; Q5M894;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=T-kininogen 2;
DE AltName: Full=Alpha-1-MAP;
DE AltName: Full=Major acute phase protein;
DE AltName: Full=T-kininogen II;
DE AltName: Full=Thiostatin;
DE Contains:
DE RecName: Full=T-kininogen 2 heavy chain;
DE AltName: Full=T-kininogen II heavy chain;
DE Contains:
DE RecName: Full=T-kinin;
DE Contains:
DE RecName: Full=T-kininogen 2 light chain;
DE AltName: Full=T-kininogen II light chain;
DE Flags: Precursor;
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 [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-430, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2413019; DOI=10.1016/s0021-9258(17)38986-x;
RA Anderson K.P., Heath E.C.;
RT "The relationship between rat major acute phase protein and the
RT kininogens.";
RL J. Biol. Chem. 260:12065-12071(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 238-430.
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).
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41570.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC088161; AAH88161.1; -; mRNA.
DR EMBL; M11661; AAA41570.1; ALT_FRAME; mRNA.
DR EMBL; M11885; AAA41491.1; -; mRNA.
DR PIR; B28055; B28055.
DR RefSeq; NP_001009628.1; NM_001009628.1.
DR AlphaFoldDB; P08932; -.
DR SMR; P08932; -.
DR STRING; 10116.ENSRNOP00000055278; -.
DR MEROPS; I25.019; -.
DR GlyConnect; 604; 6 N-Linked glycans.
DR GlyGen; P08932; 5 sites, 11 N-linked glycans (1 site).
DR jPOST; P08932; -.
DR PaxDb; P08932; -.
DR PRIDE; P08932; -.
DR GeneID; 288001; -.
DR KEGG; rno:288001; -.
DR UCSC; RGD:1359376; rat.
DR CTD; 3827; -.
DR VEuPathDB; HostDB:ENSRNOG00000030387; -.
DR eggNOG; ENOG502RYAC; Eukaryota.
DR OrthoDB; 740995at2759; -.
DR PhylomeDB; P08932; -.
DR TreeFam; TF351852; -.
DR PRO; PR:P08932; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000030387; Expressed in liver and 16 other tissues.
DR ExpressionAtlas; P08932; baseline and differential.
DR Genevisible; P08932; RN.
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 CHAIN 19..430
FT /note="T-kininogen 2"
FT /id="PRO_0000006703"
FT CHAIN 19..375
FT /note="T-kininogen 2 heavy chain"
FT /id="PRO_0000006704"
FT PEPTIDE 376..386
FT /note="T-kinin"
FT /id="PRO_0000006705"
FT CHAIN 387..430
FT /note="T-kininogen 2 light chain"
FT /id="PRO_0000006706"
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 410..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P01048"
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 26..27
FT /note="MD -> LN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="C -> R (in Ref. 2; AAA41570)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="L -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="E -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="F -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="T -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="N -> D (in Ref. 2; AAA41570)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="F -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="R -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="Y -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="A -> L (in Ref. 2; AAA41570)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 47704 MW; D94628D848C81525 CRC64;
MKLITILLLC SRLLPSLAQE EGAQEMDCND ETVFQAVDTA LKKYNAELES GNQFLLYRVT
EGTKKDGAET LYSFKYQIKE GNCSVQSGLT WQDCDFKDAE EAATGECTTT LGKKENKFSV
ATQICNITPG KGPKKTEEDL CVGCFQPIPM DSSDLKPVLK HAVEHFNNNT KHTHLFALTE
VKSAHSQVVA GMNYKIIYSI VQTNCSKEDF PFLREDCVPL PYGDHGECRG HTYVDIHNTI
AGFSQSCDLY PGDDLFSLLP KKCFGCPKNI PVDSPELKEA LGHSIAQLNA QHNHLFYFKI
DTVKKATSQV VAGTKYVIEF IARETNCSKQ TNTELTADCE TKHLGQSLNC NANVYMRPWE
NKVVPTVRCQ ALDMMISRPP GFSPFRLVQV QETKEGTTRL LNSCEYKGRL SKAGAGPAPD
HQAEASTVTP
