KNG1_HUMAN
ID KNG1_HUMAN Reviewed; 644 AA.
AC P01042; A8K474; B2RCR2; C9JEX1; P01043; Q53EQ0; Q6PAU9; Q7M4P1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=Kininogen-1;
DE AltName: Full=Alpha-2-thiol proteinase inhibitor;
DE AltName: Full=Fitzgerald factor;
DE AltName: Full=High molecular weight kininogen;
DE Short=HMWK;
DE AltName: Full=Williams-Fitzgerald-Flaujeac factor;
DE Contains:
DE RecName: Full=Kininogen-1 heavy chain;
DE Contains:
DE RecName: Full=T-kinin;
DE AltName: Full=Ile-Ser-Bradykinin;
DE Contains:
DE RecName: Full=Bradykinin {ECO:0000303|PubMed:3366244};
DE AltName: Full=Kallidin I;
DE Contains:
DE RecName: Full=Lysyl-bradykinin;
DE AltName: Full=Kallidin II;
DE Contains:
DE RecName: Full=Kininogen-1 light chain;
DE Contains:
DE RecName: Full=Low molecular weight growth-promoting factor;
DE Flags: Precursor;
GN Name=KNG1; Synonyms=BDK, KNG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LMW).
RX PubMed=6441591; DOI=10.1021/bi00319a005;
RA Ohkubo I., Kurachi K., Takasawa T., Shiokawa H., Sasaki M.;
RT "Isolation of a human cDNA for alpha 2-thiol proteinase inhibitor and its
RT identity with low molecular weight kininogen.";
RL Biochemistry 23:5691-5697(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS HMW AND LMW).
RC TISSUE=Liver;
RX PubMed=2989293; DOI=10.1016/s0021-9258(17)39515-7;
RA Takagaki Y., Kitamura N., Nakanishi S.;
RT "Cloning and sequence analysis of cDNAs for human high molecular weight and
RT low molecular weight prekininogens. Primary structures of two human
RT prekininogens.";
RL J. Biol. Chem. 260:8601-8609(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LMW).
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LMW), AND VARIANT THR-178.
RC TISSUE=Kidney;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-163; THR-178 AND
RP PRO-212.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-178.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LMW), AND VARIANT MET-197.
RC TISSUE=Kidney;
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 [9]
RP PROTEIN SEQUENCE OF 19-380, GLYCOSYLATION AT ASN-169 AND ASN-205, AND LACK
RP OF GLYCOSYLATION AT ASN-48.
RX PubMed=3484703; DOI=10.1111/j.1432-1033.1986.tb09421.x;
RA Kellermann J., Lottspeich F., Henschen A., Muller-Esterl W.;
RT "Completion of the primary structure of human high-molecular-mass
RT kininogen. The amino acid sequence of the entire heavy chain and evidence
RT for its evolution by gene triplication.";
RL Eur. J. Biochem. 154:471-478(1986).
RN [10]
RP PROTEIN SEQUENCE OF 376-389 (T-KININ), AND VARIANT 378-LEU--LYS-380 DEL.
RC TISSUE=Ascites;
RX PubMed=3828072; DOI=10.1515/bchm3.1986.367.2.1231;
RA Wunderer G., Walter I., Mueller E., Henschen A.;
RT "Human Ile-Ser-bradykinin, identical with rat T-kinin, is a major
RT permeability factor in ovarian carcinoma ascites.";
RL Biol. Chem. Hoppe-Seyler 367:1231-1234(1986).
RN [11]
RP PROTEIN SEQUENCE OF 376-389 (T-KININ), TISSUE SPECIFICITY, AND VARIANT
RP 378-LEU--LYS-380 DEL.
RX PubMed=2076202; DOI=10.1515/bchm3.1990.371.2.977;
RA Wunderer G., Walter I., Eschenbacher B., Lang M., Kellermann J.,
RA Kindermann G.;
RT "Ile-Ser-bradykinin is an aberrant permeability factor in various human
RT malignant effusions.";
RL Biol. Chem. Hoppe-Seyler 371:977-981(1990).
RN [12]
RP PROTEIN SEQUENCE OF 379-644.
RX PubMed=4054110; DOI=10.1111/j.1432-1033.1985.tb09199.x;
RA Lottspeich F., Kellermann J., Henschen A., Foertsch B., Mueller-Esterl W.;
RT "The amino acid sequence of the light chain of human high-molecular-mass
RT kininogen.";
RL Eur. J. Biochem. 152:307-314(1985).
RN [13]
RP PROTEIN SEQUENCE OF 380-389 (BRADYKININ), AND HYDROXYLATION AT PRO-383.
RX PubMed=3366244; DOI=10.1016/0014-5793(88)80427-7;
RA Kato H., Matsumura Y., Maeda H.;
RT "Isolation and identification of hydroxyproline analogues of bradykinin in
RT human urine.";
RL FEBS Lett. 232:252-254(1988).
RN [14]
RP PROTEIN SEQUENCE OF 381-389.
RX PubMed=4952632;
RA Pierce J.V.;
RT "Structural features of plasma kinins and kininogens.";
RL Fed. Proc. 27:52-57(1968).
RN [15]
RP PROTEIN SEQUENCE OF 431-434, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=7589467; DOI=10.1016/0014-5793(95)01037-f;
RA Straczek J., Maachi F., Le Nguyen D., Becchi M., Heulin M.H., Nabet P.,
RA Belleville F.;
RT "Purification from human plasma of a tetrapeptide that potentiates insulin-
RT like growth factor-I activity in chick embryo cartilage.";
RL FEBS Lett. 373:207-211(1995).
RN [16]
RP FUNCTION (BRADYKININ), AND DEGRADATION (BRADYKININ).
RX PubMed=6055465; DOI=10.1038/2151402a0;
RA Yang H.Y., Erdoes E.G.;
RT "Second kininase in human blood plasma.";
RL Nature 215:1402-1403(1967).
RN [17]
RP FUNCTION (BRADYKININ), AND DEGRADATION (BRADYKININ).
RX PubMed=4322742; DOI=10.1016/0005-2795(70)90017-6;
RA Yang H.Y., Erdoes E.G., Levin Y.;
RT "A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates
RT bradykinin.";
RL Biochim. Biophys. Acta 214:374-376(1970).
RN [18]
RP DISULFIDE BONDS.
RA Sueyoshi T., Miyata T., Kato H., Iwanaga S.;
RT "Disulfide bonds in bovine HMW kininogens.";
RL Seikagaku 56:808-808(1984).
RN [19]
RP GENE STRUCTURE.
RX PubMed=2989294; DOI=10.1016/s0021-9258(17)39516-9;
RA Kitamura N., Kitagawa H., Fukushima D., Takagaki Y., Miyata T.,
RA Nakanishi S.;
RT "Structural organization of the human kininogen gene and a model for its
RT evolution.";
RL J. Biol. Chem. 260:8610-8617(1985).
RN [20]
RP AMINO-ACID COMPOSITION OF 381-389, AND HYDROXYLATION AT PRO-383.
RX PubMed=3182782; DOI=10.1016/s0021-9258(18)37555-0;
RA Maeda H., Matsumura Y., Kato H.;
RT "Purification and identification of [hydroxyprolyl3]bradykinin in ascitic
RT fluid from a patient with gastric cancer.";
RL J. Biol. Chem. 263:16051-16054(1988).
RN [21]
RP GLYCOSYLATION AT ASN-294.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [22]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-169 AND ASN-294.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [23]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-48; ASN-169; ASN-205 AND
RP ASN-294.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Serum;
RX PubMed=19824718; DOI=10.1021/pr900603n;
RA Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A., Liotta L.A.,
RA Petricoin E.F. III;
RT "An initial characterization of the serum phosphoproteome.";
RL J. Proteome Res. 8:5523-5531(2009).
RN [25]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-169; ASN-205 AND ASN-294.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [26]
RP GLYCOSYLATION AT ASN-48; ASN-205 AND ASN-294.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [27]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-294, AND STRUCTURE OF
RP CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [29]
RP PHOSPHORYLATION AT SER-332.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [30]
RP VARIANT HAE6 LYS-379, AND INVOLVEMENT IN HAE6.
RX PubMed=31087670; DOI=10.1111/all.13869;
RA Bork K., Wulff K., Rossmann H., Steinmueller-Magin L., Braenne I.,
RA Witzke G., Hardt J.;
RT "Hereditary angioedema cosegregating with a novel kininogen 1 gene mutation
RT changing the N-terminal cleavage site of bradykinin.";
RL Allergy 74:2479-2481(2019).
RN [31]
RP VARIANT HAE6 ALA-574, AND INVOLVEMENT IN HAE6.
RX PubMed=33114181; DOI=10.3390/jcm9113402;
RA Loules G., Parsopoulou F., Zamanakou M., Csuka D., Bova M.,
RA Gonzalez-Quevedo T., Psarros F., Porebski G., Speletas M., Firinu D.,
RA Del Giacco S., Suffritti C., Makris M., Vatsiou S., Zanichelli A.,
RA Farkas H., Germenis A.E.;
RT "Deciphering the genetics of primary angioedema with normal levels of C1
RT inhibitor.";
RL J. Clin. Med. 9:0-0(2020).
CC -!- FUNCTION: Kininogens are inhibitors of thiol proteases. HMW-kininogen
CC plays an important role in blood coagulation by helping to position
CC optimally prekallikrein and factor XI next to factor XII; HMW-kininogen
CC inhibits the thrombin- and plasmin-induced aggregation of thrombocytes.
CC LMW-kininogen inhibits the aggregation of thrombocytes. LMW-kininogen
CC is in contrast to HMW-kininogen not involved in blood clotting.
CC -!- FUNCTION: [Bradykinin]: The active peptide bradykinin is a potent
CC vasodilatator that is released from HMW-kininogen shows a variety of
CC physiological effects: (A) influence in smooth muscle contraction, (B)
CC induction of hypotension, (C) natriuresis and diuresis, (D) decrease in
CC blood glucose level, (E) it is a mediator of inflammation and causes
CC (E1) increase in vascular permeability, (E2) stimulation of nociceptors
CC (4E3) release of other mediators of inflammation (e.g. prostaglandins),
CC (F) it has a cardioprotective effect (directly via bradykinin action,
CC indirectly via endothelium-derived relaxing factor action).
CC {ECO:0000305|PubMed:4322742, ECO:0000305|PubMed:6055465}.
CC -!- INTERACTION:
CC P01042; Q07021: C1QBP; NbExp=4; IntAct=EBI-6378713, EBI-347528;
CC P01042; Q10714: Ance; Xeno; NbExp=2; IntAct=EBI-6378713, EBI-115736;
CC PRO_0000006687; P46663: BDKRB1; NbExp=2; IntAct=EBI-6623250, EBI-6623218;
CC PRO_0000006688; Q9BYF1: ACE2; NbExp=5; IntAct=EBI-6623273, EBI-7730807;
CC PRO_0000006688; P30411: BDKRB2; NbExp=2; IntAct=EBI-6623273, EBI-6623386;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=HMW;
CC IsoId=P01042-1; Sequence=Displayed;
CC Name=LMW;
CC IsoId=P01042-2; Sequence=VSP_001261, VSP_001262;
CC Name=3;
CC IsoId=P01042-3; Sequence=VSP_047307, VSP_047308;
CC -!- TISSUE SPECIFICITY: Secreted in plasma. T-kinin is detected in
CC malignant ovarian, colon and breast carcinomas, but not in benign
CC tumors. {ECO:0000269|PubMed:2076202}.
CC -!- PTM: [Bradykinin]: Bradykinin is inactivated by ACE, which removes the
CC dipeptide Arg-Phe from its C-terminus. {ECO:0000269|PubMed:4322742,
CC ECO:0000269|PubMed:6055465}.
CC -!- PTM: Bradykinin is released from kininogen by plasma kallikrein.
CC {ECO:0000305|PubMed:3366244}.
CC -!- PTM: Hydroxylation of Pro-383 occurs prior to the release of
CC bradykinin. {ECO:0000269|PubMed:3182782, ECO:0000269|PubMed:3366244}.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000269|PubMed:26091039}.
CC -!- PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly core
CC 8 glycans. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
CC ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
CC ECO:0000269|PubMed:3484703}.
CC -!- POLYMORPHISM: The T-kinin peptide is missing residues 378 to 380,
CC probably as a result of a naturally occurring variant. The complete
CC sequence of the T-kinin peptide is therefore ISRPPGFSPFR. This peptide
CC is associated with malignant tumors but not with benign ones.
CC {ECO:0000269|PubMed:3828072}.
CC -!- DISEASE: High molecular weight kininogen deficiency (HMWK deficiency)
CC [MIM:228960]: Autosomal recessive coagulation defect. Patients with
CC HWMK deficiency do not have a hemorrhagic tendency, but they exhibit
CC abnormal surface-mediated activation of fibrinolysis. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Angioedema, hereditary, 6 (HAE6) [MIM:619363]: A form of
CC angioedema, a disorder characterized by episodic local swelling
CC involving subcutaneous or submucous tissue of the upper respiratory and
CC gastrointestinal tracts, face, extremities, and genitalia. HAE6 is an
CC autosomal dominant form with onset in adulthood.
CC {ECO:0000269|PubMed:31087670, ECO:0000269|PubMed:33114181}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=High molecular weight kininogen
CC entry;
CC URL="https://en.wikipedia.org/wiki/High-molecular_weight_kininogen";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/kng/";
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DR EMBL; K02566; AAA35497.1; -; mRNA.
DR EMBL; M11437; AAB59550.1; -; Genomic_DNA.
DR EMBL; M11438; AAB59550.1; JOINED; Genomic_DNA.
DR EMBL; M11521; AAB59550.1; JOINED; Genomic_DNA.
DR EMBL; M11522; AAB59550.1; JOINED; Genomic_DNA.
DR EMBL; M11523; AAB59550.1; JOINED; Genomic_DNA.
DR EMBL; M11524; AAB59550.1; JOINED; Genomic_DNA.
DR EMBL; M11525; AAB59550.1; JOINED; Genomic_DNA.
DR EMBL; M11526; AAB59550.1; JOINED; Genomic_DNA.
DR EMBL; M11527; AAB59550.1; JOINED; Genomic_DNA.
DR EMBL; M11528; AAB59550.1; JOINED; Genomic_DNA.
DR EMBL; M11437; AAB59551.1; -; Genomic_DNA.
DR EMBL; M11438; AAB59551.1; JOINED; Genomic_DNA.
DR EMBL; M11521; AAB59551.1; JOINED; Genomic_DNA.
DR EMBL; M11522; AAB59551.1; JOINED; Genomic_DNA.
DR EMBL; M11523; AAB59551.1; JOINED; Genomic_DNA.
DR EMBL; M11524; AAB59551.1; JOINED; Genomic_DNA.
DR EMBL; M11525; AAB59551.1; JOINED; Genomic_DNA.
DR EMBL; M11526; AAB59551.1; JOINED; Genomic_DNA.
DR EMBL; M11527; AAB59551.1; JOINED; Genomic_DNA.
DR EMBL; M11528; AAB59551.1; JOINED; Genomic_DNA.
DR EMBL; AK315230; BAG37659.1; -; mRNA.
DR EMBL; AK290839; BAF83528.1; -; mRNA.
DR EMBL; AK223589; BAD97309.1; -; mRNA.
DR EMBL; AY248697; AAO61092.1; -; Genomic_DNA.
DR EMBL; AC109780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78179.1; -; Genomic_DNA.
DR EMBL; BC060039; AAH60039.1; -; mRNA.
DR CCDS; CCDS3281.1; -. [P01042-2]
DR CCDS; CCDS43183.1; -. [P01042-1]
DR CCDS; CCDS54695.1; -. [P01042-3]
DR PIR; A01279; KGHUH1.
DR PIR; A01280; KGHUL1.
DR PIR; S13279; S13279.
DR RefSeq; NP_000884.1; NM_000893.3. [P01042-2]
DR RefSeq; NP_001095886.1; NM_001102416.2. [P01042-1]
DR RefSeq; NP_001159923.1; NM_001166451.1. [P01042-3]
DR PDB; 1NY2; X-ray; 2.30 A; 4=381-385.
DR PDB; 2WOK; X-ray; 1.70 A; B=381-389.
DR PDB; 4ASQ; X-ray; 1.99 A; P=381-389.
DR PDB; 4ASR; X-ray; 1.90 A; P=381-389.
DR PDB; 4ECB; X-ray; 2.20 A; A/B=498-507.
DR PDB; 4ECC; X-ray; 2.20 A; A=498-510.
DR PDB; 5I25; X-ray; 2.85 A; B=601-608.
DR PDB; 6F27; NMR; -; A=380-388.
DR PDB; 6F3V; NMR; -; A=381-389.
DR PDB; 6F3W; NMR; -; A=381-389.
DR PDB; 6F3X; NMR; -; A=380-388.
DR PDB; 6F3Y; NMR; -; A=380-388.
DR PDBsum; 1NY2; -.
DR PDBsum; 2WOK; -.
DR PDBsum; 4ASQ; -.
DR PDBsum; 4ASR; -.
DR PDBsum; 4ECB; -.
DR PDBsum; 4ECC; -.
DR PDBsum; 5I25; -.
DR PDBsum; 6F27; -.
DR PDBsum; 6F3V; -.
DR PDBsum; 6F3W; -.
DR PDBsum; 6F3X; -.
DR PDBsum; 6F3Y; -.
DR AlphaFoldDB; P01042; -.
DR BMRB; P01042; -.
DR SMR; P01042; -.
DR BioGRID; 110026; 49.
DR IntAct; P01042; 31.
DR MINT; P01042; -.
DR STRING; 9606.ENSP00000265023; -.
DR BindingDB; P01042; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR MEROPS; I25.016; -.
DR MEROPS; I25.017; -.
DR MEROPS; I25.950; -.
DR CarbonylDB; P01042; -.
DR GlyConnect; 810; 60 N-Linked glycans (5 sites), 1 O-Linked glycan (1 site).
DR GlyGen; P01042; 26 sites, 82 N-linked glycans (5 sites), 13 O-linked glycans (19 sites).
DR iPTMnet; P01042; -.
DR PhosphoSitePlus; P01042; -.
DR BioMuta; KNG1; -.
DR DMDM; 124056474; -.
DR SWISS-2DPAGE; P01042; -.
DR CPTAC; CPTAC-687; -.
DR CPTAC; non-CPTAC-1138; -.
DR EPD; P01042; -.
DR jPOST; P01042; -.
DR MassIVE; P01042; -.
DR PaxDb; P01042; -.
DR PeptideAtlas; P01042; -.
DR PRIDE; P01042; -.
DR ProteomicsDB; 51315; -. [P01042-1]
DR ProteomicsDB; 51316; -. [P01042-2]
DR ProteomicsDB; 9908; -.
DR Antibodypedia; 888; 814 antibodies from 43 providers.
DR DNASU; 3827; -.
DR Ensembl; ENST00000287611.8; ENSP00000287611.2; ENSG00000113889.14. [P01042-2]
DR Ensembl; ENST00000447445.1; ENSP00000396025.1; ENSG00000113889.14. [P01042-3]
DR Ensembl; ENST00000644859.2; ENSP00000493985.1; ENSG00000113889.14. [P01042-1]
DR GeneID; 3827; -.
DR KEGG; hsa:3827; -.
DR MANE-Select; ENST00000644859.2; ENSP00000493985.1; NM_001102416.3; NP_001095886.1.
DR UCSC; uc003fqr.4; human. [P01042-1]
DR CTD; 3827; -.
DR DisGeNET; 3827; -.
DR GeneCards; KNG1; -.
DR HGNC; HGNC:6383; KNG1.
DR HPA; ENSG00000113889; Tissue enriched (liver).
DR MalaCards; KNG1; -.
DR MIM; 228960; phenotype.
DR MIM; 612358; gene.
DR MIM; 619363; phenotype.
DR neXtProt; NX_P01042; -.
DR OpenTargets; ENSG00000113889; -.
DR Orphanet; 483; Congenital high-molecular-weight kininogen deficiency.
DR Orphanet; 599418; Hereditary angioedema with normal C1Inh not related to F12 or PLG variant.
DR PharmGKB; PA225; -.
DR VEuPathDB; HostDB:ENSG00000113889; -.
DR eggNOG; ENOG502RYAC; Eukaryota.
DR GeneTree; ENSGT00950000182930; -.
DR HOGENOM; CLU_029531_0_0_1; -.
DR InParanoid; P01042; -.
DR OMA; DQGHGHQ; -.
DR OrthoDB; 740995at2759; -.
DR PhylomeDB; P01042; -.
DR TreeFam; TF351852; -.
DR PathwayCommons; P01042; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; P01042; -.
DR SIGNOR; P01042; -.
DR BioGRID-ORCS; 3827; 11 hits in 1070 CRISPR screens.
DR ChiTaRS; KNG1; human.
DR EvolutionaryTrace; P01042; -.
DR GeneWiki; Kininogen_1; -.
DR GenomeRNAi; 3827; -.
DR Pharos; P01042; Tbio.
DR PRO; PR:P01042; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P01042; protein.
DR Bgee; ENSG00000113889; Expressed in renal medulla and 94 other tissues.
DR Genevisible; P01042; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; NAS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0030195; P:negative regulation of blood coagulation; IDA:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0045861; P:negative regulation of proteolysis; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR CDD; cd00042; CY; 3.
DR DisProt; DP01861; -.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR002395; Kininogen.
DR InterPro; IPR027358; Kininogen-type_cystatin_dom.
DR InterPro; IPR018073; Prot_inh_cystat_CS.
DR Pfam; PF00031; Cystatin; 3.
DR PRINTS; PR00334; KININOGEN.
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 3D-structure; Alternative splicing; Blood coagulation;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Hemostasis; Hydroxylation; Inflammatory response; Phosphoprotein;
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:2989293,
FT ECO:0000269|PubMed:3484703"
FT CHAIN 19..644
FT /note="Kininogen-1"
FT /id="PRO_0000006685"
FT CHAIN 19..380
FT /note="Kininogen-1 heavy chain"
FT /id="PRO_0000006686"
FT PEPTIDE 376..389
FT /note="T-kinin"
FT /id="PRO_0000372485"
FT PEPTIDE 380..389
FT /note="Lysyl-bradykinin"
FT /id="PRO_0000006687"
FT PEPTIDE 381..389
FT /note="Bradykinin"
FT /evidence="ECO:0000269|PubMed:3182782,
FT ECO:0000269|PubMed:4952632"
FT /id="PRO_0000006688"
FT CHAIN 390..644
FT /note="Kininogen-1 light chain"
FT /id="PRO_0000006689"
FT PEPTIDE 431..434
FT /note="Low molecular weight growth-promoting factor"
FT /id="PRO_0000006690"
FT DOMAIN 28..132
FT /note="Cystatin kininogen-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT DOMAIN 151..254
FT /note="Cystatin kininogen-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT DOMAIN 273..376
FT /note="Cystatin kininogen-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT REPEAT 420..449
FT REPEAT 450..479
FT REPEAT 480..510
FT REGION 120..153
FT /note="O-glycosylated at one site only"
FT REGION 387..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..514
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 48
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:3484703"
FT SITE 379..380
FT /note="Cleavage; by kallikrein"
FT /evidence="ECO:0000303|PubMed:3366244"
FT SITE 387..388
FT /note="Cleavage; by ACE"
FT /evidence="ECO:0000269|PubMed:4322742,
FT ECO:0000269|PubMed:6055465"
FT SITE 389..390
FT /note="Cleavage; by kallikrein"
FT /evidence="ECO:0000303|PubMed:3366244"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid; in mature form"
FT /evidence="ECO:0000250|UniProtKB:P01045"
FT MOD_RES 332
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:19824718, ECO:0007744|PubMed:24275569"
FT MOD_RES 383
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:3182782,
FT ECO:0000269|PubMed:3366244"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:3484703"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:3484703"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19838169"
FT CARBOHYD 401
FT /note="O-linked (GalNAc...) threonine"
FT CARBOHYD 533
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:4054110"
FT CARBOHYD 542
FT /note="O-linked (GalNAc...) threonine"
FT CARBOHYD 546
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:4054110"
FT CARBOHYD 557
FT /note="O-linked (GalNAc...) threonine"
FT CARBOHYD 571
FT /note="O-linked (GalNAc...) threonine"
FT CARBOHYD 577
FT /note="O-linked (GalNAc...) serine"
FT CARBOHYD 628
FT /note="O-linked (GalNAc...) threonine"
FT DISULFID 28..614
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979,
FT ECO:0000269|Ref.18"
FT DISULFID 83..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979,
FT ECO:0000269|Ref.18"
FT DISULFID 107..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979,
FT ECO:0000269|Ref.18"
FT DISULFID 142..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979,
FT ECO:0000269|Ref.18"
FT DISULFID 206..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979,
FT ECO:0000269|Ref.18"
FT DISULFID 229..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979,
FT ECO:0000269|Ref.18"
FT DISULFID 264..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979,
FT ECO:0000269|Ref.18"
FT DISULFID 328..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979,
FT ECO:0000269|Ref.18"
FT DISULFID 351..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00979,
FT ECO:0000269|Ref.18"
FT VAR_SEQ 189..224
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047307"
FT VAR_SEQ 402..643
FT /note="VSPPHTSMAPAQDEERDSGKEQGHTRRHDWGHEKQRKHNLGHGHKHERDQGH
FT GHQRGHGLGHGHEQQHGLGHGHKFKLDDDLEHQGGHVLDHGHKHKHGHGHGKHKNKGKK
FT NGKHNGWKTEHLASSSEDSTTPSAQTQEKTEGPTPIPSLAKPGVTVTFSDFQDSDLIAT
FT MMPPISPAPIQSDDDWIPDIQIDPNGLSFNPISDFPDTTSPKCPGRPWKSVSEINPTTQ
FT MKESYYFDLTDGL -> SHLRSCEYKGRPPKAGAEPASEREV (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047308"
FT VAR_SEQ 402..427
FT /note="VSPPHTSMAPAQDEERDSGKEQGHTR -> SHLRSCEYKGRPPKAGAEPASE
FT REVS (in isoform LMW)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:6441591,
FT ECO:0000303|Ref.4"
FT /id="VSP_001261"
FT VAR_SEQ 428..644
FT /note="Missing (in isoform LMW)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:6441591,
FT ECO:0000303|Ref.4"
FT /id="VSP_001262"
FT VARIANT 163
FT /note="G -> S (in dbSNP:rs5030015)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_019277"
FT VARIANT 178
FT /note="M -> T (in dbSNP:rs1656922)"
FT /evidence="ECO:0000269|Ref.4, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.7"
FT /id="VAR_019278"
FT VARIANT 197
FT /note="I -> M (in dbSNP:rs2304456)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028937"
FT VARIANT 212
FT /note="L -> P (in dbSNP:rs5030024)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_019279"
FT VARIANT 378..380
FT /note="Missing (in T-kinin peptide)"
FT /evidence="ECO:0000269|PubMed:2076202,
FT ECO:0000269|PubMed:3828072"
FT /id="VAR_055233"
FT VARIANT 379
FT /note="M -> K (in HAE6)"
FT /evidence="ECO:0000269|PubMed:31087670"
FT /id="VAR_085817"
FT VARIANT 430
FT /note="D -> E (in dbSNP:rs5030084)"
FT /id="VAR_048853"
FT VARIANT 574
FT /note="P -> A (in HAE6; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:33114181"
FT /id="VAR_085818"
FT VARIANT 581
FT /note="I -> T (in dbSNP:rs710446)"
FT /id="VAR_048854"
FT VARIANT 642
FT /note="G -> A (in dbSNP:rs5030087)"
FT /id="VAR_048855"
FT CONFLICT 33
FT /note="L -> F (in Ref. 3; BAF83528)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="V -> A (in Ref. 3; BAF83528)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="I -> T (in Ref. 5; AAO61092 and 12; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:6F3V"
SQ SEQUENCE 644 AA; 71957 MW; 3132B4DF2954C24E CRC64;
MKLITILFLC SRLLLSLTQE SQSEEIDCND KDLFKAVDAA LKKYNSQNQS NNQFVLYRIT
EATKTVGSDT FYSFKYEIKE GDCPVQSGKT WQDCEYKDAA KAATGECTAT VGKRSSTKFS
VATQTCQITP AEGPVVTAQY DCLGCVHPIS TQSPDLEPIL RHGIQYFNNN TQHSSLFMLN
EVKRAQRQVV AGLNFRITYS IVQTNCSKEN FLFLTPDCKS LWNGDTGECT DNAYIDIQLR
IASFSQNCDI YPGKDFVQPP TKICVGCPRD IPTNSPELEE TLTHTITKLN AENNATFYFK
IDNVKKARVQ VVAGKKYFID FVARETTCSK ESNEELTESC ETKKLGQSLD CNAEVYVVPW
EKKIYPTVNC QPLGMISLMK RPPGFSPFRS SRIGEIKEET TVSPPHTSMA PAQDEERDSG
KEQGHTRRHD WGHEKQRKHN LGHGHKHERD QGHGHQRGHG LGHGHEQQHG LGHGHKFKLD
DDLEHQGGHV LDHGHKHKHG HGHGKHKNKG KKNGKHNGWK TEHLASSSED STTPSAQTQE
KTEGPTPIPS LAKPGVTVTF SDFQDSDLIA TMMPPISPAP IQSDDDWIPD IQIDPNGLSF
NPISDFPDTT SPKCPGRPWK SVSEINPTTQ MKESYYFDLT DGLS
