KLK10_RAT
ID KLK10_RAT Reviewed; 259 AA.
AC P36375;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Glandular kallikrein-10;
DE Short=K10;
DE Short=rGK-10;
DE EC=3.4.21.35;
DE AltName: Full=Endopeptidase K;
DE AltName: Full=Proteinase B;
DE AltName: Full=T-kininogenase;
DE AltName: Full=Tissue kallikrein;
DE Contains:
DE RecName: Full=T-kininogenase light chain;
DE Contains:
DE RecName: Full=T-kininogenase heavy chain;
DE Flags: Precursor;
GN Name=Klk10; Synonyms=Klk-10;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-259, PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney, and Submandibular gland;
RX PubMed=1420203; DOI=10.1021/bi00159a036;
RA Ma J.-X., Chao J., Chao L.;
RT "Molecular cloning and characterization of rKlk10, a cDNA encoding T-
RT kininogenase from rat submandibular gland and kidney.";
RL Biochemistry 31:10922-10928(1992).
RN [3]
RP PROTEIN SEQUENCE OF 25-47 AND 112-132.
RC TISSUE=Submandibular gland;
RX PubMed=3482210; DOI=10.1093/oxfordjournals.jbchem.a122185;
RA Kato H., Nakanishi E., Enjyoji K., Hayashi I., Oh-Ishi S., Iwanaga S.;
RT "Characterization of serine proteinases isolated from rat submaxillary
RT gland: with special reference to the degradation of rat kininogens by these
RT enzymes.";
RL J. Biochem. 102:1389-1404(1987).
RN [4]
RP PROTEIN SEQUENCE OF 25-47 AND 112-148.
RC TISSUE=Submandibular gland;
RX PubMed=2303430; DOI=10.1016/s0021-9258(19)39875-8;
RA Xiong W., Chen L.-M., Chao J.;
RT "Purification and characterization of a kallikrein-like T-kininogenase.";
RL J. Biol. Chem. 265:2822-2827(1990).
RN [5]
RP PROTEIN SEQUENCE OF 25-47; 110-139 AND 194-247.
RC TISSUE=Submandibular gland;
RX PubMed=2026164; DOI=10.1111/j.1432-1033.1991.tb15928.x;
RA Gutman N., Elmoujahed A., Brillard M., du Sorbier B., Gauthier F.;
RT "Microheterogeneity of rat submaxillary gland kallikrein k10, a member of
RT the kallikrein family.";
RL Eur. J. Biochem. 197:425-429(1991).
CC -!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in
CC kininogen to release Lys-bradykinin. This protein may be involved in
CC the regulation of renal function.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule
CC substrates. Highly selective action to release kallidin (lysyl-
CC bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-
CC Xaa.; EC=3.4.21.35;
CC -!- SUBUNIT: Heterodimer of a light chain and heavy chain linked by a
CC disulfide bond.
CC -!- TISSUE SPECIFICITY: Kidney and submandibular gland, where it is found
CC in the granular convoluted tubule and striated duct cells. It is likely
CC that the enzyme is mainly synthesized in the granular convoluted
CC tubules and then transferred to other tissues by release into the
CC vasculature or interstitial space. {ECO:0000269|PubMed:1420203}.
CC -!- PTM: Probably N- and O-glycosylated.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AABR03000574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S48142; AAB24071.1; -; mRNA.
DR PIR; A44284; A44284.
DR PIR; B35545; B35545.
DR RefSeq; NP_001128645.1; NM_001135173.1.
DR RefSeq; XP_003748896.1; XM_003748848.3.
DR AlphaFoldDB; P36375; -.
DR SMR; P36375; -.
DR STRING; 10116.ENSRNOP00000048581; -.
DR MEROPS; S01.165; -.
DR GlyGen; P36375; 2 sites.
DR iPTMnet; P36375; -.
DR PhosphoSitePlus; P36375; -.
DR PaxDb; P36375; -.
DR Ensembl; ENSRNOT00000045756; ENSRNOP00000050040; ENSRNOG00000046297.
DR GeneID; 292858; -.
DR KEGG; rno:292858; -.
DR UCSC; RGD:1303242; rat.
DR CTD; 292858; -.
DR RGD; 1303242; Klk10.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; P36375; -.
DR OMA; WLENDIS; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P36375; -.
DR TreeFam; TF331065; -.
DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR PRO; PR:P36375; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000046297; Expressed in kidney and 3 other tissues.
DR Genevisible; P36375; RN.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT PROPEP 19..24
FT /note="Activation peptide"
FT /evidence="ECO:0000305|PubMed:2026164,
FT ECO:0000305|PubMed:2303430, ECO:0000305|PubMed:3482210"
FT /id="PRO_0000028013"
FT CHAIN 25..259
FT /note="Glandular kallikrein-10"
FT /id="PRO_0000028014"
FT CHAIN 25..111
FT /note="T-kininogenase light chain"
FT /id="PRO_0000028015"
FT CHAIN 112..259
FT /note="T-kininogenase heavy chain"
FT /id="PRO_0000028016"
FT DOMAIN 25..256
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 63
FT /note="Charge relay system"
FT ACT_SITE 118
FT /note="Charge relay system"
FT ACT_SITE 211
FT /note="Charge relay system"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 48..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 150..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 182..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 207..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 44
FT /note="N -> IET (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..131
FT /note="IT -> DS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="E -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="S -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 28981 MW; 18DBC31C6086E5F7 CRC64;
MWFLILFLAL SLGGIDAAPP GQSRIVGGYK CEKNSQPWQV AIINEYLCGG VLIDPSWVIT
AAHCYSNYYH VLLGRNNLFE DEPFAQYRFV NQSFPHPDYK PFLMRNHTRQ RGDDYSNDLM
LLHLSEPADI TDGVKVIDLP TEEPKVGSTC LASGWGSTKP LNWELPDDLQ CVNIHLLSNE
KCIEAYEQKV TDLMLCAGEM DGRKDTCKGD SGGPLICDGV LQGITSWGNV PCAEPYNPGV
YTKLIKFTSW IKEVMKENP
