Reviewed, UniProtKB/Swiss-Prot P36375 (KLK10_RAT)

Names and origin

Protein names

Recommended name:
    Glandular kallikrein-10
    EC=3.4.21.35
Alternative name(s):
    Tissue kallikrein
    T-kininogenase
    K10
    Proteinase B
    Endopeptidase K
Cleaved into the following 2 chains:
    1- Recommended name:
            T-kininogenase light chain
    2- Recommended name:
            T-kininogenase heavy chain

Gene names

Name:	Klk10
Synonyms:	Klk-10

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	259 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. This protein may be involved in the regulation of renal function.
Catalytic activity	Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.
Subunit structure	Heterodimer of a light chain and heavy chain linked by a disulfide bond.
Tissue specificity	Kidney and submandibular gland, where it is found in the granular convoluted tubule and striated duct cells. It is likely that the enzyme is mainly synthesized in the granular convoluted tubules and then transferred to other tissues by release into the vasculature or interstitial space. Ref.2
Post-translational modification	Probably N- and O-glycosylated.
Sequence similarities	Belongs to the peptidase S1 family. Kallikrein subfamily. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Probable
	Propeptide	19 – 24	6	Activation peptide Probable		PRO_0000028013
	Chain	25 – 259	235	Glandular kallikrein-10		PRO_0000028014
	Chain	25 – 111	87	T-kininogenase light chain		PRO_0000028015
	Chain	112 – 259	148	T-kininogenase heavy chain		PRO_0000028016
Regions
	Domain	25 – 256	232	Peptidase S1
Sites
	Active site	63	1	Charge relay system
	Active site	118	1	Charge relay system
	Active site	211	1	Charge relay system
Amino acid modifications
	Glycosylation	91	1	N-linked (GlcNAc...) Potential
	Glycosylation	106	1	N-linked (GlcNAc...) Potential
	Disulfide bond	31 ↔ 171		By similarity
	Disulfide bond	48 ↔ 64		By similarity
	Disulfide bond	150 ↔ 217		By similarity
	Disulfide bond	182 ↔ 196		By similarity
	Disulfide bond	207 ↔ 232		By similarity
Experimental info
	Sequence conflict	44	1	N → IET AA sequence Ref.4
	Sequence conflict	130 – 131	2	IT → DS AA sequence Ref.3
	Sequence conflict	143	1	E → G AA sequence Ref.4
	Sequence conflict	148	1	S → G AA sequence Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P36375-1 [UniParc]. Last modified June 12, 2007. Version 2. Checksum: 18DBC31C6086E5F7	FASTA	259	28,981
	10 20 30 40 50 60 MWFLILFLAL SLGGIDAAPP GQSRIVGGYK CEKNSQPWQV AIINEYLCGG VLIDPSWVIT 70 80 90 100 110 120 AAHCYSNYYH VLLGRNNLFE DEPFAQYRFV NQSFPHPDYK PFLMRNHTRQ RGDDYSNDLM 130 140 150 160 170 180 LLHLSEPADI TDGVKVIDLP TEEPKVGSTC LASGWGSTKP LNWELPDDLQ CVNIHLLSNE 190 200 210 220 230 240 KCIEAYEQKV TDLMLCAGEM DGRKDTCKGD SGGPLICDGV LQGITSWGNV PCAEPYNPGV 250 YTKLIKFTSW IKEVMKENP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed: 15057822] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[2]	"Molecular cloning and characterization of rKlk10, a cDNA encoding T-kininogenase from rat submandibular gland and kidney." Ma J.-X., Chao J., Chao L. Biochemistry 31:10922-10928(1992) [PubMed: 1420203] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-259, PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY. Tissue: Kidney and Submandibular gland.
[3]	"Characterization of serine proteinases isolated from rat submaxillary gland: with special reference to the degradation of rat kininogens by these enzymes." Kato H., Nakanishi E., Enjyoji K., Hayashi I., Oh-Ishi S., Iwanaga S. J. Biochem. 102:1389-1404(1987) [PubMed: 3482210] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-47 AND 112-132. Tissue: Submandibular gland.
[4]	"Purification and characterization of a kallikrein-like T-kininogenase." Xiong W., Chen L.-M., Chao J. J. Biol. Chem. 265:2822-2827(1990) [PubMed: 2303430] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-47 AND 112-148. Tissue: Submandibular gland.
[5]	"Microheterogeneity of rat submaxillary gland kallikrein k10, a member of the kallikrein family." Gutman N., Elmoujahed A., Brillard M., du Sorbier B., Gauthier F. Eur. J. Biochem. 197:425-429(1991) [PubMed: 2026164] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-47; 110-139 AND 194-247. Tissue: Submandibular gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AABR03000574 Genomic DNA. No translation available. S48142 mRNA. Translation: AAB24071.1.
IPI	IPI00886439.
PIR	A44284. B35545.
RefSeq	NP_001128645.1.
UniGene	Rn.21391
3D structure databases
HSSP	HSSP built from PDB template 1TON based on UniProtKB P00759.
SMR	P36375. Positions 10-244.
ModBase	Search...
Protein family/group databases
MEROPS	S01.165.
Genome annotation databases
Ensembl	ENSRNOG00000029266. Rattus norvegicus. [Contig view]
GeneID	292858.
KEGG	rno:292858.
Organism-specific databases
RGD	1303242. Klk10.
Phylogenomic databases
HOVERGEN	P36375.
Enzyme and pathway databases
BRENDA	3.4.21.35. 248.
Gene expression databases
ArrayExpress	P36375.
GermOnline	ENSRNOG00000029266. Rattus norvegicus.
Family and domain databases
InterPro	IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KLK10_RAT

Accession

Primary (citable) accession number: P36375

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 12, 2007
Last modified:	May 26, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)