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P15947

- KLK1_MOUSE

UniProt

P15947 - KLK1_MOUSE

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Protein

Kallikrein-1

Gene

Klk1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651Charge relay system
Active sitei120 – 1201Charge relay system
Active sitei213 – 2131Charge relay system

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.
REACT_235886. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Protein family/group databases

MEROPSiS01.167.

Names & Taxonomyi

Protein namesi
Recommended name:
Kallikrein-1 (EC:3.4.21.35)
Alternative name(s):
Glandular kallikrein K1
KAL-B
Renal kallikrein
Tissue kallikrein-6
Short name:
mGK-6
Gene namesi
Name:Klk1
Synonyms:Klk-6, Klk6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:102850. Klk1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818CuratedAdd
BLAST
Propeptidei19 – 246Activation peptide1 PublicationPRO_0000027975
Chaini25 – 261237Kallikrein-1PRO_0000027976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 173PROSITE-ProRule annotation
Disulfide bondi50 ↔ 66PROSITE-ProRule annotation
Glycosylationi102 – 1021N-linked (GlcNAc...)Curated
Disulfide bondi152 ↔ 219PROSITE-ProRule annotation
Disulfide bondi184 ↔ 198PROSITE-ProRule annotation
Disulfide bondi209 ↔ 234PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP15947.
PaxDbiP15947.
PRIDEiP15947.

Expressioni

Gene expression databases

BgeeiP15947.
CleanExiMM_KLK1.
GenevestigatoriP15947.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000074659.

Structurei

3D structure databases

ProteinModelPortaliP15947.
SMRiP15947. Positions 25-260.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 258234Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Kallikrein subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118862.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP15947.
KOiK01325.
OMAiFNTWIRE.
OrthoDBiEOG75B84T.
PhylomeDBiP15947.
TreeFamiTF331065.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15947-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRFLILFLAL SLGGIDAAPP VQSRIVGGFN CEKNSQPWQV AVYRFTKYQC
60 70 80 90 100
GGILLNANWV LTAAHCHNDK YQVWLGKNNF LEDEPSAQHR LVSKAIPHPD
110 120 130 140 150
FNMSLLNEHT PQPEDDYSND LMLLRLKKPA DITDVVKPID LPTEEPKLGS
160 170 180 190 200
TCLASGWGSI TPVKYEYPDE LQCVNLKLLP NEDCAKAHIE KVTDDMLCAG
210 220 230 240 250
DMDGGKDTCA GDSGGPLICD GVLQGITSWG PSPCGKPNVP GIYTRVLNFN
260
TWIRETMAEN D
Length:261
Mass (Da):28,775
Last modified:December 5, 2001 - v3
Checksum:i7850DDFDBFFB94B8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571A → V in AAG11389. (PubMed:3007510)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13500, M13498, M13499 Genomic DNA. Translation: AAG11389.1.
D10464 mRNA. Translation: BAA01257.1.
AK002278 mRNA. Translation: BAB21982.1.
BC010754 mRNA. Translation: AAH10754.1.
BC027736 mRNA. Translation: AAH27736.1.
BC053697 mRNA. Translation: AAH53697.1.
CCDSiCCDS21202.1.
PIRiA25606.
RefSeqiNP_034769.4. NM_010639.7.
UniGeneiMm.142722.

Genome annotation databases

EnsembliENSMUST00000075162; ENSMUSP00000074659; ENSMUSG00000063903.
GeneIDi16612.
KEGGimmu:16612.
UCSCiuc009goo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13500 , M13498 , M13499 Genomic DNA. Translation: AAG11389.1 .
D10464 mRNA. Translation: BAA01257.1 .
AK002278 mRNA. Translation: BAB21982.1 .
BC010754 mRNA. Translation: AAH10754.1 .
BC027736 mRNA. Translation: AAH27736.1 .
BC053697 mRNA. Translation: AAH53697.1 .
CCDSi CCDS21202.1.
PIRi A25606.
RefSeqi NP_034769.4. NM_010639.7.
UniGenei Mm.142722.

3D structure databases

ProteinModelPortali P15947.
SMRi P15947. Positions 25-260.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000074659.

Protein family/group databases

MEROPSi S01.167.

Proteomic databases

MaxQBi P15947.
PaxDbi P15947.
PRIDEi P15947.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000075162 ; ENSMUSP00000074659 ; ENSMUSG00000063903 .
GeneIDi 16612.
KEGGi mmu:16612.
UCSCi uc009goo.1. mouse.

Organism-specific databases

CTDi 3816.
MGIi MGI:102850. Klk1.

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000118862.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi P15947.
KOi K01325.
OMAi FNTWIRE.
OrthoDBi EOG75B84T.
PhylomeDBi P15947.
TreeFami TF331065.

Enzyme and pathway databases

Reactomei REACT_199000. Activation of Matrix Metalloproteinases.
REACT_235886. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Miscellaneous databases

NextBioi 290197.
PROi P15947.
SOURCEi Search...

Gene expression databases

Bgeei P15947.
CleanExi MM_KLK1.
Genevestigatori P15947.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse glandular kallikrein genes. Identification, structure, and expression of the renal kallikrein gene."
    van Leeuwen B.H., Evans B.A., Tregear G.W., Richards R.I.
    J. Biol. Chem. 261:5529-5535(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Identification of a tissue kallikrein gene, mGK-6, expressed in a mouse neuroendocrine cell line."
    Tada M., Peters J., Takahashi S., Inoue H., Miyake Y.
    Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon, Kidney and Salivary gland.
  5. "mGK-6-derived true tissue kallikrein is synthesized, processed, and targeted through a regulated secretory pathway in mouse pituitary AtT-20 cells."
    Peters J., Takahashi S., Tada M., Miyake Y.
    J. Biochem. 111:643-648(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-44.
    Tissue: Submandibular gland.
  6. "A cytocidal tissue kallikrein isolated from mouse submandibular glands."
    Murakami K., Ikigai H., Nagumo N., Tomita M., Shimamura T.
    FEBS Lett. 257:400-402(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 165-174.
    Tissue: Submandibular gland.

Entry informationi

Entry nameiKLK1_MOUSE
AccessioniPrimary (citable) accession number: P15947
Secondary accession number(s): Q61855
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 5, 2001
Last modified: November 26, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3