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Protein

Kell blood group glycoprotein homolog

Gene

Kel

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

Functioni

Zinc endopeptidase with endothelin-3-converting enzyme activity. Cleaves EDN1, EDN2 and EDN3 (By similarity).By similarity1 Publication

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi562 – 5621Zinc; catalyticPROSITE-ProRule annotation
Active sitei563 – 5631PROSITE-ProRule annotation
Metal bindingi566 – 5661Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi615 – 6151Zinc; catalyticPROSITE-ProRule annotation
Active sitei619 – 6191Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  • endopeptidase activity Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: HGNC
  • metallopeptidase activity Source: MGI

GO - Biological processi

  • cellular calcium ion homeostasis Source: MGI
  • cellular magnesium ion homeostasis Source: MGI
  • myelination Source: MGI
  • negative regulation of potassium ion transmembrane transport Source: MGI
  • regulation of axon diameter Source: MGI
  • regulation of cell size Source: MGI
  • skeletal muscle fiber development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-375276. Peptide ligand-binding receptors.

Protein family/group databases

MEROPSiM13.090.

Names & Taxonomyi

Protein namesi
Recommended name:
Kell blood group glycoprotein homolog (EC:3.4.24.-)
Alternative name(s):
CD_antigen: CD238
Gene namesi
Name:Kel
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1346053. Kel.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2828CytoplasmicSequence analysisAdd
BLAST
Transmembranei29 – 4820Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini49 – 713665ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 713713Kell blood group glycoprotein homologPRO_0000319886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 – 53Interchain (with C-347 in XK)By similarity
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence analysis
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence analysis
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence analysis
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence analysis
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence analysis
Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence analysis
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence analysis
Glycosylationi608 – 6081N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9EQF2.
PaxDbiQ9EQF2.
PRIDEiQ9EQF2.

PTM databases

PhosphoSiteiQ9EQF2.

Expressioni

Tissue specificityi

Highly expressed in spleen. Weaker expression in testis and heart.1 Publication

Gene expression databases

BgeeiQ9EQF2.
CleanExiMM_KEL.
ExpressionAtlasiQ9EQF2. baseline and differential.
GenevisibleiQ9EQF2. MM.

Interactioni

Subunit structurei

Heterodimer with XK; disulfide-linked.1 Publication

Protein-protein interaction databases

IntActiQ9EQF2. 1 interaction.
STRINGi10090.ENSMUSP00000031899.

Structurei

3D structure databases

ProteinModelPortaliQ9EQF2.
SMRiQ9EQF2. Positions 60-713.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M13 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3624. Eukaryota.
COG3590. LUCA.
GeneTreeiENSGT00760000119162.
HOGENOMiHOG000245574.
HOVERGENiHBG002194.
InParanoidiQ9EQF2.
KOiK06577.
OMAiHYAAFPL.
OrthoDBiEOG7QRQT9.
PhylomeDBiQ9EQF2.
TreeFamiTF315192.

Family and domain databases

InterProiIPR029737. KEL.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]
PANTHERiPTHR11733. PTHR11733. 1 hit.
PTHR11733:SF128. PTHR11733:SF128. 1 hit.
PfamiPF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]
PRINTSiPR00786. NEPRILYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EQF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPPWSQESS PEERLPTEWS RQLTRARWVL LAVLLCGLLL GSSMLWFYIF
60 70 80 90 100
RNCGPCPCET PVCMELLDHY LASGNRSVAP CTDFFSFACE KANGTSDSFQ
110 120 130 140 150
ALTEENKSRL WRLLEAPGSW HLGSGEEKAF QFYNSCMDTD AIEASGSGPL
160 170 180 190 200
IQIIEELGGW NITGNWTSLD FNQNLRLLMS QYGHFPFFRA YLRPHPAPPH
210 220 230 240 250
TPIIQIDQPE FDILLQQEQE QKVYAQILRE YVTYLNRLGT LLGSNPQEAQ
260 270 280 290 300
QHASWSIVFT SRLFQFLRPQ QQQQAQDKLF HVVTIDELQE MAPAIDWLSC
310 320 330 340 350
LQAIFTPMSL NSSQTLVVHD LDYLRNMSQL VEEGLLNHRE SIQSYMILGL
360 370 380 390 400
VDTLSPALDT KFQEARRELI QELRKLKERP PLPAYPRWMK CVEQTGAFFE
410 420 430 440 450
PTLAALFVRE AFGPSIQSAA MELFAEIKDA VIIRLKKLSW ISEETQKEAL
460 470 480 490 500
NKLAQLQVEM GAPKRAVKPD IATQEYNDIQ LGPSFLQSFL SCVRSLRARN
510 520 530 540 550
VQSFLQPFPY HRWQKSPWEV NAYYSISDHM VVFPAGLLQP PFFHPGYPRA
560 570 580 590 600
VNFGAAGSIM AHELLHIFYQ LLLPGGCPAC DTHVLQEALL CLERHYAAFP
610 620 630 640 650
LPSISSFNGS HTLLENAADI GGVAIAFQAY SKRIVEHTGE LTLPNLDLSP
660 670 680 690 700
YQLFFRSYAQ VMCRGLSSQD PQDPHSPPSL RVHGPLSNTP DFAKHFHCPR
710
GTLLNPSARC KLW
Length:713
Mass (Da):80,866
Last modified:March 1, 2001 - v1
Checksum:i5A1F32009F55DFE1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti268 – 2681R → G in AAH99961 (PubMed:15489334).Curated
Sequence conflicti377 – 3771K → Q in AAH99961 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF252870 mRNA. Translation: AAG48572.1.
AF336378 Genomic DNA. Translation: AAM53407.1.
AK028430 mRNA. Translation: BAC25947.1.
BC099961 mRNA. Translation: AAH99961.1.
CCDSiCCDS20055.1.
RefSeqiNP_115929.3. NM_032540.3.
XP_006506120.1. XM_006506057.2.
UniGeneiMm.19958.

Genome annotation databases

EnsembliENSMUST00000031899; ENSMUSP00000031899; ENSMUSG00000029866.
GeneIDi23925.
KEGGimmu:23925.
UCSCiuc009bqf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF252870 mRNA. Translation: AAG48572.1.
AF336378 Genomic DNA. Translation: AAM53407.1.
AK028430 mRNA. Translation: BAC25947.1.
BC099961 mRNA. Translation: AAH99961.1.
CCDSiCCDS20055.1.
RefSeqiNP_115929.3. NM_032540.3.
XP_006506120.1. XM_006506057.2.
UniGeneiMm.19958.

3D structure databases

ProteinModelPortaliQ9EQF2.
SMRiQ9EQF2. Positions 60-713.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9EQF2. 1 interaction.
STRINGi10090.ENSMUSP00000031899.

Protein family/group databases

MEROPSiM13.090.

PTM databases

PhosphoSiteiQ9EQF2.

Proteomic databases

MaxQBiQ9EQF2.
PaxDbiQ9EQF2.
PRIDEiQ9EQF2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031899; ENSMUSP00000031899; ENSMUSG00000029866.
GeneIDi23925.
KEGGimmu:23925.
UCSCiuc009bqf.2. mouse.

Organism-specific databases

CTDi3792.
MGIiMGI:1346053. Kel.

Phylogenomic databases

eggNOGiKOG3624. Eukaryota.
COG3590. LUCA.
GeneTreeiENSGT00760000119162.
HOGENOMiHOG000245574.
HOVERGENiHBG002194.
InParanoidiQ9EQF2.
KOiK06577.
OMAiHYAAFPL.
OrthoDBiEOG7QRQT9.
PhylomeDBiQ9EQF2.
TreeFamiTF315192.

Enzyme and pathway databases

ReactomeiR-MMU-375276. Peptide ligand-binding receptors.

Miscellaneous databases

PROiQ9EQF2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQF2.
CleanExiMM_KEL.
ExpressionAtlasiQ9EQF2. baseline and differential.
GenevisibleiQ9EQF2. MM.

Family and domain databases

InterProiIPR029737. KEL.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]
PANTHERiPTHR11733. PTHR11733. 1 hit.
PTHR11733:SF128. PTHR11733:SF128. 1 hit.
PfamiPF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]
PRINTSiPR00786. NEPRILYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The mouse Kell blood group gene (Kel): cDNA sequence, genomic organization, expression, and enzymatic function."
    Lee S., Russo D.C., Pu J., Ho M., Redman C.M.
    Immunogenetics 52:53-62(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, GLYCOSYLATION, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Spleen.
  2. "Characterization of two epithelial calcium channel genes in mice."
    Weber K., Zeitz U., Rump A., Erben R., Adamski J.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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: Liver.
  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: C57BL/6J.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung and Spleen.

Entry informationi

Entry nameiKELL_MOUSE
AccessioniPrimary (citable) accession number: Q9EQF2
Secondary accession number(s): Q499D7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.