[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. DOI=10.1073/pnas.88.14.6353; PubMed=1712490 [NCBI, ExPASy, EBI, Israel, Japan] Lee S., Zambas E.D., Marsh W.L., Redman C.M.; "Molecular cloning and primary structure of Kell blood group protein."; Proc. Natl. Acad. Sci. U.S.A. 88:6353-6357(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=7858266 [NCBI, ExPASy, EBI, Israel, Japan] Lee S., Zambas E., Green E.D., Redman C.M.; "Organization of the gene encoding the human Kell blood group protein."; Blood 85:1364-1370(1995).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-163; MET-193; TRP-281; PRO-597 AND ALA-726. SeattleSNPs variation discovery resource; Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain, and Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-308. Denomme G.A., Matheson K.A.; "PCR amplification and sequencing of the human KEL gene."; Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 569-647, AND VARIANT BLOOD GROUP KEL6/KEL7. DOI=10.1046/j.1537-2995.1995.351096026362.x; PubMed=7570911 [NCBI, ExPASy, EBI, Israel, Japan] Lee S., Wu X., Reid M.E., Redman C.M.; "Molecular basis of the K:6,-7 [Js(a+b-)] phenotype in the Kell blood group system."; Transfusion 35:822-825(1995).
[7]	SUBUNIT, DISULFIDE BOND, AND MUTAGENESIS OF CYS-72 AND CYS-319. DOI=10.1074/jbc.273.22.13950; PubMed=9593744 [NCBI, ExPASy, EBI, Israel, Japan] Russo D., Redman C., Lee S.; "Association of XK and Kell blood group proteins."; J. Biol. Chem. 273:13950-13956(1998).
[8]	VARIANT BLOOD GROUP KEL1/KEL2 MET-193. PubMed=7849312 [NCBI, ExPASy, EBI, Israel, Japan] Lee S., Wu X., Reid M.E., Zelinski T., Redman C.M.; "Molecular basis of the Kell (K1) phenotype."; Blood 85:912-916(1995).
[9]	VARIANTS BLOOD GROUP KEL3/KEL4/KEL21; KEL11/17 AND KEL10. DOI=10.1046/j.1537-2995.1996.36696269505.x; PubMed=8669078 [NCBI, ExPASy, EBI, Israel, Japan] Lee S., Wu X., Son S., Naime D., Reid M.E., Okubo Y., Sistonen P., Redman C.M.; "Point mutations characterize KEL10, the KEL3, KEL4, and KEL21 alleles, and the KEL17 and KEL11 alleles."; Transfusion 36:490-494(1996).

Comments

FUNCTION: Zinc endopeptidase with endothelin-3-converting enzyme activity.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
SUBUNIT: Heterodimer with XK; disulfide-linked.
SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Note=Spans the erythrocyte membrane, and is attached to the underlying cytoskeleton.
POLYMORPHISM: KEL is responsible for the Kell blood group system. The molecular basis of the K=KEL1/k=KEL2 blood group antigens is a single variation in position 193; Thr-193 corresponds to KEL2 and Met-193 to KEL1. The molecular basis of the Kpa=KEL3/Kpb=KEL4/Kpc=KEL21 blood group antigens is a single variation in position 281; Arg-281 corresponds to KEL4, Trp-281 to KEL3 and Gln-281 to KEL21. The molecular basis of the Jsa=KEL6/Jsb=KEL7 blood group antigens is a single variation in position 597; Leu-597 corresponds to KEL7 and Pro-597 to KEL6. The molecular basis of the KEL11/KEL17 blood group antigens is a single variation in position 302; Val-302 corresponds to KEL11 and Ala-302 to KEL17. The molecular basis of the KEL14/KEL24 blood group antigens is a single variation in position 180; Arg-180 corresponds to KEL14 and Pro-180 to KEL24.
SIMILARITY: Belongs to the peptidase M13 family [view classification].
WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation database; URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=kell";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=KEL";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/kel/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M64934; AAA03192.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172627; AAB33459.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172609; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172610; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172611; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172612; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172613; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172614; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172615; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172616; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172617; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172618; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172619; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172620; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172621; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172622; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172623; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172624; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172625; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172626; AAB33459.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY228336; AAO38053.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003135; AAH03135.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050639; AAH50639.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF279657; AAK69488.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S80081; AAB47018.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00220459; -.

NP_000411.1; -.

3D structure databases

ModBase

P23276.

Protein-protein interaction databases

IntAct

P23276; 1.

Protein family/group databases

MEROPS

M13.090; -.

Organism-specific databases

GC07M142348; -.

HIX0007164; -.

HGNC:6308; KEL.

KEL.

110900; gene+phenotype. [NCBI / EBI]

PharmGKB

PA30087; -.

Gene expression databases

ArrayExpress

P23276; -.

Bgee

P23276; -.

CleanEx

HS_KEL; -.

Ontologies

GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0016511;	Molecular function: endothelin-converting enzyme activity (inferred from direct assay from HGNC).
GO:0004222;	Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from HGNC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006487;	Biological process: protein amino acid N-linked glycosylation (traceable author statement from ProtInc).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
GO:0042310;	Biological process: vasoconstriction (traceable author statement from HGNC).
QuickGo view.

Family and domain databases

InterPro

IPR006025; Pept_M_Zn_BS.
IPR000718; Peptidase_M13.
IPR018497; Peptidase_M13_C.
IPR008753; Peptidase_M13_N.
Graphical view of domain structure.

PANTHER

PTHR11733; Peptidase_M13; 1.

Pfam

PF01431; Peptidase_M13; 1.
PF05649; Peptidase_M13_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00786; NEPRILYSIN.

PROSITE

PS00142; ZINC_PROTEASE; 1.

Proteomic databases

PRIDE

P23276; -.

Genome annotation databases

Ensembl

ENSG00000197993; Homo sapiens. [Contig view]

GeneID

3792; -.

KEGG

hsa:3792; -.

Phylogenomic databases

HOGENOM

P23276; -.

HOVERGEN

P23276; -.

OMA

P23276; RDFLQSH.

Other

14891; -.

KEL; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Blood group antigen; Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; Polymorphism; Protease; Signal-anchor; Transmembrane; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 732`	`732`	`Kell blood group glycoprotein.`	`PRO_0000078227`
`TOPO_DOM`	`1 47`	`47`	`Cytoplasmic (Potential).`
`TRANSMEM`	`48 67`	`20`	`Signal-anchor for type II membrane protein (Potential).`
`TOPO_DOM`	`68 732`	`665`	`Extracellular (Potential).`
`ACT_SITE`	`582 582`		`By similarity.`
`ACT_SITE`	`638 638`		`Proton donor (By similarity).`
`METAL`	`581 581`		`Zinc; catalytic (By similarity).`
`METAL`	`585 585`		`Zinc; catalytic (By similarity).`
`METAL`	`634 634`		`Zinc; catalytic (By similarity).`
`CARBOHYD`	`94 94`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`115 115`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`191 191`		`N-linked (GlcNAc...); in KEL2 antigen.`
`CARBOHYD`	`345 345`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`627 627`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`72 72`		`Interchain (with C-347 in XK).`
`VARIANT`	`163 163`	`1`	`A -> T (in dbSNP:rs8175974 [NCBI]).`	`VAR_016265`
`VARIANT`	`180 180`	`1`	`R -> P (in KEL24 antigen).`	`VAR_006731`
`VARIANT`	`193 193`	`1`	`T -> M (in KEL1/K antigen; dbSNP:rs8176058 [NCBI]).`	`VAR_006732`
`VARIANT`	`248 248`	`1`	`R -> Q (in KEL25 antigen).`	`VAR_015120`
`VARIANT`	`249 249`	`1`	`E -> K (in KEL27 antigen).`	`VAR_015121`
`VARIANT`	`281 281`	`1`	`R -> Q (in KEL21/Kp(c) antigen).`	`VAR_006734`
`VARIANT`	`281 281`	`1`	`R -> W (in KEL3/Kp(a) antigen; dbSNP:rs8176059 [NCBI]).`	`VAR_006733`
`VARIANT`	`302 302`	`1`	`V -> A (in KEL17 antigen).`	`VAR_006735`
`VARIANT`	`322 322`	`1`	`A -> V (in KEL22 antigen).`	`VAR_015122`
`VARIANT`	`382 382`	`1`	`Q -> R (in KEL23 antigen).`	`VAR_015123`
`VARIANT`	`406 406`	`1`	`R -> Q (in KEL26 antigen).`	`VAR_015124`
`VARIANT`	`492 492`	`1`	`R -> Q (in KEL19 antigen).`	`VAR_015125`
`VARIANT`	`494 494`	`1`	`E -> V (in KEL10/Ul(a) antigen).`	`VAR_006736`
`VARIANT`	`548 548`	`1`	`H -> R (in KEL12 antigen).`	`VAR_015126`
`VARIANT`	`597 597`	`1`	`L -> P (in KEL6/Js(a) antigen; dbSNP:rs8176038 [NCBI]).`	`VAR_006737`
`VARIANT`	`726 726`	`1`	`S -> A (in dbSNP:rs8176048 [NCBI]).`	`VAR_016266`
`MUTAGEN`	`72 72`		`C->S: Loss of Kell-XK complex.`
`MUTAGEN`	`319 319`		`C->S: No loss of Kell-XK complex.`

Sequence information

Length: 732 AA [This is the length of the unprocessed precursor]

Molecular weight: 82824 Da [This is the MW of the unprocessed precursor]

CRC64: 604A168AD300EDB4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEGGDQSEEE PRERSQAGGM GTLWSQESTP EERLPVEGSR PWAVARRVLT AILILGLLLC 

        70         80         90        100        110        120 
FSVLLFYNFQ NCGPRPCETS VCLDLRDHYL ASGNTSVAPC TDFFSFACGR AKETNNSFQE 

       130        140        150        160        170        180 
LATKNKNRLR RILEVQNSWH PGSGEEKAFQ FYNSCMDTLA IEAAGTGPLR QVIEELGGWR 

       190        200        210        220        230        240 
ISGKWTSLNF NRTLRLLMSQ YGHFPFFRAY LGPHPASPHT PVIQIDQPEF DVPLKQDQEQ 

       250        260        270        280        290        300 
KIYAQIFREY LTYLNQLGTL LGGDPSKVQE HSSLSISITS RLFQFLRPLE QRRAQGKLFQ 

       310        320        330        340        350        360 
MVTIDQLKEM APAIDWLSCL QATFTPMSLS PSQSLVVHDV EYLKNMSQLV EEMLLKQRDF 

       370        380        390        400        410        420 
LQSHMILGLV VTLSPALDSQ FQEARRKLSQ KLRELTEQPP MPARPRWMKC VEETGTFFEP 

       430        440        450        460        470        480 
TLAALFVREA FGPSTRSAAM KLFTAIRDAL ITRLRNLPWM NEETQNMAQD KVAQLQVEMG 

       490        500        510        520        530        540 
ASEWALKPEL ARQEYNDIQL GSSFLQSVLS CVRSLRARIV QSFLQPHPQH RWKVSPWDVN 

       550        560        570        580        590        600 
AYYSVSDHVV VFPAGLLQPP FFHPGYPRAV NFGAAGSIMA HELLHIFYQL LLPGGCLACD 

       610        620        630        640        650        660 
NHALQEAHLC LKRHYAAFPL PSRTSFNDSL TFLENAADVG GLAIALQAYS KRLLRHHGET 

       670        680        690        700        710        720 
VLPSLDLSPQ QIFFRSYAQV MCRKPSPQDS HDTHSPPHLR VHGPLSSTPA FARYFRCARG 

       730 
ALLNPSSRCQ LW

P23276 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools