KELL_MOUSE
ID KELL_MOUSE Reviewed; 713 AA.
AC Q9EQF2; Q499D7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Kell blood group glycoprotein homolog;
DE EC=3.4.24.-;
DE AltName: CD_antigen=CD238;
GN Name=Kel;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=11132157; DOI=10.1007/s002510000251;
RA Lee S., Russo D.C., Pu J., Ho M., Redman C.M.;
RT "The mouse Kell blood group gene (Kel): cDNA sequence, genomic
RT organization, expression, and enzymatic function.";
RL Immunogenetics 52:53-62(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Weber K., Zeitz U., Rump A., Erben R., Adamski J.;
RT "Characterization of two epithelial calcium channel genes in mice.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Zinc endopeptidase with endothelin-3-converting enzyme
CC activity. Cleaves EDN1, EDN2 and EDN3 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11132157}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer with XK; disulfide-linked.
CC {ECO:0000269|PubMed:11132157}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}. Note=Spans the erythrocyte membrane,
CC and is attached to the underlying cytoskeleton. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen. Weaker expression in
CC testis and heart. {ECO:0000269|PubMed:11132157}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11132157}.
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
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DR EMBL; AF252870; AAG48572.1; -; mRNA.
DR EMBL; AF336378; AAM53407.1; -; Genomic_DNA.
DR EMBL; AK028430; BAC25947.1; -; mRNA.
DR EMBL; BC099961; AAH99961.1; -; mRNA.
DR CCDS; CCDS20055.1; -.
DR RefSeq; NP_115929.3; NM_032540.3.
DR RefSeq; XP_006506120.1; XM_006506057.3.
DR AlphaFoldDB; Q9EQF2; -.
DR SMR; Q9EQF2; -.
DR STRING; 10090.ENSMUSP00000031899; -.
DR MEROPS; M13.090; -.
DR GlyGen; Q9EQF2; 8 sites.
DR PhosphoSitePlus; Q9EQF2; -.
DR MaxQB; Q9EQF2; -.
DR PaxDb; Q9EQF2; -.
DR PRIDE; Q9EQF2; -.
DR ProteomicsDB; 263430; -.
DR ABCD; Q9EQF2; 1 sequenced antibody.
DR Antibodypedia; 18443; 357 antibodies from 27 providers.
DR DNASU; 23925; -.
DR Ensembl; ENSMUST00000031899; ENSMUSP00000031899; ENSMUSG00000029866.
DR GeneID; 23925; -.
DR KEGG; mmu:23925; -.
DR UCSC; uc009bqf.2; mouse.
DR CTD; 3792; -.
DR MGI; MGI:1346053; Kel.
DR VEuPathDB; HostDB:ENSMUSG00000029866; -.
DR eggNOG; KOG3624; Eukaryota.
DR GeneTree; ENSGT00940000161830; -.
DR HOGENOM; CLU_006187_8_2_1; -.
DR InParanoid; Q9EQF2; -.
DR OMA; QESYDTH; -.
DR OrthoDB; 282463at2759; -.
DR PhylomeDB; Q9EQF2; -.
DR TreeFam; TF315192; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR BioGRID-ORCS; 23925; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q9EQF2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9EQF2; protein.
DR Bgee; ENSMUSG00000029866; Expressed in fetal liver hematopoietic progenitor cell and 68 other tissues.
DR ExpressionAtlas; Q9EQF2; baseline and differential.
DR Genevisible; Q9EQF2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISS:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:HGNC-UCL.
DR GO; GO:0008237; F:metallopeptidase activity; IMP:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IGI:MGI.
DR GO; GO:0010961; P:cellular magnesium ion homeostasis; IGI:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IGI:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IGI:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IGI:MGI.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0031133; P:regulation of axon diameter; IGI:MGI.
DR GO; GO:0008361; P:regulation of cell size; IGI:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IGI:MGI.
DR CDD; cd08662; M13; 1.
DR Gene3D; 1.10.1380.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR029737; KEL.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR000718; Peptidase_M13.
DR InterPro; IPR018497; Peptidase_M13_C.
DR InterPro; IPR042089; Peptidase_M13_dom_2.
DR InterPro; IPR008753; Peptidase_M13_N.
DR PANTHER; PTHR11733; PTHR11733; 1.
DR PANTHER; PTHR11733:SF128; PTHR11733:SF128; 1.
DR Pfam; PF01431; Peptidase_M13; 1.
DR Pfam; PF05649; Peptidase_M13_N; 1.
DR PRINTS; PR00786; NEPRILYSIN.
DR PROSITE; PS51885; NEPRILYSIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..713
FT /note="Kell blood group glycoprotein homolog"
FT /id="PRO_0000319886"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..48
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..713
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 57..713
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT ACT_SITE 563
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 619
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 566
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 615
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53
FT /note="Interchain (with C-347 in XK)"
FT /evidence="ECO:0000250"
FT DISULFID 58..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 81..698
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 89..663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 136..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 591..710
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT CONFLICT 268
FT /note="R -> G (in Ref. 4; AAH99961)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="K -> Q (in Ref. 4; AAH99961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 713 AA; 80866 MW; 5A1F32009F55DFE1 CRC64;
MGPPWSQESS PEERLPTEWS RQLTRARWVL LAVLLCGLLL GSSMLWFYIF RNCGPCPCET
PVCMELLDHY LASGNRSVAP CTDFFSFACE KANGTSDSFQ ALTEENKSRL WRLLEAPGSW
HLGSGEEKAF QFYNSCMDTD AIEASGSGPL IQIIEELGGW NITGNWTSLD FNQNLRLLMS
QYGHFPFFRA YLRPHPAPPH TPIIQIDQPE FDILLQQEQE QKVYAQILRE YVTYLNRLGT
LLGSNPQEAQ QHASWSIVFT SRLFQFLRPQ QQQQAQDKLF HVVTIDELQE MAPAIDWLSC
LQAIFTPMSL NSSQTLVVHD LDYLRNMSQL VEEGLLNHRE SIQSYMILGL VDTLSPALDT
KFQEARRELI QELRKLKERP PLPAYPRWMK CVEQTGAFFE PTLAALFVRE AFGPSIQSAA
MELFAEIKDA VIIRLKKLSW ISEETQKEAL NKLAQLQVEM GAPKRAVKPD IATQEYNDIQ
LGPSFLQSFL SCVRSLRARN VQSFLQPFPY HRWQKSPWEV NAYYSISDHM VVFPAGLLQP
PFFHPGYPRA VNFGAAGSIM AHELLHIFYQ LLLPGGCPAC DTHVLQEALL CLERHYAAFP
LPSISSFNGS HTLLENAADI GGVAIAFQAY SKRIVEHTGE LTLPNLDLSP YQLFFRSYAQ
VMCRGLSSQD PQDPHSPPSL RVHGPLSNTP DFAKHFHCPR GTLLNPSARC KLW
