KELL_HUMAN
ID KELL_HUMAN Reviewed; 732 AA.
AC P23276; B2RBV4; Q96RS8; Q99885;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Kell blood group glycoprotein;
DE EC=3.4.24.-;
DE AltName: CD_antigen=CD238;
GN Name=KEL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1712490; DOI=10.1073/pnas.88.14.6353;
RA Lee S., Zambas E.D., Marsh W.L., Redman C.M.;
RT "Molecular cloning and primary structure of Kell blood group protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6353-6357(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7858266;
RA Lee S., Zambas E., Green E.D., Redman C.M.;
RT "Organization of the gene encoding the human Kell blood group protein.";
RL Blood 85:1364-1370(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-163; MET-193; TRP-281;
RP PRO-597 AND ALA-726.
RG SeattleSNPs variation discovery resource;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-308.
RA Denomme G.A., Matheson K.A.;
RT "PCR amplification and sequencing of the human KEL gene.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 569-647, VARIANT BLOOD GROUP KEL6/KEL7
RP PRO-597, AND POLYMORPHISM.
RX PubMed=7570911; DOI=10.1046/j.1537-2995.1995.351096026362.x;
RA Lee S., Wu X., Reid M.E., Redman C.M.;
RT "Molecular basis of the K:6,-7 [Js(a+b-)] phenotype in the Kell blood group
RT system.";
RL Transfusion 35:822-825(1995).
RN [9]
RP INTERACTION WITH XK, DISULFIDE BOND, AND MUTAGENESIS OF CYS-72 AND CYS-319.
RX PubMed=9593744; DOI=10.1074/jbc.273.22.13950;
RA Russo D., Redman C., Lee S.;
RT "Association of XK and Kell blood group proteins.";
RL J. Biol. Chem. 273:13950-13956(1998).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF GLU-582.
RX PubMed=10438732;
RA Lee S., Lin M., Mele A., Cao Y., Farmar J., Russo D., Redman C.;
RT "Proteolytic processing of big endothelin-3 by the kell blood group
RT protein.";
RL Blood 94:1440-1450(1999).
RN [11]
RP TISSUE SPECIFICITY, AND INTERACTION WITH XK.
RX PubMed=10891471;
RA Russo D., Wu X., Redman C.M., Lee S.;
RT "Expression of Kell blood group protein in nonerythroid tissues.";
RL Blood 96:340-346(2000).
RN [12]
RP TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=11336649; DOI=10.1042/0264-6021:3560171;
RA Camara-Clayette V., Rahuel C., Lopez C., Hattab C., Verkarre V.,
RA Bertrand O., Cartron J.P.;
RT "Transcriptional regulation of the KEL gene and Kell protein expression in
RT erythroid and non-erythroid cells.";
RL Biochem. J. 356:171-180(2001).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP VARIANT BLOOD GROUP KEL1/KEL2 MET-193, AND POLYMORPHISM.
RX PubMed=7849312;
RA Lee S., Wu X., Reid M.E., Zelinski T., Redman C.M.;
RT "Molecular basis of the Kell (K1) phenotype.";
RL Blood 85:912-916(1995).
RN [15]
RP VARIANTS BLOOD GROUP KEL3/KEL4/KEL21; KEL11/17 AND KEL10, AND POLYMORPHISM.
RX PubMed=8669078; DOI=10.1046/j.1537-2995.1996.36696269505.x;
RA Lee S., Wu X., Son S., Naime D., Reid M.E., Okubo Y., Sistonen P.,
RA Redman C.M.;
RT "Point mutations characterize KEL10, the KEL3, KEL4, and KEL21 alleles, and
RT the KEL17 and KEL11 alleles.";
RL Transfusion 36:490-494(1996).
RN [16]
RP VARIANT BLOOD GROUP KEL14/KEL24 PRO-180, AND POLYMORPHISM.
RX PubMed=9354821; DOI=10.1046/j.1537-2995.1997.371098016441.x;
RA Lee S., Naime D., Reid M., Redman C.;
RT "The KEL24 and KEL14 alleles of the Kell blood group system.";
RL Transfusion 37:1035-1038(1997).
CC -!- FUNCTION: Zinc endopeptidase with endothelin-3-converting enzyme
CC activity. Cleaves EDN1, EDN2 and EDN3, with a marked preference for
CC EDN3. {ECO:0000269|PubMed:10438732}.
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:9593744}.
CC -!- INTERACTION:
CC P23276; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-746662, EBI-10827839;
CC P23276; P01031: C5; NbExp=3; IntAct=EBI-746662, EBI-8558308;
CC P23276; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-746662, EBI-12256978;
CC P23276; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-746662, EBI-11339910;
CC P23276; P17612: PRKACA; NbExp=3; IntAct=EBI-746662, EBI-476586;
CC P23276; P50454: SERPINH1; NbExp=3; IntAct=EBI-746662, EBI-350723;
CC P23276; P37173: TGFBR2; NbExp=3; IntAct=EBI-746662, EBI-296151;
CC P23276; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-746662, EBI-10243654;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein. Note=Spans the erythrocyte membrane, and is attached to the
CC underlying cytoskeleton.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in erythrocytes and testis
CC (in Sertoli cells), and, at lower levels, in skeletal muscle, tonsils
CC (in follicular dendritic cells), lymph node, spleen and appendix (at
CC protein level). Also expressed in many adult and fetal nonerythroid
CC tissues, including brain, spleen, lymph nodes and bone marrow.
CC {ECO:0000269|PubMed:10891471, ECO:0000269|PubMed:11336649}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11336649}.
CC -!- POLYMORPHISM: KEL is responsible for the Kell blood group system. The
CC molecular basis of the K=KEL1/k=KEL2 blood group antigens is a single
CC variation in position 193; Thr-193 corresponds to KEL2 and Met-193 to
CC KEL1 (PubMed:7849312). The molecular basis of the
CC Kpa=KEL3/Kpb=KEL4/Kpc=KEL21 blood group antigens is a single variation
CC in position 281; Arg-281 corresponds to KEL4, Trp-281 to KEL3 and Gln-
CC 281 to KEL21 (PubMed:8669078). The molecular basis of the
CC Jsa=KEL6/Jsb=KEL7 blood group antigens is a single variation in
CC position 597; Leu-597 corresponds to KEL7 and Pro-597 to KEL6
CC (PubMed:7570911). The molecular basis of the KEL11/KEL17 blood group
CC antigens is a single variation in position 302; Val-302 corresponds to
CC KEL11 and Ala-302 to KEL17 (PubMed:8669078). The molecular basis of the
CC KEL14/KEL24 blood group antigens is a single variation in position 180;
CC Arg-180 corresponds to KEL14 and Pro-180 to KEL24 (PubMed:9354821).
CC {ECO:0000269|PubMed:7570911, ECO:0000269|PubMed:7849312,
CC ECO:0000269|PubMed:8669078, ECO:0000269|PubMed:9354821}.
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=kell";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/kel/";
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DR EMBL; M64934; AAA03192.1; -; mRNA.
DR EMBL; AF172627; AAB33459.1; -; Genomic_DNA.
DR EMBL; AF172609; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172610; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172611; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172612; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172613; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172614; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172615; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172616; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172617; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172618; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172619; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172620; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172621; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172622; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172623; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172624; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172625; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AF172626; AAB33459.1; JOINED; Genomic_DNA.
DR EMBL; AY228336; AAO38053.1; -; Genomic_DNA.
DR EMBL; AK314831; BAG37351.1; -; mRNA.
DR EMBL; CH471198; EAW51891.1; -; Genomic_DNA.
DR EMBL; BC003135; AAH03135.1; -; mRNA.
DR EMBL; BC050639; AAH50639.1; -; mRNA.
DR EMBL; AF279657; AAK69488.1; -; Genomic_DNA.
DR EMBL; S80081; AAB47018.1; -; Genomic_DNA.
DR CCDS; CCDS34766.1; -.
DR RefSeq; NP_000411.1; NM_000420.2.
DR AlphaFoldDB; P23276; -.
DR SMR; P23276; -.
DR BioGRID; 109993; 41.
DR IntAct; P23276; 12.
DR MINT; P23276; -.
DR STRING; 9606.ENSP00000347409; -.
DR DrugBank; DB02557; Phosphoramidon.
DR MEROPS; M13.090; -.
DR GlyGen; P23276; 5 sites.
DR iPTMnet; P23276; -.
DR PhosphoSitePlus; P23276; -.
DR BioMuta; KEL; -.
DR DMDM; 1346376; -.
DR EPD; P23276; -.
DR jPOST; P23276; -.
DR MassIVE; P23276; -.
DR MaxQB; P23276; -.
DR PaxDb; P23276; -.
DR PeptideAtlas; P23276; -.
DR PRIDE; P23276; -.
DR ProteomicsDB; 54076; -.
DR ABCD; P23276; 3 sequenced antibodies.
DR Antibodypedia; 18443; 357 antibodies from 27 providers.
DR DNASU; 3792; -.
DR Ensembl; ENST00000355265.7; ENSP00000347409.2; ENSG00000197993.9.
DR Ensembl; ENST00000615381.2; ENSP00000477793.1; ENSG00000276615.2.
DR GeneID; 3792; -.
DR KEGG; hsa:3792; -.
DR MANE-Select; ENST00000355265.7; ENSP00000347409.2; NM_000420.3; NP_000411.1.
DR UCSC; uc003wcb.4; human.
DR CTD; 3792; -.
DR DisGeNET; 3792; -.
DR GeneCards; KEL; -.
DR HGNC; HGNC:6308; KEL.
DR HPA; ENSG00000197993; Group enriched (bone marrow, testis).
DR MalaCards; KEL; -.
DR MIM; 110900; phenotype.
DR MIM; 613883; gene.
DR neXtProt; NX_P23276; -.
DR OpenTargets; ENSG00000197993; -.
DR PharmGKB; PA30087; -.
DR VEuPathDB; HostDB:ENSG00000197993; -.
DR eggNOG; KOG3624; Eukaryota.
DR GeneTree; ENSGT00940000161830; -.
DR HOGENOM; CLU_006187_8_2_1; -.
DR InParanoid; P23276; -.
DR OMA; QESYDTH; -.
DR OrthoDB; 282463at2759; -.
DR PhylomeDB; P23276; -.
DR TreeFam; TF315192; -.
DR PathwayCommons; P23276; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR SignaLink; P23276; -.
DR SIGNOR; P23276; -.
DR BioGRID-ORCS; 3792; 12 hits in 1072 CRISPR screens.
DR GenomeRNAi; 3792; -.
DR Pharos; P23276; Tbio.
DR PRO; PR:P23276; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P23276; protein.
DR Bgee; ENSG00000197993; Expressed in right testis and 94 other tissues.
DR ExpressionAtlas; P23276; baseline and differential.
DR Genevisible; P23276; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; TAS:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:HGNC-UCL.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0010961; P:cellular magnesium ion homeostasis; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0031133; P:regulation of axon diameter; IEA:Ensembl.
DR GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR GO; GO:0042310; P:vasoconstriction; TAS:HGNC-UCL.
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 Blood group antigen; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Phosphoprotein; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..732
FT /note="Kell blood group glycoprotein"
FT /id="PRO_0000078227"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..67
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..732
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 76..732
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 582
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT ACT_SITE 638
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 581
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 585
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 634
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine; in KEL2 antigen"
FT /evidence="ECO:0000269|PubMed:11336649"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72
FT /note="Interchain (with C-347 in XK)"
FT /evidence="ECO:0000269|PubMed:9593744"
FT DISULFID 77..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 100..717
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 108..682
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 155..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 610..729
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT VARIANT 163
FT /note="A -> T (in dbSNP:rs8175974)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_016265"
FT VARIANT 180
FT /note="R -> P (in KEL24 antigen; dbSNP:rs61729039)"
FT /evidence="ECO:0000269|PubMed:9354821"
FT /id="VAR_006731"
FT VARIANT 193
FT /note="T -> M (in KEL1/K antigen; dbSNP:rs8176058)"
FT /evidence="ECO:0000269|PubMed:7849312, ECO:0000269|Ref.3"
FT /id="VAR_006732"
FT VARIANT 248
FT /note="R -> Q (in KEL25 antigen; dbSNP:rs61729040)"
FT /id="VAR_015120"
FT VARIANT 249
FT /note="E -> K (in KEL27 antigen; dbSNP:rs61729042)"
FT /id="VAR_015121"
FT VARIANT 281
FT /note="R -> Q (in KEL21/Kp(c) antigen; dbSNP:rs61729036)"
FT /evidence="ECO:0000269|PubMed:8669078"
FT /id="VAR_006734"
FT VARIANT 281
FT /note="R -> W (in KEL3/Kp(a) antigen; dbSNP:rs8176059)"
FT /evidence="ECO:0000269|PubMed:8669078, ECO:0000269|Ref.3"
FT /id="VAR_006733"
FT VARIANT 302
FT /note="V -> A (in KEL17 antigen; dbSNP:rs61729034)"
FT /evidence="ECO:0000269|PubMed:8669078"
FT /id="VAR_006735"
FT VARIANT 322
FT /note="A -> V (in KEL22 antigen; dbSNP:rs61729037)"
FT /id="VAR_015122"
FT VARIANT 382
FT /note="Q -> R (in KEL23 antigen; dbSNP:rs61729038)"
FT /id="VAR_015123"
FT VARIANT 406
FT /note="R -> Q (in KEL26 antigen; dbSNP:rs61729041)"
FT /id="VAR_015124"
FT VARIANT 492
FT /note="R -> Q (in KEL19 antigen; dbSNP:rs61729035)"
FT /id="VAR_015125"
FT VARIANT 494
FT /note="E -> V (in KEL10/Ul(a) antigen; dbSNP:rs61729032)"
FT /evidence="ECO:0000269|PubMed:8669078"
FT /id="VAR_006736"
FT VARIANT 548
FT /note="H -> R (in KEL12 antigen; dbSNP:rs61729033)"
FT /id="VAR_015126"
FT VARIANT 597
FT /note="L -> P (in KEL6/Js(a) antigen; dbSNP:rs8176038)"
FT /evidence="ECO:0000269|PubMed:7570911, ECO:0000269|Ref.3"
FT /id="VAR_006737"
FT VARIANT 726
FT /note="S -> A (in dbSNP:rs8176048)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_016266"
FT MUTAGEN 72
FT /note="C->S: Loss of Kell-XK complex."
FT /evidence="ECO:0000269|PubMed:9593744"
FT MUTAGEN 319
FT /note="C->S: No loss of Kell-XK complex."
FT /evidence="ECO:0000269|PubMed:9593744"
FT MUTAGEN 582
FT /note="E->G: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:10438732"
SQ SEQUENCE 732 AA; 82824 MW; 604A168AD300EDB4 CRC64;
MEGGDQSEEE PRERSQAGGM GTLWSQESTP EERLPVEGSR PWAVARRVLT AILILGLLLC
FSVLLFYNFQ NCGPRPCETS VCLDLRDHYL ASGNTSVAPC TDFFSFACGR AKETNNSFQE
LATKNKNRLR RILEVQNSWH PGSGEEKAFQ FYNSCMDTLA IEAAGTGPLR QVIEELGGWR
ISGKWTSLNF NRTLRLLMSQ YGHFPFFRAY LGPHPASPHT PVIQIDQPEF DVPLKQDQEQ
KIYAQIFREY LTYLNQLGTL LGGDPSKVQE HSSLSISITS RLFQFLRPLE QRRAQGKLFQ
MVTIDQLKEM APAIDWLSCL QATFTPMSLS PSQSLVVHDV EYLKNMSQLV EEMLLKQRDF
LQSHMILGLV VTLSPALDSQ FQEARRKLSQ KLRELTEQPP MPARPRWMKC VEETGTFFEP
TLAALFVREA FGPSTRSAAM KLFTAIRDAL ITRLRNLPWM NEETQNMAQD KVAQLQVEMG
ASEWALKPEL ARQEYNDIQL GSSFLQSVLS CVRSLRARIV QSFLQPHPQH RWKVSPWDVN
AYYSVSDHVV VFPAGLLQPP FFHPGYPRAV NFGAAGSIMA HELLHIFYQL LLPGGCLACD
NHALQEAHLC LKRHYAAFPL PSRTSFNDSL TFLENAADVG GLAIALQAYS KRLLRHHGET
VLPSLDLSPQ QIFFRSYAQV MCRKPSPQDS HDTHSPPHLR VHGPLSSTPA FARYFRCARG
ALLNPSSRCQ LW
