(data stored in ACNUC16324 zone)

HOGENOM: HS7_PE4225

ID   HS7_PE4225                           STANDARD;      PRT;   732 AA.
AC   HS7_PE4225; P23276; B2RBV4; Q96RS8; Q99885;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Kell blood group glycoprotein; EC=3.4.24 -;AltName:
DE   CD_antigen=CD238; (HS7.PE4225).
GN   Name=KEL;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS7.PE4225.
CC       Homo sapiens chromosome 7 GRCh37  sequence 1..159128663 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:KELL_HUMAN
CC   -!- FUNCTION: Zinc endopeptidase with endothelin-3-converting enzyme
CC       activity. Cleaves EDN1, EDN2 and EDN3, with a marked preference
CC       for EDN3.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Heterodimer with XK; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC       protein. Note=Spans the erythrocyte membrane, and is attached to
CC       the underlying cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in erythrocytes and
CC       testis (in Sertoli cells), and, at lower levels, in skeletal
CC       muscle, tonsils (in follicular dendritic cells), lymph node,
CC       spleen and appendix (at protein level). Also expressed in many
CC       adult and fetal nonerythroid tissues, including brain, spleen,
CC       lymph nodes and bone marrow.
CC   -!- PTM: N-glycosylated.
CC   -!- POLYMORPHISM: KEL is responsible for the Kell blood group system.
CC       The molecular basis of the K=KEL1/k=KEL2 blood group antigens is a
CC       single variation in position 193; Thr-193 corresponds to KEL2 and
CC       Met-193 to KEL1. The molecular basis of the
CC       Kpa=KEL3/Kpb=KEL4/Kpc=KEL21 blood group antigens is a single
CC       variation in position 281; Arg-281 corresponds to KEL4, Trp-281 to
CC       KEL3 and Gln-281 to KEL21. 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. The
CC       molecular basis of the KEL11/KEL17 blood group antigens is a
CC       single variation in position 302; Val-302 corresponds to KEL11 and
CC       Ala-302 to KEL17. The molecular basis of the KEL14/KEL24 blood
CC       group antigens is a single variation in position 180; Arg-180
CC       corresponds to KEL14 and Pro-180 to KEL24.
CC   -!- SIMILARITY: Belongs to the peptidase M13 family.
CC   -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
CC       mutation database;
CC       URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=kell";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/KEL";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/kel/";
CC   -!- GENE_FAMILY: HOG000245574 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000197993;ENST00000355265;ENSP00000347409.
DR   EMBL; AF172609; - ;
DR   EMBL; AF172610; - ;
DR   EMBL; AF172611; - ;
DR   EMBL; AF172612; - ;
DR   EMBL; AF172613; - ;
DR   EMBL; AF172614; - ;
DR   EMBL; AF172615; - ;
DR   EMBL; AF172616; - ;
DR   EMBL; AF172617; - ;
DR   EMBL; AF172618; - ;
DR   EMBL; AF172619; - ;
DR   EMBL; AF172620; - ;
DR   EMBL; AF172621; - ;
DR   EMBL; AF172622; - ;
DR   EMBL; AF172623; - ;
DR   EMBL; AF172624; - ;
DR   EMBL; AF172625; - ;
DR   EMBL; AF172626; - ;
DR   EMBL; AF172627; - ;
DR   EMBL; AF279657; - ;
DR   EMBL; AK314831; - ;
DR   EMBL; AM085113; - ;
DR   EMBL; AM085114; - ;
DR   EMBL; AM085115; - ;
DR   EMBL; AM085116; - ;
DR   EMBL; AM085117; - ;
DR   EMBL; AM085118; - ;
DR   EMBL; AM085119; - ;
DR   EMBL; AM085120; - ;
DR   EMBL; AM085121; - ;
DR   EMBL; AM085122; - ;
DR   EMBL; AM085123; - ;
DR   EMBL; AM085124; - ;
DR   EMBL; AM085125; - ;
DR   EMBL; AM085126; - ;
DR   EMBL; AM085127; - ;
DR   EMBL; AM085128; - ;
DR   EMBL; AM183928; - ;
DR   EMBL; AM183929; - ;
DR   EMBL; AM403714; - ;
DR   EMBL; AM902715; - ;
DR   EMBL; AY228336; - ;
DR   EMBL; BC003135; - ;
DR   EMBL; BC050639; - ;
DR   EMBL; CH471198; - ;
DR   EMBL; DQ905957; - ;
DR   EMBL; DQ923321; - ;
DR   EMBL; EF208899; - ;
DR   EMBL; FM208212; - ;
DR   EMBL; FM208265; - ;
DR   EMBL; M64934; - ;
DR   EMBL; S80081; - ;
DR   UniProtKB/Swiss-Prot; P23276; B2RBV4; Q96RS8; Q99885; -.
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   IPI; IPI00220459; -.
DR   RefSeq; NP_000411.1; NM_000420.2.
DR   UniGene; Hs.368588; -.
DR   ProteinModelPortal; P23276; -.
DR   SMR; P23276; 79-732.
DR   IntAct; P23276; 1.
DR   MINT; MINT-1464824; -.
DR   STRING; P23276; -.
DR   MEROPS; M13.090; -.
DR   PRIDE; P23276; -.
DR   Ensembl; ENST00000355265; ENSP00000347409; ENSG00000197993.
DR   GeneID; 3792; -.
DR   KEGG; hsa:3792; -.
DR   UCSC; uc003wcb.1; human.
DR   CTD; 3792; -.
DR   GeneCards; GC07M136976; -.
DR   H-InvDB; HIX0007164; -.
DR   HGNC; HGNC:6308; KEL.
DR   MIM; 110900; phenotype.
DR   MIM; 613883; gene.
DR   neXtProt; NX_P23276; -.
DR   PharmGKB; PA30087; -.
DR   InParanoid; P23276; -.
DR   OMA; GGCPACD; -.
DR   OrthoDB; EOG47PX5G; -.
DR   PhylomeDB; P23276; -.
DR   NextBio; 14891; -.
DR   ArrayExpress; P23276; -.
DR   Bgee; P23276; -.
DR   CleanEx; HS_KEL; -.
DR   Genevestigator; P23276; -.
DR   GO; GO:0016021; C:integral to membrane; TAS:HGNC.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IDA:HGNC.
DR   GO; GO:0005515; F:protein binding; IPI:HGNC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0042310; P:vasoconstriction; TAS:HGNC.
DR   InterPro; IPR000718; Peptidase_M13.
DR   InterPro; IPR018497; Peptidase_M13_C.
DR   InterPro; IPR008753; Peptidase_M13_N.
DR   PANTHER; PTHR11733; Peptidase_M13; 1.
DR   Pfam; PF01431; Peptidase_M13; 1.
DR   Pfam; PF05649; Peptidase_M13_N; 1.
DR   PRINTS; PR00786; NEPRILYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   HOGENOMDNA; HS7.PE4225; -.
KW   ENSG000001979931755old_1320000031; ENSP000003474097901old_1320000031;
KW   A3F6J8_HUMAN; A8YPS5_HUMAN; B5U6Z5_HUMAN; C7TP28_HUMAN; Q05GI3_HUMAN;
KW   Q09GN6_HUMAN; Q0KH83_HUMAN; Q0KH84_HUMAN; Q0KH85_HUMAN; Q0KH86_HUMAN;
KW   Q0KH88_HUMAN; Q0KH89_HUMAN; Q0KH90_HUMAN; Q0KH91_HUMAN; Q0KH92_HUMAN;
KW   Q0KH95_HUMAN; Q0KH97_HUMAN; Q2A681_HUMAN; Q2A682_HUMAN; AF172609;
KW   AF172611; AF172612; AF172613; AF172614; AF172615; AF172616; AF172617;
KW   AF172619; AF172620; AF172621; AF172622; AF172623; AF172624; AF172625;
KW   AF172627; AF279657; AK314831; AM085113; AM085114; AM085115; AM085116;
KW   AM085118; AM085119; AM085120; AM085121; AM085122; AM085123; AM085124;
KW   AM085126; AM085127; AM085128; AM183928; AM183929; AM403714; AM902715;
KW   BC003135; BC050639; CH471198; DQ905957; DQ923321; EF208899; FM208212;
KW   M64934; S80081;
KW   Blood group antigen; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Membrane; Metal-binding; Metalloprotease; Polymorphism; Protease;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Zinc.
SQ   SEQUENCE   732 AA;  UNKNOWN MW;  UNKNOWN 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
//

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