(data stored in ACNUC16324 zone)

HOGENOM: MOUSE6_PE599

ID   MOUSE6_PE599                         STANDARD;      PRT;   713 AA.
AC   MOUSE6_PE599; Q9EQF2; Q499D7;
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 homolog; EC=3.4.24 -;AltName:
DE   CD_antigen=CD238; (MOUSE6.PE599).
GN   Name=Kel;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE6.PE599.
CC       Mus musculus chromosome 6 NCBIM37  sequence 1..149517037 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:KELL_MOUSE
CC   -!- FUNCTION: Zinc endopeptidase with endothelin-3-converting enzyme
CC       activity. Cleaves EDN1, EDN2 and EDN3 (By similarity).
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 (By similarity). Note=Spans the erythrocyte membrane, and
CC       is attached to the underlying cytoskeleton (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in spleen. Weaker expression
CC       in testis and heart.
CC   -!- PTM: N-glycosylated.
CC   -!- SIMILARITY: Belongs to the peptidase M13 family.
CC   -!- GENE_FAMILY: HOG000245574 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000029866;ENSMUST00000031899;ENSMUSP00000031899.
DR   EMBL; AF252870; - ;
DR   EMBL; AF336378; - ;
DR   EMBL; AK028430; - ;
DR   EMBL; BC099961; - ;
DR   UniProtKB/Swiss-Prot; Q9EQF2; Q499D7; -.
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   IPI; IPI00111137; -.
DR   RefSeq; NP_115929.3; NM_032540.3.
DR   UniGene; Mm.19958; -.
DR   ProteinModelPortal; Q9EQF2; -.
DR   SMR; Q9EQF2; 60-713.
DR   IntAct; Q9EQF2; 1.
DR   STRING; Q9EQF2; -.
DR   MEROPS; M13.090; -.
DR   PRIDE; Q9EQF2; -.
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   eggNOG; roNOG07550; -.
DR   GeneTree; ENSGT00550000074200; -.
DR   InParanoid; Q9EQF2; -.
DR   OMA; GGCPACD; -.
DR   OrthoDB; EOG47PX5G; -.
DR   PhylomeDB; Q9EQF2; -.
DR   NextBio; 303717; -.
DR   ArrayExpress; Q9EQF2; -.
DR   Bgee; Q9EQF2; -.
DR   CleanEx; MM_KEL; -.
DR   Genevestigator; Q9EQF2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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; ISS:HGNC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; MOUSE6.PE599; -.
KW   ENSMUSG000000298665old_1320000031; ENSMUSP000000318991old_1320000031;
KW   AF252870; AF336378; AK028430; BC099961;
KW   Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Zinc.
SQ   SEQUENCE   713 AA;  UNKNOWN MW;  UNKNOWN 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
//

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