GenomeNet

Database: UniProt
Entry: H2RKN2_TAKRU
LinkDB: H2RKN2_TAKRU
Original site: H2RKN2_TAKRU 
ID   H2RKN2_TAKRU            Unreviewed;       469 AA.
AC   H2RKN2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   25-OCT-2017, entry version 24.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|Ensembl:ENSTRUP00000000695};
GN   Name=dnpep {ECO:0000313|Ensembl:ENSTRUP00000000695};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae;
OC   Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000000695, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000000695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A.,
RA   Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu
RT   facilitates insights into distinct features of genome evolution in
RT   teleosts and mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000000695}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSTRUP00000000695}.
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DR   MEROPS; M18.002; -.
DR   Ensembl; ENSTRUT00000000698; ENSTRUP00000000695; ENSTRUG00000000306.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; COG1362; LUCA.
DR   GeneTree; ENSGT00390000003164; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005226};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   469 AA;  51312 MW;  75983781CE0C203A CRC64;
     SVIMKTSKEA VQAAAKEFLQ FVNRGVSPYH VVEECRQRLL KAGFLELKEV DQWDIQPSNK
     YFLTRNFSSI IAFAVGGRYQ PGNGFSMVGA HTDSPCLRVK PRSKRTKQGC LQVGVECYGG
     GIWNTWFDRD LTIAGRVMVK CWQSDAKLVH RLVHIPRPML RIPHLAIHLQ RDINDSFGPN
     KENHLVPIIA TAVQEELETG SASSGDASSA AEKHHPALVK VLCAELGVEP EALLDFELCL
     TDTQPAALGG VYEEFIFSPR LDNLHSCFCA LQGLVQSCAG ESLAHDPNIR MITLFDNEEV
     GSESAQGAQS NLTELILGRL ASSTTNITAF QQAAPRSFMI SADMAHAVHP NYQEKHEENH
     RPAFHKGPVI KFNSNQRYAT TAVTASVVRE IGSRVGVPLQ DVMVRNDSPC GTTIGPILAS
     RLGIPVLDIG APQLSMHSIR EMCCTSSVLQ SITLFKDAPV IPRSPPQAG
//
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