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Database: UniProt
Entry: G3I620_CRIGR
LinkDB: G3I620_CRIGR
Original site: G3I620_CRIGR 
ID   G3I620_CRIGR            Unreviewed;       471 AA.
AC   G3I620;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   25-OCT-2017, entry version 27.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:EGW07801.1};
GN   ORFNames=I79_018931 {ECO:0000313|EMBL:EGW07801.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW07801.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W.,
RA   Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B.,
RA   Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J.,
RA   Quake S.R., Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell
RT   line.";
RL   Nat. Biotechnol. 29:735-741(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; JH001338; EGW07801.1; -; Genomic_DNA.
DR   RefSeq; XP_003510642.1; XM_003510594.3.
DR   RefSeq; XP_007635992.1; XM_007637802.2.
DR   MEROPS; M18.002; -.
DR   GeneID; 100764694; -.
DR   KEGG; cge:100764694; -.
DR   CTD; 23549; -.
DR   InParanoid; G3I620; -.
DR   KO; K01267; -.
DR   Proteomes; UP000001075; Unassembled WGS sequence.
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   ECO:0000313|EMBL:EGW07801.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001075};
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:UP000001075};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   471 AA;  51947 MW;  BB84CAA4961591F9 CRC64;
     MNGRARKEAI QATARELLKF VNRSPSPFHV VAECRSRLLQ AGFRELKETE GWDIVPENKY
     FLTRNSSSII AFAVGGQYVP GNGFSLIGAH TDSPCLRVKR KSRRSQAGYH QVGVETYGGG
     IWSSWFDRDL TLAGRVIIKC PTSGRLEQRL VHVDRPILRI PHLAIHLQRS INENFGPNTE
     MHLVPILATA VQEELEKGTP EPGPINAADE RHHSVLMSLL CTQLGLGPEN ILEMELCLAD
     TQLAVLGGAY EEFIFAPRLD NLHSCFCALQ ALIDSCAAPS SLAREPHVRM VTFYDNEEVG
     SESAQGAQSL LTELVLRRIS ATPQHLTAFE EAIPKSFMIS ADMAHAVHPN YVDKHEENHR
     PLFHKGPVIK VNSKQRYASN AVSEALIREV ASQVGVPLQD LMVRNDSPCG TTIGPILASR
     LGLRVLDLGS PQLAMHSIRE TACTTGVLQT LTLFKGFFEL FPSVSRNLAV D
//
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