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NAR5_BOVIN
ID   NAR5_BOVIN              Reviewed;         316 AA.
AC   Q0VC22;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Ecto-ADP-ribosyltransferase 5;
DE            EC=2.4.2.31;
DE   AltName: Full=ADP-ribosyltransferase C2 and C3 toxin-like 5;
DE            Short=ARTC5;
DE   AltName: Full=Mono(ADP-ribosyl)transferase 5;
DE   AltName: Full=NAD(P)(+)--arginine ADP-ribosyltransferase 5;
DE   Flags: Precursor;
GN   Name=ART5;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-
CC         ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149,
CC         Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:142554; EC=2.4.2.31;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Membrane {ECO:0000305}.
CC       Note=Membrane-associated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; BC120389; AAI20390.1; -; mRNA.
DR   RefSeq; NP_001069983.1; NM_001076515.1.
DR   AlphaFoldDB; Q0VC22; -.
DR   SMR; Q0VC22; -.
DR   STRING; 9913.ENSBTAP00000039644; -.
DR   PaxDb; Q0VC22; -.
DR   PRIDE; Q0VC22; -.
DR   GeneID; 618664; -.
DR   KEGG; bta:618664; -.
DR   eggNOG; ENOG502SKQR; Eukaryota.
DR   InParanoid; Q0VC22; -.
DR   OrthoDB; 963174at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; IBA:GO_Central.
DR   InterPro; IPR000768; ART.
DR   Pfam; PF01129; ART; 1.
DR   PRINTS; PR00970; RIBTRNSFRASE.
DR   PROSITE; PS01291; ART; 1.
DR   PROSITE; PS51996; TR_MART; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosyltransferase; Membrane; NAD; NADP;
KW   Nucleotidyltransferase; Reference proteome; Secreted; Signal; Transferase.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..316
FT                   /note="Ecto-ADP-ribosyltransferase 5"
FT                   /id="PRO_0000379471"
FT   DOMAIN          70..261
FT                   /note="TR mART core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        229
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   BINDING         107
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..266
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   316 AA;  34894 MW;  7209F0A5540E33BF CRC64;
     MIQATLLISL SCLSFYTLGS GVRRYDPGQG VTIQYLSLAP DTFDDAYVGC SEEMEEKAVL
     LLEKEMANHT RLRESWETAQ KAWEQKRAGL TLPPGFRSQH GIAIMVYTNS SNTLYRELNQ
     AVRTGGGSWE SYMKHFPFKA LHFYLTRALQ LLRGGGGCSR EPRQEVFRGV RRIHFVPKSV
     GDSIRLGQFA SSSLDEAVAC GFGSATFFSL RTCSGAPIQA LSVFPEEREV LIPPYEVFVV
     SNFSKDGNKS LMTLSSSDQM CSHFNCAYLG EKKRPSCEFV PIGGQGDSLS KGAFSLLSWK
     TLLLASWGFQ LLGAGL
 
 
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