位置:首页 > 蛋白库 > TRI23_CAEEL
TRI23_CAEEL
ID   TRI23_CAEEL             Reviewed;         539 AA.
AC   Q09654;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 3.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=E3 ubiquitin-protein ligase arc-1;
DE            EC=2.3.2.27;
DE   AltName: Full=Putative GTP-binding protein trim-23 homolog;
DE   AltName: Full=RING-type E3 ubiquitin transferase arc-1 {ECO:0000305};
GN   Name=arc-1; Synonyms=arl-4; ORFNames=ZK1320.6;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase.
CC       {ECO:0000250|UniProtKB:P36406}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the small GTPase
CC       superfamily. Arf family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z46934; CAA87044.3; -; Genomic_DNA.
DR   PIR; T27752; T27752.
DR   RefSeq; NP_496089.3; NM_063688.5.
DR   AlphaFoldDB; Q09654; -.
DR   SMR; Q09654; -.
DR   BioGRID; 39848; 1.
DR   IntAct; Q09654; 1.
DR   MINT; Q09654; -.
DR   STRING; 6239.ZK1320.6; -.
DR   EPD; Q09654; -.
DR   PaxDb; Q09654; -.
DR   EnsemblMetazoa; ZK1320.6.1; ZK1320.6.1; WBGene00000180.
DR   GeneID; 174525; -.
DR   KEGG; cel:CELE_ZK1320.6; -.
DR   UCSC; ZK1320.6; c. elegans.
DR   CTD; 174525; -.
DR   WormBase; ZK1320.6; CE37598; WBGene00000180; arc-1.
DR   eggNOG; KOG0070; Eukaryota.
DR   eggNOG; KOG4185; Eukaryota.
DR   GeneTree; ENSGT00940000158562; -.
DR   HOGENOM; CLU_033905_0_0_1; -.
DR   InParanoid; Q09654; -.
DR   OMA; ACEERYE; -.
DR   OrthoDB; 1362554at2759; -.
DR   PhylomeDB; Q09654; -.
DR   Reactome; R-CEL-1660514; Synthesis of PIPs at the Golgi membrane.
DR   Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q09654; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00000180; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR024156; Small_GTPase_ARF.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   InterPro; IPR027370; Znf-RING_LisH.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11711; PTHR11711; 1.
DR   Pfam; PF00025; Arf; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..539
FT                   /note="E3 ubiquitin-protein ligase arc-1"
FT                   /id="PRO_0000207486"
FT   ZN_FING         6..53
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         103..149
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   REGION          369..539
FT                   /note="ARF-like"
FT   BINDING         376..383
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         422..426
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         481..484
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   539 AA;  60682 MW;  79F959556BB0755A CRC64;
     MNEYGCNVCN EEYSARDPLK CPRVLTGCGH TICHNCAISI AGRNSSIFCP FDRTATQIPG
     GDLQNLKKNF ALLELLEKIA DGGGLLEKSG EVVKFDRYSK ERLLNLECDE DSEHVAVIYC
     TVCDSNLCER CSESTHSTNV LSKHRRIPLT EKPPPLVHCR LHSSYVVEFV CKELSCDTES
     PLMCMMCRDY GRHKGHSHVL IEKEVEDLRE KVREHLGELS KQSETIGNAL HSIDSVIHEL
     TPGQEDGSLE ETRQEVRNHF RRLRTALDRD EEDAVETVDR YARNRVESLQ TQKERLEAIS
     SKIGNTCTTL QKALIMERGK ILDRKDDLLA LAESTAAEPT AVLDQSQLST RIAFSFLNDR
     KLHIGDFIES RVVLLGLDGA GKTSIVRRLK KVQMDTVMAP HPTIGFNIET IHYKNYRLNF
     WDVGGLPKLR HLWKHYYSNA QAIFYVIDGY AVERFSEAIK ELNRVMSDPL VGTCPVIVAV
     NRKDGYALNG HMDALLSQLE ALPFQHHFHC CDAATGSGID QIIDQITVCL SRLNGTCPV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024