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CAND1_CAEEL
ID   CAND1_CAEEL             Reviewed;        1274 AA.
AC   G5ED41;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Cullin-associated NEDD8-dissociated protein 1;
DE   AltName: Full=Cullin-associated and neddylation-dissociated protein 1;
GN   Name=cand-1; ORFNames=Y102A5A.1;
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).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP   AND INTERACTION WITH CUL-1; CUL-2; CUL-3; CUL-4; CUL-5 AND CUL-6.
RX   PubMed=20659444; DOI=10.1016/j.ydbio.2010.07.020;
RA   Bosu D.R., Feng H., Min K., Kim Y., Wallenfang M.R., Kipreos E.T.;
RT   "C. elegans CAND-1 regulates cullin neddylation, cell proliferation and
RT   morphogenesis in specific tissues.";
RL   Dev. Biol. 346:113-126(2010).
CC   -!- FUNCTION: Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3
CC       ubiquitin ligase complexes that promotes the exchange of the substrate-
CC       recognition F-box subunit in SCF complexes, thereby playing a key role
CC       in the cellular repertoire of SCF complexes. Acts as a F-box protein
CC       exchange factor (Probable). {ECO:0000305|PubMed:20659444}.
CC   -!- SUBUNIT: Interacts with cul-1, cul-2, cul-3, cul-4, cul-5 and cul-6.
CC       {ECO:0000269|PubMed:20659444}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20659444}.
CC   -!- DEVELOPMENTAL STAGE: In early embryos, expressed in all cells.
CC       Expression is higher during early stages and is reduced in late-stage
CC       embryos. Present in the one-cell stage zygote, indicating it is
CC       provided as a maternal product by the hermaphrodite parent. During
CC       larval stages, expressed in proliferative cell lineages, including the
CC       seam cells, intestine, P-lineage cells, somatic gonad, and germline.
CC       Also observed in a subset of non-proliferative tissues, including
CC       hypodermal cells (at protein level). {ECO:0000269|PubMed:20659444}.
CC   -!- DISRUPTION PHENOTYPE: Worms show impenetrant phenotypes, including
CC       developmental arrest, morphological defects of the vulva and tail and
CC       reduced fecundity. Worms also display supernumerary seam cell
CC       divisions, defective alae formation, and the accumulation of the
CC       SCF(lin-23) target, the glutamate receptor glr-1. Increased levels of
CC       the neddylated isoforms of Cul-2 and cul-4.
CC       {ECO:0000269|PubMed:20659444}.
CC   -!- SIMILARITY: Belongs to the CAND family. {ECO:0000305}.
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DR   EMBL; AL023822; CAA19440.1; -; Genomic_DNA.
DR   EMBL; Z81593; CAA19440.1; JOINED; Genomic_DNA.
DR   PIR; T25024; T25024.
DR   RefSeq; NP_507244.1; NM_074843.5.
DR   AlphaFoldDB; G5ED41; -.
DR   SMR; G5ED41; -.
DR   BioGRID; 45111; 7.
DR   IntAct; G5ED41; 1.
DR   STRING; 6239.Y102A5A.1; -.
DR   EPD; G5ED41; -.
DR   PaxDb; G5ED41; -.
DR   PeptideAtlas; G5ED41; -.
DR   EnsemblMetazoa; Y102A5A.1.1; Y102A5A.1.1; WBGene00013606.
DR   GeneID; 180125; -.
DR   KEGG; cel:CELE_Y102A5A.1; -.
DR   CTD; 180125; -.
DR   WormBase; Y102A5A.1; CE20378; WBGene00013606; cand-1.
DR   eggNOG; KOG1824; Eukaryota.
DR   GeneTree; ENSGT00390000017740; -.
DR   HOGENOM; CLU_007157_0_0_1; -.
DR   InParanoid; G5ED41; -.
DR   OMA; MGGTQDD; -.
DR   OrthoDB; 194023at2759; -.
DR   PhylomeDB; G5ED41; -.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   Reactome; R-CEL-8951664; Neddylation.
DR   Reactome; R-CEL-917937; Iron uptake and transport.
DR   PRO; PR:G5ED41; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00013606; Expressed in embryo and 4 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0060625; P:regulation of protein deneddylation; IMP:WormBase.
DR   GO; GO:0010265; P:SCF complex assembly; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039852; CAND1/CAND2.
DR   InterPro; IPR013932; TATA-bd_TIP120.
DR   PANTHER; PTHR12696; PTHR12696; 1.
DR   Pfam; PF08623; TIP120; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN           1..1274
FT                   /note="Cullin-associated NEDD8-dissociated protein 1"
FT                   /id="PRO_0000422240"
FT   REPEAT          41..79
FT                   /note="HEAT 1"
FT   REPEAT          127..167
FT                   /note="HEAT 2"
FT   REPEAT          375..413
FT                   /note="HEAT 3"
FT   REPEAT          500..540
FT                   /note="HEAT 4"
FT   REPEAT          617..655
FT                   /note="HEAT 5"
FT   REPEAT          671..709
FT                   /note="HEAT 6"
FT   REPEAT          1000..1038
FT                   /note="HEAT 7"
FT   REPEAT          1041..1078
FT                   /note="HEAT 8"
FT   REPEAT          1079..1117
FT                   /note="HEAT 9"
FT   REGION          320..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..348
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1274 AA;  141726 MW;  4D0D62BAD14B83D2 CRC64;
     MSAYHVGQLV DKMSNPDKDF RFMACNDLMK DLQTGTIALE DDSTAKVIRA LIKLLSDSNG
     EVQNLAIKCI GLLAQPSKIK THHLEYLVEE LTPHVFSKAE QSRDIHSLTL KAMILNLAPS
     ASSNATTTVV KRMLPKFVDS LSLCAPDDAA RVDVLDLIGE VLLRFGDVVP EMHKGSLKVM
     VDHLYSFRSA IRKKAITGIG HLASVINGEL YDELVQDLLK ELAQRSPPSS AAQNVQLRTL
     VIALSTVARA SGSRFSKHTP KVVPFLLQYL QIDPGTESEH DDLREASIQG LEVFLYRNPQ
     EVVAFEKEVI QQLTDALAYD PNYEYGDDDE DEQMEDDEDD DEDEYSDDED VTWKVRRAAA
     KAIEAMISSH RESLLNLSQK IGPVVIGRFK EREETVRTEI ISVYIALLNQ ISILVPDLQK
     AVVAADEDSI ETDDIVVIGG TKFSTNYLSR SQLAIIQSLA DQKDVLLRTI TKSMKKHPKT
     GPKCIELLSA LIRTYPSGLE DSLDDIIPAV SNILTDKNAS AQGKMTVLSF ISNALTLNNP
     KRFKNLLSPL TTIMTHSISE PFYKVSAEGL AVCCKYIDVL RELSACGGNE EAKKLLVVVE
     KKFMANDTDQ EVRERAISAI SMLLAAFKDV LKNETPAILE KMTERIGRDM TCLVAFRAST
     HIVEAGIIFS SAQLQSILRH VVDYVKKIAR SLRMTCLNFV EKLMKHSPAG SIPVEELTCV
     LGEMSNLISE TDLQITNQAF CCLTYAFLNF PTCVSLHMQP ILDSIIRLLT SPLIQGLALN
     SLLNLFTAIV KTDFPEKPTF ESLLDSVTSP VYDNVALSRH AHMAIASCAA VITESTQNLE
     KSRSLAKKLA QQLQTANMSD SIRLFAMITL GELGRRVPDT YSPDFPVKPE DLAIKAFNHH
     HEDLKSAAAQ ALGALAVGNL NVYLPFILEQ IRTQPKKQYL LLHALKEVIV WESSSEESTK
     STDLFRSAIV DIWGMLMANA GGNEDGTRSV VAECLGRLCS FDPESLLPKL KESMRSSDPA
     IRSSAVSAIK YMINDEKRIV DITLQKQIGD FLAAVRDEDL KVRRVALVVL NSAAHNKPAL
     VRDLLPDLLP AVYEETKLRK ELIKEVEMGP FKHQVDEGLD LRKCAFECMF TLLESCVDKI
     DITQFSSVME VGLSDQNHDV KLLNYLTLQR VANLAPGQVL QRIDRVCEPL KTQLNVRPRG
     NAVKQEVEKL EELKKAVIRV VYGLKLKLPE VERNPQFLDL YNTIKHTKEL EALANDVLKE
     SQRAVVYDTP META
 
 
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