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WHT1_CAEEL
ID   WHT1_CAEEL              Reviewed;         671 AA.
AC   Q11180; A0A2K5ATT2; A0A2K5ATU8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   22-APR-2020, sequence version 3.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=ABC transporter ATP-binding protein/permease wht-1;
GN   Name=wht-1 {ECO:0000312|WormBase:C05D10.3a};
GN   ORFNames=C05D10.3 {ECO:0000312|WormBase:C05D10.3a};
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   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15522294; DOI=10.1016/j.jmb.2004.09.052;
RA   Zhao Z., Sheps J.A., Ling V., Fang L.L., Baillie D.L.;
RT   "Expression analysis of ABC transporters reveals differential functions of
RT   tandemly duplicated genes in Caenorhabditis elegans.";
RL   J. Mol. Biol. 344:409-417(2004).
RN   [3]
RP   FUNCTION.
RX   PubMed=16723499; DOI=10.1091/mbc.e06-03-0192;
RA   Sundaram P., Echalier B., Han W., Hull D., Timmons L.;
RT   "ATP-binding cassette transporters are required for efficient RNA
RT   interference in Caenorhabditis elegans.";
RL   Mol. Biol. Cell 17:3678-3688(2006).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=17850180; DOI=10.1371/journal.pbio.0050237;
RA   Hunt-Newbury R., Viveiros R., Johnsen R., Mah A., Anastas D., Fang L.,
RA   Halfnight E., Lee D., Lin J., Lorch A., McKay S., Okada H.M., Pan J.,
RA   Schulz A.K., Tu D., Wong K., Zhao Z., Alexeyenko A., Burglin T.,
RA   Sonnhammer E., Schnabel R., Jones S.J., Marra M.A., Baillie D.L.,
RA   Moerman D.G.;
RT   "High-throughput in vivo analysis of gene expression in Caenorhabditis
RT   elegans.";
RL   PLoS Biol. 5:E237-E237(2007).
RN   [5]
RP   FUNCTION.
RX   PubMed=18245353; DOI=10.1534/genetics.107.081588;
RA   Sundaram P., Han W., Cohen N., Echalier B., Albin J., Timmons L.;
RT   "Caenorhabditis elegans ABCRNAi transporters interact genetically with rde-
RT   2 and mut-7.";
RL   Genetics 178:801-814(2008).
CC   -!- FUNCTION: Required for efficient RNA interference (RNAi)
CC       (PubMed:16723499, PubMed:18245353). Plays a role in germline
CC       development (PubMed:16723499, PubMed:18245353).
CC       {ECO:0000269|PubMed:16723499, ECO:0000269|PubMed:18245353}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000312|WormBase:C05D10.3a};
CC         IsoId=Q11180-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:C05D10.3b};
CC         IsoId=Q11180-2; Sequence=VSP_060561;
CC   -!- TISSUE SPECIFICITY: Expressed in the intestine in both larvae and
CC       adults (PubMed:17850180). Expressed in the gut of males
CC       (PubMed:15522294). {ECO:0000269|PubMed:15522294,
CC       ECO:0000269|PubMed:17850180}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos.
CC       {ECO:0000269|PubMed:15522294}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
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DR   EMBL; BX284603; SPC47526.1; -; Genomic_DNA.
DR   EMBL; BX284603; SPC47527.1; -; Genomic_DNA.
DR   PIR; B88474; B88474.
DR   AlphaFoldDB; Q11180; -.
DR   SMR; Q11180; -.
DR   STRING; 6239.C05D10.3; -.
DR   TCDB; 3.A.1.204.3; the atp-binding cassette (abc) superfamily.
DR   iPTMnet; Q11180; -.
DR   EPD; Q11180; -.
DR   PaxDb; Q11180; -.
DR   PeptideAtlas; Q11180; -.
DR   EnsemblMetazoa; C05D10.3a.1; C05D10.3a.1; WBGene00015479. [Q11180-1]
DR   EnsemblMetazoa; C05D10.3b.1; C05D10.3b.1; WBGene00015479. [Q11180-2]
DR   WormBase; C05D10.3a; CE52537; WBGene00015479; wht-1. [Q11180-1]
DR   WormBase; C05D10.3b; CE52612; WBGene00015479; wht-1. [Q11180-2]
DR   eggNOG; KOG0061; Eukaryota.
DR   GeneTree; ENSGT00970000196382; -.
DR   HOGENOM; CLU_000604_57_6_1; -.
DR   InParanoid; Q11180; -.
DR   OrthoDB; 1022017at2759; -.
DR   PhylomeDB; Q11180; -.
DR   PRO; PR:Q11180; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00015479; Expressed in embryo and 3 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC_2_trans.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR043926; ABCG_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005284; Pigment_permease/Abcg.
DR   Pfam; PF01061; ABC2_membrane; 1.
DR   Pfam; PF19055; ABC2_membrane_7; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00955; 3a01204; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..671
FT                   /note="ABC transporter ATP-binding protein/permease wht-1"
FT                   /id="PRO_0000449487"
FT   TOPO_DOM        1..408
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        409..429
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        430..451
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        452..472
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        473..497
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        498..518
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        519..525
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        526..546
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        547..550
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        551..571
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        572..644
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        645..665
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        666..671
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          64..310
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         100..107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   VAR_SEQ         1..259
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060561"
SQ   SEQUENCE   671 AA;  75210 MW;  F47D515E3A4FD545 CRC64;
     MHKAPISTLI LDSLFSNMML AEMMNDDQLE LLKHQQTGIQ PVVPEGCNLY WSSLNVTGPE
     TKPTNFVDRF RNNMPKRRVK EILHNVSGMA ESGKLLAILG SSGAGKTTLM NVLTSRNLTN
     LDVQGSILID GRRANKWKIR EMSAFVQQHD MFVGTMTARE HLQFMARLRM GDQYYSDHER
     QLRVEQVLTQ MGLKKCADTV IGIPNQLKGL SCGEKKRLSF ASEILTCPKI LFCDEPTSGL
     DAFMAGHVVQ ALRSLADNGM TVIITIHQPS SHVYSLFNNV CLMACGRVIY LGPGDQAVPL
     FEKCGYPCPA YYNPADHLIR TLAVIDSDRA TSMKTISKIR QGFLSTDLGQ SVLAIGNANK
     LRAASFVTGS DTSEKTKTFF NQDYNASFWT QFLALFWRSW LTVIRDPNLL SVRLLQILIT
     AFITGIVFFQ TPVTPATIIS INGIMFNHIR NMNFMLQFPN VPVITAELPI VLRENANGVY
     RTSAYFLAKN IAELPQYIIL PILYNTIVYW MSGLYPNFWN YCFASLVTIL ITNVAISISY
     AVATIFANTD VAMTILPIFV VPIMAFGGFF ITFDAIPSYF KWLSSLSYFK YGYEALAINE
     WDSIKVIPEC FNSSMTAFAL DSCPKNGHQV LESIDFSASH KIFDISILFG MFIGIRIIAY
     VALLIRSYNN T
 
 
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