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CLCD_DICDI
ID   CLCD_DICDI              Reviewed;        1000 AA.
AC   Q1ZXJ0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Chloride channel protein D;
GN   Name=clcD; ORFNames=DDB_G0278639;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17659086; DOI=10.1186/gb-2007-8-7-r144;
RA   Sawai S., Guan X.-J., Kuspa A., Cox E.C.;
RT   "High-throughput analysis of spatio-temporal dynamics in Dictyostelium.";
RL   Genome Biol. 8:R144.1-R144.15(2007).
CC   -!- FUNCTION: Voltage-gated chloride channel. Chloride channels may have
CC       several functions including the regulation of cell volume, membrane
CC       potential stabilization and signal transduction (By similarity).
CC       Required for normal aggregation. {ECO:0000250,
CC       ECO:0000269|PubMed:17659086}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells display slow oscillators with delayed
CC       aggregation. {ECO:0000269|PubMed:17659086}.
CC   -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000023; EAS66897.1; -; Genomic_DNA.
DR   RefSeq; XP_001134581.3; XM_001134581.2.
DR   AlphaFoldDB; Q1ZXJ0; -.
DR   SMR; Q1ZXJ0; -.
DR   STRING; 44689.DDB0233313; -.
DR   PaxDb; Q1ZXJ0; -.
DR   PRIDE; Q1ZXJ0; -.
DR   GeneID; 8621440; -.
DR   KEGG; ddi:DDB_G0278639; -.
DR   dictyBase; DDB_G0278639; clcD.
DR   eggNOG; KOG0474; Eukaryota.
DR   HOGENOM; CLU_003181_4_1_1; -.
DR   InParanoid; Q1ZXJ0; -.
DR   OMA; FMHEHIS; -.
DR   PhylomeDB; Q1ZXJ0; -.
DR   Reactome; R-DDI-2672351; Stimuli-sensing channels.
DR   PRO; PR:Q1ZXJ0; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR   Gene3D; 3.10.580.10; -; 2.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR014743; Cl-channel_core.
DR   InterPro; IPR001807; Cl-channel_volt-gated.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   SUPFAM; SSF81340; SSF81340; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   3: Inferred from homology;
KW   CBS domain; Chloride; Chloride channel; Ion channel; Ion transport;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN           1..1000
FT                   /note="Chloride channel protein D"
FT                   /id="PRO_0000328046"
FT   TOPO_DOM        1..256
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        534..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        678..698
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        710..730
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        733..753
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        772..792
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          824..881
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          926..984
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1000 AA;  112657 MW;  4860E16E1F153FBE CRC64;
     MSSGNPFDNG NPNDGNKSPS IDELYSPSES LARDGDDNNN NNNNNNNNNN NNNNNNNSSV
     SEKKKSKKKV RIQEEERLTE SYDDDGDDEE RRAYIENEEG EEEETEDGII LQPIVRDHST
     YRPKNLYGSS DDIREGDSFG AKVSKTFGKT NKKIKQKIGE SNKKIETRVK HSNKAIEEGW
     KTIAQTTMKP VDNIREQHHR RAEQHEVAER AVWFKDKLQI QKYECLDYVT IYNKAHRNEL
     YKNFSKLASD HEVLRWIVSL FMGIFIGVIA YFSHACVSNI TKYKFKFVEA VLELDLFLAF
     LTYFLLNTLL ATCSSLLAVY YEPTAAGSGI PEVKGYLNGT KIPHTLKMKT LWTKFLSMVL
     AVSSGLQAGS EGPMIHIGAI VGNGFSQAQS KEFGFKIPFL RSFRNDKDKR DFVTSGAGAG
     VAAAFSAPLG GTLFSLEEVS SFWSIALTWR AFFCCMVATY TMNVLQSNSG SLTGLIIFNT
     GIGDKESYNW FEIIPFLLIG VLGGLGGALF TWINVKVTEF RREKINKIKS LRVLEVFLII
     GLSTCIQFFL PLFFSCQNTA PFIPSVGNST LTDVTLTNGA FYNSTIINGT FYNSTIANGT
     IYNSKFYNSS IYNSTITNGT GVSYDPAETL KELSEFKRFN CKEGWYNPMA TLIFASYEES
     ITNLLKVNSN NVTNTERLGL WPMFLFCIFY LFFAAYTAGC AVATGTLVPM LVIGASYGRF
     VGLVVYHILG DKVSIDPGIY AVMGAAAFMG GVSRLTISLT VILIEITDRL KYLLPLMLTV
     MTAKWVADAL IHPLFDLLMQ MKYIPYLELD QSKEMKLMMC KHIMAKKPVY LAEKDTLGNL
     RVLKETRHNG FPVVNNDEEK LVKGLILRTQ LLMILERISD VYIPNSEAIY SHIEYTTKLT
     WKLPSVNDFN FDPADYSQEI DLSDVMNLTV ITVNVEFAVS EAFQLFRTMG LRHMPVVNEN
     NKLKGIITKK DLLEKTCEQR YRELNHMKLG IDQLIHVGDE
 
 
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