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