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GXCB_DICDI
ID   GXCB_DICDI              Reviewed;        1198 AA.
AC   Q55E26; Q2MCX4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Rac guanine nucleotide exchange factor B;
GN   Name=gxcB; Synonyms=Trix; ORFNames=DDB_G0269424;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=AX2;
RX   PubMed=16781009; DOI=10.1016/j.ejcb.2006.05.005;
RA   Strehle A., Schleicher M., Faix J.;
RT   "Trix, a novel Rac guanine-nucleotide exchange factor from Dictyostelium
RT   discoideum is an actin-binding protein and accumulates at endosomes.";
RL   Eur. J. Cell Biol. 85:1035-1045(2006).
RN   [2]
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).
CC   -!- FUNCTION: Involved in the regulation of the late steps of the endocytic
CC       pathway. {ECO:0000269|PubMed:16781009}.
CC   -!- SUBUNIT: Binds to F-actin.
CC   -!- SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:16781009}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during vegetative growth and early
CC       stages of development. {ECO:0000269|PubMed:16781009}.
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DR   EMBL; AM181592; CAJ57479.1; -; mRNA.
DR   EMBL; AAFI02000005; EAL72062.1; -; Genomic_DNA.
DR   RefSeq; XP_645955.1; XM_640863.1.
DR   AlphaFoldDB; Q55E26; -.
DR   SMR; Q55E26; -.
DR   STRING; 44689.DDB0233173; -.
DR   PaxDb; Q55E26; -.
DR   PRIDE; Q55E26; -.
DR   EnsemblProtists; EAL72062; EAL72062; DDB_G0269424.
DR   GeneID; 8616899; -.
DR   KEGG; ddi:DDB_G0269424; -.
DR   dictyBase; DDB_G0269424; gxcB.
DR   eggNOG; KOG2046; Eukaryota.
DR   eggNOG; KOG3522; Eukaryota.
DR   HOGENOM; CLU_271096_0_0_1; -.
DR   InParanoid; Q55E26; -.
DR   OMA; LYSYLIM; -.
DR   PRO; PR:Q55E26; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR   GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR   GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR   GO; GO:0008093; F:cytoskeletal anchor activity; IBA:GO_Central.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0051764; P:actin crosslink formation; IDA:dictyBase.
DR   GO; GO:0051017; P:actin filament bundle assembly; IDA:dictyBase.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006887; P:exocytosis; IMP:dictyBase.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd00014; CH; 2.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.10.418.10; -; 3.
DR   Gene3D; 1.20.900.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR003096; SM22_calponin.
DR   Pfam; PF00307; CH; 3.
DR   Pfam; PF00621; RhoGEF; 1.
DR   PRINTS; PR00888; SM22CALPONIN.
DR   SMART; SM00033; CH; 3.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF47576; SSF47576; 2.
DR   SUPFAM; SSF48065; SSF48065; 1.
DR   PROSITE; PS50021; CH; 3.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Endocytosis; Endosome; Guanine-nucleotide releasing factor;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1198
FT                   /note="Rac guanine nucleotide exchange factor B"
FT                   /id="PRO_0000328627"
FT   DOMAIN          126..232
FT                   /note="Calponin-homology (CH) 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          341..449
FT                   /note="Calponin-homology (CH) 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          511..619
FT                   /note="Calponin-homology (CH) 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          632..846
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          876..1026
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          940..989
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1076..1198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..954
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        963..989
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1123..1157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1198 AA;  134479 MW;  FF31F4B5E94F0FEB CRC64;
     MFSNFFGSSK RNTIASSSSS SKKDKDNGKD ESSKLKNSGS STLPKPITNN ESGNNFITSP
     SVSSPLISPL SSSPSPLLSS SSNSIQSTSH QQQQQHQGVI TSLQMKPSCT SLTDDIEKKK
     QAKYDSSLEQ TARKWVCDVL EIQLEDDKTF YELFKNGVLL CRLINKLRGG TIKRINESTI
     SFKQLENIEN YLKACKTLGL QSVNLFNSID LHENKDISLV ITNIVVLGKH ASKIEGYNGI
     HLAGERKIIK ITTTPVSPLF GGNHNNNNNN NNNNNTSNGD LSPVSITSAS GGSSNYNSYS
     NNPLNKSSNG KKAKWRKSVK IPAVSSLNSD IRTKEAFKFS PELQKAAQDW IEEVTKEKFK
     LPSFSSSLKD GILLCRVINT IIPNTILYIN NGNSSFKKME NIGNYLKGCL VVGLKKTDLF
     DTPDLFEEKN INFVISNIHV LGNHVNKMYS HLKLPLIKNI GNGGNGGNGG IGGGGGSDGS
     PLKMYSSIIH SKFGNGSSNT SSGNGGVIIP PEDMKDLKDW INHHLRAHHS LQIGSDMSND
     LRNGVTLLTL LEELTLQKVG IFAREPVLPW HFMQNICLLL NFLRENSVHN VSDISPHDLF
     NGDIHSLCMI TRLIRENFDT DHQMKSIPMD TRRQKVIEEI IATEQSYVKS LSTVYNLLIV
     PLLNSLDTNS PILSNDEISS IFGNWEHLLR SHINLLKEFK LKLNLPFNDL TIDDSNQNQN
     HNNIFGDSIF DSNITIGDVF LEKCEFLKDN YTNYINNYDN SYQRVKRLKK SNSNFEELVN
     TFEIFQDTHN GLDLYSYLIM PIQRIVRYIL LLKEVIKYTP STHPDYQMLQ NAKENIKRVA
     DHVNESKMAV ENKRKILSIQ DSIQNLQFNL MDKERTYIRE GFLEIEDTFK KDSYFFLFSD
     LLLFVKYKPS EETGKEFKYK EVFYLDQVVD VSDILSDDEG EACVDGDDDG GEYEGGNGDA
     TSGSADPEDQ TLRRSCNSNN NNNSNSNKSN TVYSFEIETC EFSLVLLAES HTEKIEWMED
     LRSCLQHQLI KEEDQLSSLS LSDNDDDNDA DADVESSLNS ISSPLLLLNN NNIINNNNNN
     NNNNNNNNNN NNNNNNCKNS NININSSIDN NSDNNNNDYD SKINSEENGD SSDEENKTSN
     RRSVSFKTHK RLESDETISD TESDDYELVC GRSKKSQPPP VPPRKITFSD TIKNIDNQ
 
 
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