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BORG5_BOVIN
ID   BORG5_BOVIN             Reviewed;         361 AA.
AC   Q17QW1;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Cdc42 effector protein 1;
DE   AltName: Full=Binder of Rho GTPases 5;
GN   Name=CDC42EP1 {ECO:0000250|UniProtKB:Q00587};
GN   Synonyms=BORG5 {ECO:0000250|UniProtKB:Q00587};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1] {ECO:0000312|EMBL:AAI18149.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford {ECO:0000312|EMBL:AAI18149.1};
RC   TISSUE=Ascending colon {ECO:0000312|EMBL:AAI18149.1};
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably involved in the organization of the actin
CC       cytoskeleton. Induced membrane extensions in fibroblasts (By
CC       similarity). {ECO:0000250|UniProtKB:Q00587}.
CC   -!- SUBUNIT: Interacts with RHOQ and CDC42, in a GTP-dependent manner.
CC       {ECO:0000250|UniProtKB:Q00587}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- DOMAIN: The CRIB domain mediates interaction with CDC42.
CC       {ECO:0000250|UniProtKB:Q00587}.
CC   -!- SIMILARITY: Belongs to the BORG/CEP family. {ECO:0000255}.
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DR   EMBL; BC118148; AAI18149.1; -; mRNA.
DR   RefSeq; NP_001068963.1; NM_001075495.1.
DR   AlphaFoldDB; Q17QW1; -.
DR   STRING; 9913.ENSBTAP00000028798; -.
DR   PaxDb; Q17QW1; -.
DR   Ensembl; ENSBTAT00000028798; ENSBTAP00000028798; ENSBTAG00000030258.
DR   GeneID; 511099; -.
DR   KEGG; bta:511099; -.
DR   CTD; 11135; -.
DR   VEuPathDB; HostDB:ENSBTAG00000030258; -.
DR   VGNC; VGNC:27072; CDC42EP1.
DR   eggNOG; ENOG502RZ2H; Eukaryota.
DR   GeneTree; ENSGT00940000160068; -.
DR   HOGENOM; CLU_787446_0_0_1; -.
DR   InParanoid; Q17QW1; -.
DR   OMA; PRGHCPN; -.
DR   OrthoDB; 1244464at2759; -.
DR   TreeFam; TF331725; -.
DR   Reactome; R-BTA-9013404; RAC2 GTPase cycle.
DR   Reactome; R-BTA-9013406; RHOQ GTPase cycle.
DR   Reactome; R-BTA-9013408; RHOG GTPase cycle.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000030258; Expressed in urinary bladder and 100 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
DR   GO; GO:0031274; P:positive regulation of pseudopodium assembly; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR   GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR   InterPro; IPR029273; Cdc42_effect.
DR   InterPro; IPR000095; CRIB_dom.
DR   Pfam; PF14957; BORG_CEP; 1.
DR   Pfam; PF00786; PBD; 1.
DR   SMART; SM00285; PBD; 1.
DR   PROSITE; PS50108; CRIB; 1.
PE   2: Evidence at transcript level;
KW   Cell shape; Cytoplasm; Cytoskeleton; Membrane; Methylation; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..361
FT                   /note="Cdc42 effector protein 1"
FT                   /id="PRO_0000278119"
FT   DOMAIN          38..52
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   REPEAT          220..226
FT                   /note="1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          229..235
FT                   /note="2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          236..242
FT                   /note="3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          243..249
FT                   /note="4"
FT                   /evidence="ECO:0000255"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..249
FT                   /note="4 X 7 AA tandem repeats of [PT]-[AT]-A-[ENT]-[PT]-
FT                   [PTS]-[AG]"
FT                   /evidence="ECO:0000255"
FT   REGION          320..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..241
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         34
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91W92"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91W92"
FT   MOD_RES         53
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91W92"
FT   MOD_RES         180
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         190
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         192
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         195
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A1A5P0"
FT   MOD_RES         320
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
SQ   SEQUENCE   361 AA;  37334 MW;  85AE4CE083E082AD CRC64;
     MPGPQGAGGA PAMNLGKLSP VGWVSSSQGK KRLTADMISP PLGDFRHTMH VGRGGDVFGD
     TSFLSNHGGG SGSTHRSPRG FLAKKLQLVR RVGAPPRRMA SPPAPSPAPP AISPIIKNAI
     SLPQLNQAAY DSLVVGKLSF DRSPASSTDG HSAYGLDSGF CTISRLPRPE KPRDRDRDSS
     FPAEPELRRS DSLLSFRLDL DLGPSLLTEL LGAMSLSEGS AAETPAPAPA ASPPASVANP
     PAPASSPSLR GRCPNGVTTR LGPVAEARAS VVGEGPRAPA DEGPGKHRGA VSGGSQSRHH
     YTEVDARAEG LGALSQARAS WGSLDEEWGA SQAGSRTPVP STVQANTFEF ADAEEDDEVK
     V
 
 
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