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GGTB2_CAEEL
ID   GGTB2_CAEEL             Reviewed;         335 AA.
AC   P41992; Q2V4X4;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Probable geranylgeranyl transferase type-2 subunit beta;
DE            EC=2.5.1.60;
DE   AltName: Full=Geranylgeranyl transferase type II subunit beta;
DE            Short=GGTase-II-beta;
DE   AltName: Full=Rab geranyl-geranyltransferase subunit beta;
DE            Short=Rab GG transferase beta;
DE            Short=Rab GGTase beta;
DE   AltName: Full=Rab geranylgeranyltransferase subunit beta;
DE   AltName: Full=Type II protein geranyl-geranyltransferase subunit beta;
GN   Name=ggtb-1; ORFNames=B0280.1;
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], AND ALTERNATIVE SPLICING.
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).
CC   -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC       geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an
CC       -XXCC, -XCXC and -CCXX C-terminal. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] =
CC         diphosphate + S-geranylgeranyl-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC         ChEBI:CHEBI:86021; EC=2.5.1.60;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=P41992-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=P41992-2; Sequence=VSP_018160;
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC       family. {ECO:0000305}.
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DR   EMBL; FO080148; CCD61597.1; -; Genomic_DNA.
DR   EMBL; FO080148; CCD61598.1; -; Genomic_DNA.
DR   RefSeq; NP_498559.1; NM_066158.6. [P41992-1]
DR   RefSeq; NP_741214.2; NM_171183.3. [P41992-2]
DR   AlphaFoldDB; P41992; -.
DR   SMR; P41992; -.
DR   BioGRID; 41210; 3.
DR   STRING; 6239.B0280.1a; -.
DR   EPD; P41992; -.
DR   PaxDb; P41992; -.
DR   PeptideAtlas; P41992; -.
DR   PRIDE; P41992; -.
DR   EnsemblMetazoa; B0280.1a.1; B0280.1a.1; WBGene00015099. [P41992-1]
DR   EnsemblMetazoa; B0280.1b.1; B0280.1b.1; WBGene00015099. [P41992-2]
DR   EnsemblMetazoa; B0280.1b.2; B0280.1b.2; WBGene00015099. [P41992-2]
DR   GeneID; 175998; -.
DR   KEGG; cel:CELE_B0280.1; -.
DR   UCSC; B0280.1a; c. elegans. [P41992-1]
DR   CTD; 175998; -.
DR   WormBase; B0280.1a; CE24762; WBGene00015099; ggtb-1. [P41992-1]
DR   WormBase; B0280.1b; CE00735; WBGene00015099; ggtb-1. [P41992-2]
DR   eggNOG; KOG0366; Eukaryota.
DR   GeneTree; ENSGT00950000183128; -.
DR   HOGENOM; CLU_028946_3_0_1; -.
DR   InParanoid; P41992; -.
DR   OMA; VKRCQCP; -.
DR   OrthoDB; 1042804at2759; -.
DR   PhylomeDB; P41992; -.
DR   Reactome; R-CEL-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR   Reactome; R-CEL-8873719; RAB geranylgeranylation.
DR   PRO; PR:P41992; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00015099; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0004663; F:Rab geranylgeranyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR   GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR   CDD; cd02894; GGTase-II; 1.
DR   InterPro; IPR001330; PFTB_repeat.
DR   InterPro; IPR045089; PGGT1B-like.
DR   InterPro; IPR026873; Ptb1.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11774; PTHR11774; 1.
DR   Pfam; PF00432; Prenyltrans; 5.
DR   SUPFAM; SSF48239; SSF48239; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Metal-binding; Prenyltransferase; Reference proteome;
KW   Repeat; Transferase; Zinc.
FT   CHAIN           1..335
FT                   /note="Probable geranylgeranyl transferase type-2 subunit
FT                   beta"
FT                   /id="PRO_0000119766"
FT   REPEAT          74..115
FT                   /note="PFTB 1"
FT   REPEAT          122..163
FT                   /note="PFTB 2"
FT   REPEAT          170..211
FT                   /note="PFTB 3"
FT   REPEAT          218..259
FT                   /note="PFTB 4"
FT   REPEAT          266..312
FT                   /note="PFTB 5"
FT   BINDING         196..198
FT                   /ligand="geranylgeranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57533"
FT                   /evidence="ECO:0000250"
FT   BINDING         238..250
FT                   /ligand="geranylgeranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57533"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         292..335
FT                   /note="ADPFHTVFGIAALSLFGDDTLESVDPIFCMTKRCLGDKQVEMYY -> VSFL
FT                   NNIQKFIFVLQSNNVLATTKQLFECSFNNS (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018160"
SQ   SEQUENCE   335 AA;  37226 MW;  F54AB54E58F9A67E CRC64;
     MSFAGLLDFA RKDVDLPQNS PNELLKDLHA NFINQYEKNK NSYHYIMAEH LRVSGIYWCV
     NAMDLSKQLE RMSTEEIVNY VLGCRNTDGG YGPAPGHDSH LLHTLCAVQT LIIFNSIEKA
     DADTISEYVK GLQQEDGSFC GDLSGEVDTR FTLCSLATCH LLGRLSTLNI DSAVRFLMRC
     YNTDGGFGTR PGSESHSGQI YCCVGALAIA GRLDEIDRDR TAEWLAFRQC DSGGLNGRPE
     KLPDVCYSWW VLASLAILGR LNFIDSDAMK KFIYACQDDE TGGFADRPGD CADPFHTVFG
     IAALSLFGDD TLESVDPIFC MTKRCLGDKQ VEMYY
 
 
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